The Central Role of the F-Actin Surface in Myosin Force Generation

Actin is one of the most abundant and versatile proteins in eukaryotic cells. As discussed in many contributions to this Special Issue, its transition from a monomeric G-actin to a filamentous F-actin form plays a critical role in a variety of cellular processes, including control of cell shape and...

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Published inBiology (Basel, Switzerland) Vol. 10; no. 12; p. 1221
Main Authors Doran, Matthew H, Lehman, William
Format Journal Article
LanguageEnglish
Published Switzerland MDPI AG 23.11.2021
MDPI
Subjects
Actin
actin-binding proteins
Adenosine triphosphatase
Amino acids
Binding sites
Cell size
Electron microscopy
Enzymes
Filaments
force production
Hydrolysis
Isoforms
Kinases
molecular motor
Motor activity
Myosin
Myosin ATPase
Polymerization
Proteins
Review
Somatic cells
tropomyosin
myosin
actin
tropomyosin
force production
actin-binding proteins
molecular motor
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Abstract Actin is one of the most abundant and versatile proteins in eukaryotic cells. As discussed in many contributions to this Special Issue, its transition from a monomeric G-actin to a filamentous F-actin form plays a critical role in a variety of cellular processes, including control of cell shape and cell motility. Once polymerized from G-actin, F-actin forms the central core of muscle-thin filaments and acts as molecular tracks for myosin-based motor activity. The ATP-dependent cross-bridge cycle of myosin attachment and detachment drives the sliding of myosin thick filaments past thin filaments in muscle and the translocation of cargo in somatic cells. The variation in actin function is dependent on the variation in muscle and non-muscle myosin isoform behavior as well as interactions with a plethora of additional actin-binding proteins. Extensive work has been devoted to defining the kinetics of actin-based force generation powered by the ATPase activity of myosin. In addition, over the past decade, cryo-electron microscopy has revealed the atomic-evel details of the binding of myosin isoforms on the F-actin surface. Most accounts of the structural interactions between myosin and actin are described from the perspective of the myosin molecule. Here, we discuss myosin-binding to actin as viewed from the actin surface. We then describe conserved structural features of actin required for the binding of all or most myosin isoforms while also noting specific interactions unique to myosin isoforms.
AbstractList Actin is one of the most abundant and versatile proteins in eukaryotic cells. As discussed in many contributions to this Special Issue, its transition from a monomeric G-actin to a filamentous F-actin form plays a critical role in a variety of cellular processes, including control of cell shape and cell motility. Once polymerized from G-actin, F-actin forms the central core of muscle-thin filaments and acts as molecular tracks for myosin-based motor activity. The ATP-dependent cross-bridge cycle of myosin attachment and detachment drives the sliding of myosin thick filaments past thin filaments in muscle and the translocation of cargo in somatic cells. The variation in actin function is dependent on the variation in muscle and non-muscle myosin isoform behavior as well as interactions with a plethora of additional actin-binding proteins. Extensive work has been devoted to defining the kinetics of actin-based force generation powered by the ATPase activity of myosin. In addition, over the past decade, cryo-electron microscopy has revealed the atomic-evel details of the binding of myosin isoforms on the F-actin surface. Most accounts of the structural interactions between myosin and actin are described from the perspective of the myosin molecule. Here, we discuss myosin-binding to actin as viewed from the actin surface. We then describe conserved structural features of actin required for the binding of all or most myosin isoforms while also noting specific interactions unique to myosin isoforms.
Simple SummaryAlthough actin is a highly conserved protein, it is involved in many diverse cellular processes. Actin owes its diversity of function to its ability to bind to a host of actin-binding proteins (ABPs) that localize across its surface. Among the most studied ABPs is the molecular motor, myosin. Myosin generates force on actin filaments by pairing ATP hydrolysis, product release, and actin-binding to the conformational changes that lead to movement. Central to this process is the progression of myosin binding to the actin surface as it moves through its ATPase cycle. During binding, actin acts as a myosin ATPase activator, catalyzing essential hydrolysis release steps. Here, we use the current model of actin-myosin binding as a roadmap to describe the portions of the actin-myosin interface that are sequentially formed throughout the motor cycle. At each step, we compare the interactions of a diverse set of high-resolution actin-myosin cryo-electron microscopy structures to define what portions of the interface are conserved and which are isoform-specific.AbstractActin is one of the most abundant and versatile proteins in eukaryotic cells. As discussed in many contributions to this Special Issue, its transition from a monomeric G-actin to a filamentous F-actin form plays a critical role in a variety of cellular processes, including control of cell shape and cell motility. Once polymerized from G-actin, F-actin forms the central core of muscle-thin filaments and acts as molecular tracks for myosin-based motor activity. The ATP-dependent cross-bridge cycle of myosin attachment and detachment drives the sliding of myosin thick filaments past thin filaments in muscle and the translocation of cargo in somatic cells. The variation in actin function is dependent on the variation in muscle and non-muscle myosin isoform behavior as well as interactions with a plethora of additional actin-binding proteins. Extensive work has been devoted to defining the kinetics of actin-based force generation powered by the ATPase activity of myosin. In addition, over the past decade, cryo-electron microscopy has revealed the atomic-evel details of the binding of myosin isoforms on the F-actin surface. Most accounts of the structural interactions between myosin and actin are described from the perspective of the myosin molecule. Here, we discuss myosin-binding to actin as viewed from the actin surface. We then describe conserved structural features of actin required for the binding of all or most myosin isoforms while also noting specific interactions unique to myosin isoforms.
Actin is one of the most abundant and versatile proteins in eukaryotic cells. As discussed in many contributions to this Special Issue, its transition from a monomeric G-actin to a filamentous F-actin form plays a critical role in a variety of cellular processes, including control of cell shape and cell motility. Once polymerized from G-actin, F-actin forms the central core of muscle-thin filaments and acts as molecular tracks for myosin-based motor activity. The ATP-dependent cross-bridge cycle of myosin attachment and detachment drives the sliding of myosin thick filaments past thin filaments in muscle and the translocation of cargo in somatic cells. The variation in actin function is dependent on the variation in muscle and non-muscle myosin isoform behavior as well as interactions with a plethora of additional actin-binding proteins. Extensive work has been devoted to defining the kinetics of actin-based force generation powered by the ATPase activity of myosin. In addition, over the past decade, cryo-electron microscopy has revealed the atomic-evel details of the binding of myosin isoforms on the F-actin surface. Most accounts of the structural interactions between myosin and actin are described from the perspective of the myosin molecule. Here, we discuss myosin-binding to actin as viewed from the actin surface. We then describe conserved structural features of actin required for the binding of all or most myosin isoforms while also noting specific interactions unique to myosin isoforms.Actin is one of the most abundant and versatile proteins in eukaryotic cells. As discussed in many contributions to this Special Issue, its transition from a monomeric G-actin to a filamentous F-actin form plays a critical role in a variety of cellular processes, including control of cell shape and cell motility. Once polymerized from G-actin, F-actin forms the central core of muscle-thin filaments and acts as molecular tracks for myosin-based motor activity. The ATP-dependent cross-bridge cycle of myosin attachment and detachment drives the sliding of myosin thick filaments past thin filaments in muscle and the translocation of cargo in somatic cells. The variation in actin function is dependent on the variation in muscle and non-muscle myosin isoform behavior as well as interactions with a plethora of additional actin-binding proteins. Extensive work has been devoted to defining the kinetics of actin-based force generation powered by the ATPase activity of myosin. In addition, over the past decade, cryo-electron microscopy has revealed the atomic-evel details of the binding of myosin isoforms on the F-actin surface. Most accounts of the structural interactions between myosin and actin are described from the perspective of the myosin molecule. Here, we discuss myosin-binding to actin as viewed from the actin surface. We then describe conserved structural features of actin required for the binding of all or most myosin isoforms while also noting specific interactions unique to myosin isoforms.
Author Doran, Matthew H
Lehman, William
AuthorAffiliation Department of Physiology & Biophysics, Boston University School of Medicine, Boston, MA 02118, USA
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  surname: Lehman
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  organization: Department of Physiology & Biophysics, Boston University School of Medicine, Boston, MA 02118, USA
BackLink https://www.ncbi.nlm.nih.gov/pubmed/34943138$$D View this record in MEDLINE/PubMed
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Cites_doi 10.1152/physrev.00001.2007
10.1146/annurev-cellbio-100809-151502
10.15252/embj.2019104006
10.1073/pnas.93.9.4459
10.1023/A:1024415409406
10.1016/S0969-2126(96)00103-7
10.1016/j.str.2010.05.009
10.1007/s10974-019-09501-5
10.1038/s41467-017-01367-w
10.1002/1873-3468.13486
10.1091/mbc.e06-05-0449
10.1101/cshperspect.a021931
10.1007/978-0-387-85766-4_3
10.1093/gbe/evu013
10.1016/S0022-2836(63)80081-9
10.1056/NEJM200012073432304
10.1073/pnas.93.1.21
10.1074/jbc.M001966200
10.1101/cshperspect.a021972
10.1038/nrm3609
10.1073/pnas.1517566112
10.1038/348217a0
10.1074/jbc.M006930200
10.1038/ncb3390
10.1161/01.CIR.0000066323.15244.54
10.1016/j.tibs.2004.09.004
10.1038/347037a0
10.1016/j.tibs.2016.09.006
10.1016/j.str.2018.08.007
10.1002/(SICI)1097-0029(19991015)47:2<93::AID-JEMT2>3.0.CO;2-P
10.1038/nature01927
10.1073/pnas.1516598113
10.1371/journal.pone.0084874
10.1038/ng1775
10.1073/pnas.1222257110
10.1021/bi701554a
10.1073/pnas.1718316115
10.1016/j.devcel.2015.03.025
10.1021/bi9826815
10.1242/jcs.094300
10.1016/j.jsb.2017.10.003
10.1074/jbc.M114.606665
10.1038/ncomms9314
10.1371/journal.pone.0070636
10.3389/fcell.2020.00342
10.1038/nature07685
10.1074/jbc.M808338200
10.1038/nature14033
10.1242/jcs.165563
10.1021/bi602439f
10.1073/pnas.0408784102
10.1016/j.bpj.2018.08.017
10.1038/gim.2016.90
10.1091/mbc.e06-08-0771
10.1042/BST0391115
10.1038/s41413-020-0095-2
10.1136/heart.89.10.1179
10.1016/j.jmb.2007.01.071
10.1016/0092-8674(90)90274-I
10.1073/pnas.1807028115
10.1038/s41467-021-22093-4
10.7554/eLife.31125
10.3389/fnsyn.2018.00010
10.1126/science.164.3886.1356
10.1038/nature18295
10.1038/347044a0
10.1016/j.bpj.2010.12.3697
10.1021/acs.chemrev.9b00264
10.1016/S0014-5793(98)00751-0
10.1006/jmcc.2000.1287
10.1016/0022-2836(70)90192-0
10.1111/asj.13226
10.1021/bi000985x
10.1242/jeb.125930
10.1126/science.8316857
10.1038/ncomms13969
10.1016/j.cub.2016.11.033
10.1016/j.ceb.2007.11.006
10.1016/j.bpj.2012.08.066
10.1126/science.8316858
10.1126/science.1175862
10.1038/s41467-017-02357-8
10.1007/164_2016_29
10.1016/j.jmb.2021.167178
10.1016/j.ceb.2006.04.009
10.1038/s41594-018-0128-3
10.1073/pnas.94.1.91
10.1172/JCI116900
10.1038/s41467-017-00176-5
10.1016/j.cub.2005.04.008
10.1038/nsmb.2216
10.1101/cshperspect.a018226
10.1111/tra.12388
10.1038/368065a0
10.1146/annurev.bi.55.070186.005011
10.1002/bip.22853
10.1016/j.cell.2012.05.037
10.1146/annurev-biophys-042910-155359
10.1371/journal.pcbi.1002995
10.1146/annurev.biochem.68.1.687
10.1080/19490992.2015.1054092
10.1016/j.tibs.2018.11.010
10.1016/j.bpj.2020.07.006
10.1016/B978-0-12-386043-9.00005-0
10.1016/S0969-2126(98)00141-5
10.1016/j.str.2020.09.013
10.1186/s12862-017-1056-2
10.7554/eLife.62514
10.1007/s12013-009-9047-6
10.1016/j.abb.2013.09.011
10.1073/pnas.0601595103
10.2210/pdb7ad9/pdb
10.1021/bi991595h
10.1038/s41594-018-0074-0
10.1083/jcb.200105079
10.1021/bi035510v
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Issue 12
Keywords myosin
actin
tropomyosin
force production
actin-binding proteins
molecular motor
Language English
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References Huxley (ref_53) 1969; 164
Gunning (ref_1) 2015; 128
Dominguez (ref_2) 2011; 40
Richard (ref_71) 2003; 107
Lehman (ref_22) 2015; 519
Yang (ref_104) 2015; 290
Oda (ref_19) 2010; 18
Trivedi (ref_76) 2015; 112
ref_95
Milligan (ref_101) 1990; 348
Cope (ref_114) 1996; 4
Hartman (ref_16) 2011; 27
Mierke (ref_40) 2009; 53
Heissler (ref_59) 2016; 17
Lehman (ref_47) 2018; 115
Lehman (ref_23) 2019; 41
Schwebach (ref_36) 2020; 8
Woo (ref_108) 2003; 89
Grintsevich (ref_57) 2017; 8
ref_29
Murphy (ref_92) 1999; 38
Geeves (ref_3) 1999; 68
Mei (ref_43) 2020; 9
Yengo (ref_96) 2004; 43
Pollard (ref_5) 2009; 326
Dominguez (ref_9) 2004; 29
Peng (ref_41) 2011; 287
Moore (ref_21) 1970; 50
Pollard (ref_8) 2016; 8
Coureux (ref_106) 2003; 425
Walsh (ref_109) 2017; 19
Sasaki (ref_99) 2002; 23
Stradal (ref_32) 1998; 431
Varland (ref_55) 2019; 44
Uyeda (ref_61) 1996; 93
Banerjee (ref_86) 2017; 200
Milligan (ref_102) 1996; 93
Ojima (ref_66) 2019; 90
Lehman (ref_48) 2014; 552–553
Sweeney (ref_14) 2018; 10
Hokanson (ref_64) 2006; 17
Risi (ref_44) 2018; 26
Bond (ref_17) 2011; 39
Holmes (ref_26) 1990; 347
Onishi (ref_91) 2006; 103
Kass (ref_73) 1990; 62
Rayment (ref_98) 1993; 261
Struchholz (ref_94) 2009; 284
Gunning (ref_113) 2017; 27
Li (ref_49) 2011; 100
Pylypenko (ref_97) 2020; 120
Richards (ref_116) 2014; 6
Lehman (ref_54) 1994; 368
Heissler (ref_67) 2015; 4
Muretta (ref_79) 2013; 110
Hartman (ref_82) 2017; 8
Fujii (ref_74) 2017; 8
DePina (ref_13) 1999; 47
Xu (ref_88) 2021; 12
Gurel (ref_85) 2017; 6
Rayment (ref_63) 1993; 261
Yang (ref_105) 2012; 19
Masters (ref_60) 2017; 235
Marx (ref_69) 2001; 33
Chou (ref_28) 2019; 116
Kumari (ref_33) 2020; 39
Hampton (ref_37) 2007; 368
Gunning (ref_51) 2008; 88
Toydemir (ref_72) 2006; 38
Dausse (ref_68) 1993; 92
Kabsch (ref_25) 1990; 347
Gyimesi (ref_110) 2008; 47
Dash (ref_111) 2007; 46
Hanson (ref_52) 1963; 6
Hatch (ref_46) 2001; 154
Furch (ref_103) 1999; 38
Mentes (ref_80) 2018; 115
Gooding (ref_50) 2008; 644
Boczkowska (ref_39) 2015; 6
Risi (ref_45) 2021; 433
Ross (ref_18) 2008; 20
Sata (ref_62) 1997; 94
Batters (ref_65) 2019; 593
ref_115
ref_117
Grintsevich (ref_56) 2016; 18
Iwamoto (ref_35) 2018; 25
Doran (ref_83) 2020; 119
Uhlenbrock (ref_93) 2007; 18
Gunning (ref_112) 2015; 128
Merino (ref_27) 2018; 25
Singh (ref_38) 2012; 103
Behrmann (ref_87) 2012; 150
Miralles (ref_4) 2006; 18
Heissler (ref_24) 2016; 534
Houdusse (ref_58) 2016; 41
Geeves (ref_78) 2016; 105
Kamisago (ref_70) 2000; 343
Titus (ref_6) 2018; 10
Saraste (ref_30) 1998; 6
Risi (ref_84) 2021; 29
Unsain (ref_11) 2018; 10
ref_42
Llinas (ref_77) 2015; 33
Avery (ref_34) 2017; 8
Magalhaes (ref_10) 2013; 14
Yin (ref_31) 2020; 8
Joel (ref_90) 2001; 276
Burgess (ref_12) 2005; 15
Sasaki (ref_107) 2000; 275
Oda (ref_20) 2009; 457
Furch (ref_89) 2000; 39
Wulf (ref_75) 2016; 113
Fischer (ref_81) 2005; 102
Spudich (ref_100) 2016; 219
Pollard (ref_7) 1986; 55
Hartman (ref_15) 2012; 125
References_xml – volume: 88
  start-page: 1
  year: 2008
  ident: ref_51
  article-title: Tropomyosin-based regulation of the actin cytoskeleton in time and space
  publication-title: Physiol. Rev.
  doi: 10.1152/physrev.00001.2007
  contributor:
    fullname: Gunning
– volume: 27
  start-page: 133
  year: 2011
  ident: ref_16
  article-title: Principles of unconventional myosin function and targeting
  publication-title: Annu. Rev. Cell Dev. Biol.
  doi: 10.1146/annurev-cellbio-100809-151502
  contributor:
    fullname: Hartman
– volume: 39
  start-page: e104006
  year: 2020
  ident: ref_33
  article-title: Structural insights into actin filament recognition by commonly used cellular actin markers
  publication-title: EMBO J.
  doi: 10.15252/embj.2019104006
  contributor:
    fullname: Kumari
– volume: 93
  start-page: 4459
  year: 1996
  ident: ref_61
  article-title: The neck region of the myosin motor domain acts as a lever arm to generate movement
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.93.9.4459
  contributor:
    fullname: Uyeda
– volume: 23
  start-page: 697
  year: 2002
  ident: ref_99
  article-title: Dictyostelium myosin II as a model to study the actin-myosin interactions during force generation
  publication-title: J. Muscle Res. Cell Motil.
  doi: 10.1023/A:1024415409406
  contributor:
    fullname: Sasaki
– volume: 4
  start-page: 969
  year: 1996
  ident: ref_114
  article-title: Conservation within the myosin motor domain: Implications for structure and function
  publication-title: Structure
  doi: 10.1016/S0969-2126(96)00103-7
  contributor:
    fullname: Cope
– volume: 18
  start-page: 761
  year: 2010
  ident: ref_19
  article-title: Multiple Conformations of F-actin
  publication-title: Structure
  doi: 10.1016/j.str.2010.05.009
  contributor:
    fullname: Oda
– volume: 41
  start-page: 23
  year: 2019
  ident: ref_23
  article-title: A new twist on tropomyosin binding to actin filaments: Perspectives on thin filament function, assembly and biomechanics
  publication-title: J. Muscle Res. Cell Motil.
  doi: 10.1007/s10974-019-09501-5
  contributor:
    fullname: Lehman
– volume: 8
  start-page: 1350
  year: 2017
  ident: ref_34
  article-title: Structural basis for high-affinity actin binding revealed by a β-III-spectrin SCA5 missense mutation
  publication-title: Nat. Commun.
  doi: 10.1038/s41467-017-01367-w
  contributor:
    fullname: Avery
– volume: 593
  start-page: 1494
  year: 2019
  ident: ref_65
  article-title: The MYO6 interactome: Selective motor-cargo complexes for diverse cellular processes
  publication-title: FEBS Lett.
  doi: 10.1002/1873-3468.13486
  contributor:
    fullname: Batters
– volume: 17
  start-page: 4856
  year: 2006
  ident: ref_64
  article-title: Myo1c binds phosphoinositides through a putative pleckstrin homology domain
  publication-title: Mol. Biol. Cell
  doi: 10.1091/mbc.e06-05-0449
  contributor:
    fullname: Hokanson
– volume: 10
  start-page: a021931
  year: 2018
  ident: ref_14
  article-title: Motor Proteins
  publication-title: Cold Spring Harb. Perspect. Biol.
  doi: 10.1101/cshperspect.a021931
  contributor:
    fullname: Sweeney
– volume: 644
  start-page: 27
  year: 2008
  ident: ref_50
  article-title: Tropomyosin exons as models for alternative splicing
  publication-title: Adv. Exp. Med. Biol.
  doi: 10.1007/978-0-387-85766-4_3
  contributor:
    fullname: Gooding
– volume: 128
  start-page: 2965
  year: 2015
  ident: ref_112
  article-title: Tropomyosin—Master regulator of actin filament function in the cytoskeleton
  publication-title: J. Cell Sci.
  contributor:
    fullname: Gunning
– volume: 6
  start-page: 290
  year: 2014
  ident: ref_116
  article-title: Evolution and classification of myosins, a paneukaryotic whole-genome approach
  publication-title: Genome Biol. Evol.
  doi: 10.1093/gbe/evu013
  contributor:
    fullname: Richards
– volume: 6
  start-page: 46-IN5
  year: 1963
  ident: ref_52
  article-title: The structure of F-actin and of actin filaments isolated from muscle
  publication-title: J. Mol. Biol.
  doi: 10.1016/S0022-2836(63)80081-9
  contributor:
    fullname: Hanson
– volume: 343
  start-page: 1688
  year: 2000
  ident: ref_70
  article-title: Mutations in sarcomere protein genes as a cause of dilated cardiomyopathy
  publication-title: N. Engl. J. Med.
  doi: 10.1056/NEJM200012073432304
  contributor:
    fullname: Kamisago
– volume: 93
  start-page: 21
  year: 1996
  ident: ref_102
  article-title: Protein-protein interactions in the rigor actomyosin complex
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.93.1.21
  contributor:
    fullname: Milligan
– volume: 275
  start-page: 38705
  year: 2000
  ident: ref_107
  article-title: Insertion or Deletion of a Single Residue in the Strut Sequence of Dictyostelium Myosin II Abolishes Strong Binding to Actin *
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M001966200
  contributor:
    fullname: Sasaki
– volume: 10
  start-page: a021972
  year: 2018
  ident: ref_6
  article-title: Myosin-Driven Intracellular Transport
  publication-title: Cold Spring Harb. Perspect. Biol.
  doi: 10.1101/cshperspect.a021972
  contributor:
    fullname: Titus
– volume: 14
  start-page: 405
  year: 2013
  ident: ref_10
  article-title: Functions of cofilin in cell locomotion and invasion
  publication-title: Nat. Rev. Mol. Cell Biol.
  doi: 10.1038/nrm3609
  contributor:
    fullname: Magalhaes
– volume: 112
  start-page: 14593
  year: 2015
  ident: ref_76
  article-title: Direct measurements of the coordination of lever arm swing and the catalytic cycle in myosin V
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.1517566112
  contributor:
    fullname: Trivedi
– volume: 348
  start-page: 217
  year: 1990
  ident: ref_101
  article-title: Molecular structure of F-actin and location of surface binding sites
  publication-title: Nature
  doi: 10.1038/348217a0
  contributor:
    fullname: Milligan
– volume: 276
  start-page: 2998
  year: 2001
  ident: ref_90
  article-title: Two conserved lysines at the 50/20-kDa junction of myosin are necessary for triggering actin activation
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M006930200
  contributor:
    fullname: Joel
– volume: 18
  start-page: 876
  year: 2016
  ident: ref_56
  article-title: F-actin dismantling through a redox-driven synergy between Mical and cofilin
  publication-title: Nat. Cell Biol.
  doi: 10.1038/ncb3390
  contributor:
    fullname: Grintsevich
– volume: 107
  start-page: 2227
  year: 2003
  ident: ref_71
  article-title: Hypertrophic Cardiomyopathy
  publication-title: Circulation
  doi: 10.1161/01.CIR.0000066323.15244.54
  contributor:
    fullname: Richard
– volume: 29
  start-page: 572
  year: 2004
  ident: ref_9
  article-title: Actin-binding proteins— A unifying hypothesis
  publication-title: Trends Biochem. Sci.
  doi: 10.1016/j.tibs.2004.09.004
  contributor:
    fullname: Dominguez
– volume: 347
  start-page: 37
  year: 1990
  ident: ref_25
  article-title: Atomic structure of the actin: DNase I complex
  publication-title: Nature
  doi: 10.1038/347037a0
  contributor:
    fullname: Kabsch
– volume: 41
  start-page: 989
  year: 2016
  ident: ref_58
  article-title: How myosin generates force on actin filaments
  publication-title: Trends Biochem. Sci.
  doi: 10.1016/j.tibs.2016.09.006
  contributor:
    fullname: Houdusse
– volume: 26
  start-page: 1604
  year: 2018
  ident: ref_44
  article-title: N-Terminal Domains of Cardiac Myosin Binding Protein C Cooperatively Activate the Thin Filament
  publication-title: Structure
  doi: 10.1016/j.str.2018.08.007
  contributor:
    fullname: Risi
– volume: 47
  start-page: 93
  year: 1999
  ident: ref_13
  article-title: Vesicle transport: The role of actin filaments and myosin motors
  publication-title: Microsc. Res. Tech.
  doi: 10.1002/(SICI)1097-0029(19991015)47:2<93::AID-JEMT2>3.0.CO;2-P
  contributor:
    fullname: DePina
– volume: 425
  start-page: 419
  year: 2003
  ident: ref_106
  article-title: A structural state of the myosin V motor without bound nucleotide
  publication-title: Nature
  doi: 10.1038/nature01927
  contributor:
    fullname: Coureux
– volume: 113
  start-page: E1844
  year: 2016
  ident: ref_75
  article-title: Force-producing ADP state of myosin bound to actin
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.1516598113
  contributor:
    fullname: Wulf
– ident: ref_95
  doi: 10.1371/journal.pone.0084874
– volume: 38
  start-page: 561
  year: 2006
  ident: ref_72
  article-title: Mutations in embryonic myosin heavy chain (MYH3) cause Freeman-Sheldon syndrome and Sheldon-Hall syndrome
  publication-title: Nat. Genet.
  doi: 10.1038/ng1775
  contributor:
    fullname: Toydemir
– volume: 110
  start-page: 7211
  year: 2013
  ident: ref_79
  article-title: Direct real-time detection of the actin-activated power stroke within the myosin catalytic domain
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.1222257110
  contributor:
    fullname: Muretta
– volume: 47
  start-page: 283
  year: 2008
  ident: ref_110
  article-title: Kinetic characterization of the function of myosin loop 4 in the actin-myosin interaction
  publication-title: Biochemistry
  doi: 10.1021/bi701554a
  contributor:
    fullname: Gyimesi
– volume: 115
  start-page: 1292
  year: 2018
  ident: ref_80
  article-title: High-resolution cryo-EM structures of actin-bound myosin states reveal the mechanism of myosin force sensing
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.1718316115
  contributor:
    fullname: Mentes
– volume: 33
  start-page: 401
  year: 2015
  ident: ref_77
  article-title: How Actin Initiates the Motor Activity of Myosin
  publication-title: Dev. Cell
  doi: 10.1016/j.devcel.2015.03.025
  contributor:
    fullname: Llinas
– volume: 38
  start-page: 3785
  year: 1999
  ident: ref_92
  article-title: The sequence of the myosin 50–20 K loop affects Myosin’s affinity for actin throughout the actin-myosin ATPase cycle and its maximum ATPase activity
  publication-title: Biochemistry
  doi: 10.1021/bi9826815
  contributor:
    fullname: Murphy
– volume: 125
  start-page: 1627
  year: 2012
  ident: ref_15
  article-title: The myosin superfamily at a glance
  publication-title: J. Cell Sci.
  doi: 10.1242/jcs.094300
  contributor:
    fullname: Hartman
– volume: 200
  start-page: 325
  year: 2017
  ident: ref_86
  article-title: The structure of the actin-smooth muscle myosin motor domain complex in the rigor state
  publication-title: J. Struct. Biol.
  doi: 10.1016/j.jsb.2017.10.003
  contributor:
    fullname: Banerjee
– volume: 290
  start-page: 1679
  year: 2015
  ident: ref_104
  article-title: Structural model of weak binding actomyosin in the prepowerstroke state
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M114.606665
  contributor:
    fullname: Yang
– volume: 6
  start-page: 8314
  year: 2015
  ident: ref_39
  article-title: How Leiomodin and Tropomodulin use a common fold for different actin assembly functions
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms9314
  contributor:
    fullname: Boczkowska
– ident: ref_117
  doi: 10.1371/journal.pone.0070636
– volume: 8
  start-page: 342
  year: 2020
  ident: ref_31
  article-title: Structural Characteristics, Binding Partners and Related Diseases of the Calponin Homology (CH) Domain
  publication-title: Front. Cell Dev. Biol.
  doi: 10.3389/fcell.2020.00342
  contributor:
    fullname: Yin
– volume: 457
  start-page: 441
  year: 2009
  ident: ref_20
  article-title: The nature of the globular- to fibrous-actin transition
  publication-title: Nature
  doi: 10.1038/nature07685
  contributor:
    fullname: Oda
– volume: 284
  start-page: 3663
  year: 2009
  ident: ref_94
  article-title: Functional Role of the Extended Loop 2 in the Myosin 9b Head for Binding F-actin *
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M808338200
  contributor:
    fullname: Struchholz
– volume: 519
  start-page: 114
  year: 2015
  ident: ref_22
  article-title: Structure of the F-actin-tropomyosin complex
  publication-title: Nature
  doi: 10.1038/nature14033
  contributor:
    fullname: Lehman
– volume: 128
  start-page: 2009
  year: 2015
  ident: ref_1
  article-title: The evolution of compositionally and functionally distinct actin filaments
  publication-title: J. Cell Sci.
  doi: 10.1242/jcs.165563
  contributor:
    fullname: Gunning
– volume: 46
  start-page: 2779
  year: 2007
  ident: ref_111
  article-title: Myosin surface loop 4 modulates inhibition of actomyosin 1b ATPase activity by tropomyosin
  publication-title: Biochemistry
  doi: 10.1021/bi602439f
  contributor:
    fullname: Dash
– volume: 102
  start-page: 6873
  year: 2005
  ident: ref_81
  article-title: Structural mechanism of the recovery stroke in the myosin molecular motor
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.0408784102
  contributor:
    fullname: Fischer
– volume: 115
  start-page: 1082
  year: 2018
  ident: ref_47
  article-title: Precise Binding of Tropomyosin on Actin Involves Sequence-Dependent Variance in Coiled-Coil Twisting
  publication-title: Biophys. J.
  doi: 10.1016/j.bpj.2018.08.017
  contributor:
    fullname: Lehman
– volume: 19
  start-page: 192
  year: 2017
  ident: ref_109
  article-title: Reassessment of Mendelian gene pathogenicity using 7,855 cardiomyopathy cases and 60,706 reference samples
  publication-title: Genet. Med.
  doi: 10.1038/gim.2016.90
  contributor:
    fullname: Walsh
– volume: 18
  start-page: 1507
  year: 2007
  ident: ref_93
  article-title: The Myosin IXb Motor Activity Targets the Myosin IXb RhoGAP Domain as Cargo to Sites of Actin Polymerization
  publication-title: Mol. Biol. Cell
  doi: 10.1091/mbc.e06-08-0771
  contributor:
    fullname: Uhlenbrock
– volume: 39
  start-page: 1115
  year: 2011
  ident: ref_17
  article-title: Myosin motor proteins are involved in the final stages of the secretory pathways
  publication-title: Biochem. Soc. Trans.
  doi: 10.1042/BST0391115
  contributor:
    fullname: Bond
– volume: 8
  start-page: 21
  year: 2020
  ident: ref_36
  article-title: Osteogenesis imperfecta mutations in plastin 3 lead to impaired calcium regulation of actin bundling
  publication-title: Bone Res.
  doi: 10.1038/s41413-020-0095-2
  contributor:
    fullname: Schwebach
– volume: 89
  start-page: 1179
  year: 2003
  ident: ref_108
  article-title: Mutations of the β myosin heavy chain gene in hypertrophic cardiomyopathy: Critical functional sites determine prognosis
  publication-title: Heart
  doi: 10.1136/heart.89.10.1179
  contributor:
    fullname: Woo
– volume: 368
  start-page: 92
  year: 2007
  ident: ref_37
  article-title: Novel structures for α-actinin: F-actin interactions and their implications for actin-membrane attachment and tension sensing in the cytoskeleton
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2007.01.071
  contributor:
    fullname: Hampton
– volume: 62
  start-page: 999
  year: 1990
  ident: ref_73
  article-title: A molecular basis for familial hypertrophic cardiomyopathy: A beta cardiac myosin heavy chain gene missense mutation
  publication-title: Cell
  doi: 10.1016/0092-8674(90)90274-I
  contributor:
    fullname: Kass
– volume: 116
  start-page: 4265
  year: 2019
  ident: ref_28
  article-title: Mechanism of actin polymerization revealed by cryo-EM structures of actin filaments with three different bound nucleotides
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.1807028115
  contributor:
    fullname: Chou
– volume: 12
  start-page: 1892
  year: 2021
  ident: ref_88
  article-title: The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity
  publication-title: Nat. Commun.
  doi: 10.1038/s41467-021-22093-4
  contributor:
    fullname: Xu
– volume: 6
  start-page: e31125
  year: 2017
  ident: ref_85
  article-title: Cryo-EM structures reveal specialization at the myosin VI-actin interface and a mechanism of force sensitivity
  publication-title: eLife
  doi: 10.7554/eLife.31125
  contributor:
    fullname: Gurel
– volume: 10
  start-page: 10
  year: 2018
  ident: ref_11
  article-title: The Actin/Spectrin Membrane-Associated Periodic Skeleton in Neurons
  publication-title: Front. Synaptic Neurosci.
  doi: 10.3389/fnsyn.2018.00010
  contributor:
    fullname: Unsain
– volume: 164
  start-page: 1356
  year: 1969
  ident: ref_53
  article-title: The Mechanism of Muscular Contraction
  publication-title: Science
  doi: 10.1126/science.164.3886.1356
  contributor:
    fullname: Huxley
– volume: 534
  start-page: 724
  year: 2016
  ident: ref_24
  article-title: Cryo-EM structure of a human cytoplasmic actomyosin complex at near-atomic resolution
  publication-title: Nature
  doi: 10.1038/nature18295
  contributor:
    fullname: Heissler
– volume: 347
  start-page: 44
  year: 1990
  ident: ref_26
  article-title: Atomic model of the actin filament
  publication-title: Nature
  doi: 10.1038/347044a0
  contributor:
    fullname: Holmes
– volume: 100
  start-page: 1005
  year: 2011
  ident: ref_49
  article-title: Tropomyosin position on F-actin revealed by EM reconstruction and computational chemistry
  publication-title: Biophys. J.
  doi: 10.1016/j.bpj.2010.12.3697
  contributor:
    fullname: Li
– volume: 120
  start-page: 5
  year: 2020
  ident: ref_97
  article-title: Force Generation by Myosin Motors: A Structural Perspective
  publication-title: Chem. Rev.
  doi: 10.1021/acs.chemrev.9b00264
  contributor:
    fullname: Pylypenko
– volume: 431
  start-page: 134
  year: 1998
  ident: ref_32
  article-title: CH domains revisited
  publication-title: FEBS Lett.
  doi: 10.1016/S0014-5793(98)00751-0
  contributor:
    fullname: Stradal
– volume: 33
  start-page: 141
  year: 2001
  ident: ref_69
  article-title: Beta-myosin heavy chain gene mutations and hypertrophic cardiomyopathy in Austrian children
  publication-title: J. Mol. Cell. Cardiol.
  doi: 10.1006/jmcc.2000.1287
  contributor:
    fullname: Marx
– volume: 50
  start-page: 279
  year: 1970
  ident: ref_21
  article-title: Three-dimensional reconstruction of F-actin, thin filaments and decorated thin filaments
  publication-title: J. Mol. Biol.
  doi: 10.1016/0022-2836(70)90192-0
  contributor:
    fullname: Moore
– volume: 90
  start-page: 801
  year: 2019
  ident: ref_66
  article-title: Myosin: Formation and maintenance of thick filaments
  publication-title: Anim. Sci. J.
  doi: 10.1111/asj.13226
  contributor:
    fullname: Ojima
– volume: 39
  start-page: 11602
  year: 2000
  ident: ref_89
  article-title: Stabilization of the Actomyosin Complex by Negative Charges on Myosin
  publication-title: Biochemistry
  doi: 10.1021/bi000985x
  contributor:
    fullname: Furch
– volume: 219
  start-page: 161
  year: 2016
  ident: ref_100
  article-title: Effects of hypertrophic and dilated cardiomyopathy mutations on power output by human β-cardiac myosin
  publication-title: J. Exp. Biol.
  doi: 10.1242/jeb.125930
  contributor:
    fullname: Spudich
– volume: 261
  start-page: 10
  year: 1993
  ident: ref_63
  article-title: Three-Dimensional Structure of Myosin Subfragment-1: A Molecular Motor
  publication-title: Science
  doi: 10.1126/science.8316857
  contributor:
    fullname: Rayment
– volume: 8
  start-page: 1
  year: 2017
  ident: ref_74
  article-title: Structure of actomyosin rigour complex at 5.2 Å resolution and insights into the ATPase cycle mechanism
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms13969
  contributor:
    fullname: Fujii
– volume: 27
  start-page: R8
  year: 2017
  ident: ref_113
  article-title: Tropomyosins
  publication-title: Curr. Biol.
  doi: 10.1016/j.cub.2016.11.033
  contributor:
    fullname: Gunning
– volume: 20
  start-page: 41
  year: 2008
  ident: ref_18
  article-title: Cargo transport: Molecular motors navigate a complex cytoskeleton
  publication-title: Curr. Opin. Cell Biol.
  doi: 10.1016/j.ceb.2007.11.006
  contributor:
    fullname: Ross
– volume: 103
  start-page: 1970
  year: 2012
  ident: ref_38
  article-title: The N-Terminal Actin-Binding Tandem Calponin-Homology (CH) Domain of Dystrophin Is in a Closed Conformation in Solution and When Bound to F-actin
  publication-title: Biophys. J.
  doi: 10.1016/j.bpj.2012.08.066
  contributor:
    fullname: Singh
– volume: 261
  start-page: 58
  year: 1993
  ident: ref_98
  article-title: Structure of the actin-myosin complex and its implications for muscle contraction
  publication-title: Science
  doi: 10.1126/science.8316858
  contributor:
    fullname: Rayment
– volume: 326
  start-page: 1208
  year: 2009
  ident: ref_5
  article-title: Actin, a Central Player in Cell Shape and Movement
  publication-title: Science
  doi: 10.1126/science.1175862
  contributor:
    fullname: Pollard
– volume: 8
  start-page: 2183
  year: 2017
  ident: ref_57
  article-title: Catastrophic disassembly of actin filaments via Mical-mediated oxidation
  publication-title: Nat. Commun.
  doi: 10.1038/s41467-017-02357-8
  contributor:
    fullname: Grintsevich
– volume: 235
  start-page: 77
  year: 2017
  ident: ref_60
  article-title: Myosins: Domain Organisation, Motor Properties, Physiological Roles and Cellular Functions
  publication-title: Handb. Exp. Pharmacol.
  doi: 10.1007/164_2016_29
  contributor:
    fullname: Masters
– volume: 433
  start-page: 167178
  year: 2021
  ident: ref_45
  article-title: Interaction of the C2 Ig-like Domain of Cardiac Myosin Binding Protein-C with F-actin
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2021.167178
  contributor:
    fullname: Risi
– volume: 18
  start-page: 261
  year: 2006
  ident: ref_4
  article-title: Actin in transcription and transcription regulation
  publication-title: Curr. Opin. Cell Biol.
  doi: 10.1016/j.ceb.2006.04.009
  contributor:
    fullname: Miralles
– volume: 25
  start-page: 918
  year: 2018
  ident: ref_35
  article-title: Structural basis of the filamin A actin-binding domain interaction with F-actin
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/s41594-018-0128-3
  contributor:
    fullname: Iwamoto
– volume: 94
  start-page: 91
  year: 1997
  ident: ref_62
  article-title: The motor domain and the regulatory domain of myosin solely dictate enzymatic activity and phosphorylation-dependent regulation, respectively
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.94.1.91
  contributor:
    fullname: Sata
– volume: 92
  start-page: 2807
  year: 1993
  ident: ref_68
  article-title: Familial hypertrophic cardiomyopathy. Microsatellite haplotyping and identification of a hot spot for mutations in the beta-myosin heavy chain gene
  publication-title: J. Clin. Investig.
  doi: 10.1172/JCI116900
  contributor:
    fullname: Dausse
– volume: 8
  start-page: 190
  year: 2017
  ident: ref_82
  article-title: Mechanistic and structural basis for activation of cardiac myosin force production by omecamtiv mecarbil
  publication-title: Nat. Commun.
  doi: 10.1038/s41467-017-00176-5
  contributor:
    fullname: Hartman
– volume: 15
  start-page: R310
  year: 2005
  ident: ref_12
  article-title: Cytokinesis: New roles for myosin
  publication-title: Curr. Biol. CB
  doi: 10.1016/j.cub.2005.04.008
  contributor:
    fullname: Burgess
– volume: 19
  start-page: 299
  year: 2012
  ident: ref_105
  article-title: A novel actin binding site of myosin required for effective muscle contraction
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.2216
  contributor:
    fullname: Yang
– volume: 8
  start-page: a018226
  year: 2016
  ident: ref_8
  article-title: Actin and Actin-Binding Proteins
  publication-title: Cold Spring Harb. Perspect. Biol.
  doi: 10.1101/cshperspect.a018226
  contributor:
    fullname: Pollard
– volume: 17
  start-page: 839
  year: 2016
  ident: ref_59
  article-title: Kinetic Adaptations of Myosins for Their Diverse Cellular Functions
  publication-title: Traffic
  doi: 10.1111/tra.12388
  contributor:
    fullname: Heissler
– volume: 368
  start-page: 65
  year: 1994
  ident: ref_54
  article-title: Ca(2+)-induced tropomyosin movement in Limulus thin filaments revealed by three-dimensional reconstruction
  publication-title: Nature
  doi: 10.1038/368065a0
  contributor:
    fullname: Lehman
– volume: 55
  start-page: 987
  year: 1986
  ident: ref_7
  article-title: Actin and actin-binding proteins. A critical evaluation of mechanisms and functions
  publication-title: Annu. Rev. Biochem.
  doi: 10.1146/annurev.bi.55.070186.005011
  contributor:
    fullname: Pollard
– volume: 105
  start-page: 483
  year: 2016
  ident: ref_78
  article-title: Review: The ATPase mechanism of myosin and actomyosin
  publication-title: Biopolymers
  doi: 10.1002/bip.22853
  contributor:
    fullname: Geeves
– volume: 150
  start-page: 327
  year: 2012
  ident: ref_87
  article-title: Structure of the Rigor Actin-Tropomyosin-Myosin Complex
  publication-title: Cell
  doi: 10.1016/j.cell.2012.05.037
  contributor:
    fullname: Behrmann
– volume: 40
  start-page: 169
  year: 2011
  ident: ref_2
  article-title: Actin Structure and Function
  publication-title: Annu. Rev. Biophys.
  doi: 10.1146/annurev-biophys-042910-155359
  contributor:
    fullname: Dominguez
– ident: ref_42
  doi: 10.1371/journal.pcbi.1002995
– volume: 68
  start-page: 687
  year: 1999
  ident: ref_3
  article-title: Structural mechanism of muscle contraction
  publication-title: Annu. Rev. Biochem.
  doi: 10.1146/annurev.biochem.68.1.687
  contributor:
    fullname: Geeves
– volume: 4
  start-page: 169
  year: 2015
  ident: ref_67
  article-title: Myosin light chains: Teaching old dogs new tricks
  publication-title: Bioarchitecture
  doi: 10.1080/19490992.2015.1054092
  contributor:
    fullname: Heissler
– volume: 44
  start-page: 502
  year: 2019
  ident: ref_55
  article-title: Actin Post-translational Modifications: The Cinderella of Cytoskeletal Control
  publication-title: Trends Biochem. Sci.
  doi: 10.1016/j.tibs.2018.11.010
  contributor:
    fullname: Varland
– volume: 119
  start-page: 821
  year: 2020
  ident: ref_83
  article-title: Cryo-EM and Molecular Docking Shows Myosin Loop 4 Contacts Actin and Tropomyosin on Thin Filaments
  publication-title: Biophys. J.
  doi: 10.1016/j.bpj.2020.07.006
  contributor:
    fullname: Doran
– volume: 287
  start-page: 191
  year: 2011
  ident: ref_41
  article-title: New Insights into Vinculin Function and Regulation
  publication-title: Int. Rev. Cell Mol. Biol.
  doi: 10.1016/B978-0-12-386043-9.00005-0
  contributor:
    fullname: Peng
– volume: 6
  start-page: 1419
  year: 1998
  ident: ref_30
  article-title: Structural comparisons of calponin homology domains: Implications for actin binding
  publication-title: Structure
  doi: 10.1016/S0969-2126(98)00141-5
  contributor:
    fullname: Saraste
– volume: 29
  start-page: 50
  year: 2021
  ident: ref_84
  article-title: High-Resolution Cryo-EM Structure of the Cardiac Actomyosin Complex
  publication-title: Structure
  doi: 10.1016/j.str.2020.09.013
  contributor:
    fullname: Risi
– ident: ref_115
  doi: 10.1186/s12862-017-1056-2
– volume: 9
  start-page: e62514
  year: 2020
  ident: ref_43
  article-title: Molecular mechanism for direct actin force-sensing by α-catenin
  publication-title: eLife
  doi: 10.7554/eLife.62514
  contributor:
    fullname: Mei
– volume: 53
  start-page: 115
  year: 2009
  ident: ref_40
  article-title: The role of vinculin in the regulation of the mechanical properties of cells
  publication-title: Cell Biochem. Biophys.
  doi: 10.1007/s12013-009-9047-6
  contributor:
    fullname: Mierke
– volume: 552–553
  start-page: 68
  year: 2014
  ident: ref_48
  article-title: The structural dynamics of α-tropomyosin on F-actin shape the overlap complex between adjacent tropomyosin molecules
  publication-title: Arch. Biochem. Biophys.
  doi: 10.1016/j.abb.2013.09.011
  contributor:
    fullname: Lehman
– volume: 103
  start-page: 6136
  year: 2006
  ident: ref_91
  article-title: Toward understanding actin activation of myosin ATPase: The role of myosin surface loops
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.0601595103
  contributor:
    fullname: Onishi
– ident: ref_29
  doi: 10.2210/pdb7ad9/pdb
– volume: 38
  start-page: 15078
  year: 1999
  ident: ref_103
  article-title: Functional characterization of the secondary actin binding site of myosin II
  publication-title: Biochemistry
  doi: 10.1021/bi991595h
  contributor:
    fullname: Furch
– volume: 25
  start-page: 528
  year: 2018
  ident: ref_27
  article-title: Structural transitions of F-actin upon ATP hydrolysis at near-atomic resolution revealed by cryo-EM
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/s41594-018-0074-0
  contributor:
    fullname: Merino
– volume: 154
  start-page: 611
  year: 2001
  ident: ref_46
  article-title: Myosin light chain kinase binding to a unique site on F-actin revealed by three-dimensional image reconstruction
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.200105079
  contributor:
    fullname: Hatch
– volume: 43
  start-page: 2605
  year: 2004
  ident: ref_96
  article-title: Functional role of loop 2 in myosin V
  publication-title: Biochemistry
  doi: 10.1021/bi035510v
  contributor:
    fullname: Yengo
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Snippet Actin is one of the most abundant and versatile proteins in eukaryotic cells. As discussed in many contributions to this Special Issue, its transition from a...
Simple SummaryAlthough actin is a highly conserved protein, it is involved in many diverse cellular processes. Actin owes its diversity of function to its...
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SubjectTerms Actin
actin-binding proteins
Adenosine triphosphatase
Amino acids
Binding sites
Cell size
Electron microscopy
Enzymes
Filaments
force production
Hydrolysis
Isoforms
Kinases
molecular motor
Motor activity
Myosin
Myosin ATPase
Polymerization
Proteins
Review
Somatic cells
tropomyosin
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Title The Central Role of the F-Actin Surface in Myosin Force Generation
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