Caldesmon controls stress fiber force-balance through dynamic cross-linking of myosin II and actin-tropomyosin filaments

Contractile actomyosin bundles are key force-producing and mechanosensing elements in muscle and non-muscle tissues. Whereas the organization of muscle myofibrils and mechanism regulating their contractility are relatively well-established, the principles by which myosin-II activity and force-balanc...

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Published inNature communications Vol. 13; no. 1; p. 6032
Main Authors Kokate, Shrikant B., Ciuba, Katarzyna, Tran, Vivien D., Kumari, Reena, Tojkander, Sari, Engel, Ulrike, Kogan, Konstantin, Kumar, Sanjay, Lappalainen, Pekka
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 13.10.2022
Nature Publishing Group
Nature Portfolio
Subjects
13/109
14/1
14/19
14/34
14/35
14/63
14/69
38/22
38/23
38/77
42/41
42/44
42/70
45/29
49/31
631/80/128/1675
631/80/128/2031
631/80/84/2336
82/1
82/80
82/83
Actin
Actin Cytoskeleton - metabolism
Actins - metabolism
Actomyosin
Actomyosin - metabolism
Calmodulin-Binding Proteins - metabolism
Cell migration
Crosslinking
Depletion
Fibers
Filaments
Humanities and Social Sciences
Morphogenesis
multidisciplinary
Muscle contraction
Muscle, Smooth - metabolism
Muscles
Myofibrils
Myosin
Myosin Type II - metabolism
Myosins - metabolism
Science
Science (multidisciplinary)
Smooth muscle
Stress
Stress Fibers - metabolism
Tropomyosin
Tropomyosin - metabolism
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Abstract Contractile actomyosin bundles are key force-producing and mechanosensing elements in muscle and non-muscle tissues. Whereas the organization of muscle myofibrils and mechanism regulating their contractility are relatively well-established, the principles by which myosin-II activity and force-balance are regulated in non-muscle cells have remained elusive. We show that Caldesmon, an important component of smooth muscle and non-muscle cell actomyosin bundles, is an elongated protein that functions as a dynamic cross-linker between myosin-II and tropomyosin-actin filaments. Depletion of Caldesmon results in aberrant lateral movement of myosin-II filaments along actin bundles, leading to irregular myosin distribution within stress fibers. This manifests as defects in stress fiber network organization and contractility, and accompanied problems in cell morphogenesis, migration, invasion, and mechanosensing. These results identify Caldesmon as critical factor that ensures regular myosin-II spacing within non-muscle cell actomyosin bundles, and reveal how stress fiber networks are controlled through dynamic cross-linking of tropomyosin-actin and myosin filaments. In this study the authors report that Caldesmon controls force-balance and architecture of stress fibers through dynamic cross-linking of actin and myosin filaments. Caldesmon depletion led to consequent problems in cell morphogenesis, motility and mechanosensing.
AbstractList Contractile actomyosin bundles are key force-producing and mechanosensing elements in muscle and non-muscle tissues. Whereas the organization of muscle myofibrils and mechanism regulating their contractility are relatively well-established, the principles by which myosin-II activity and force-balance are regulated in non-muscle cells have remained elusive. We show that Caldesmon, an important component of smooth muscle and non-muscle cell actomyosin bundles, is an elongated protein that functions as a dynamic cross-linker between myosin-II and tropomyosin-actin filaments. Depletion of Caldesmon results in aberrant lateral movement of myosin-II filaments along actin bundles, leading to irregular myosin distribution within stress fibers. This manifests as defects in stress fiber network organization and contractility, and accompanied problems in cell morphogenesis, migration, invasion, and mechanosensing. These results identify Caldesmon as critical factor that ensures regular myosin-II spacing within non-muscle cell actomyosin bundles, and reveal how stress fiber networks are controlled through dynamic cross-linking of tropomyosin-actin and myosin filaments. In this study the authors report that Caldesmon controls force-balance and architecture of stress fibers through dynamic cross-linking of actin and myosin filaments. Caldesmon depletion led to consequent problems in cell morphogenesis, motility and mechanosensing.
Contractile actomyosin bundles are key force-producing and mechanosensing elements in muscle and non-muscle tissues. Whereas the organization of muscle myofibrils and mechanism regulating their contractility are relatively well-established, the principles by which myosin-II activity and force-balance are regulated in non-muscle cells have remained elusive. We show that Caldesmon, an important component of smooth muscle and non-muscle cell actomyosin bundles, is an elongated protein that functions as a dynamic cross-linker between myosin-II and tropomyosin-actin filaments. Depletion of Caldesmon results in aberrant lateral movement of myosin-II filaments along actin bundles, leading to irregular myosin distribution within stress fibers. This manifests as defects in stress fiber network organization and contractility, and accompanied problems in cell morphogenesis, migration, invasion, and mechanosensing. These results identify Caldesmon as critical factor that ensures regular myosin-II spacing within non-muscle cell actomyosin bundles, and reveal how stress fiber networks are controlled through dynamic cross-linking of tropomyosin-actin and myosin filaments.
Abstract Contractile actomyosin bundles are key force-producing and mechanosensing elements in muscle and non-muscle tissues. Whereas the organization of muscle myofibrils and mechanism regulating their contractility are relatively well-established, the principles by which myosin-II activity and force-balance are regulated in non-muscle cells have remained elusive. We show that Caldesmon, an important component of smooth muscle and non-muscle cell actomyosin bundles, is an elongated protein that functions as a dynamic cross-linker between myosin-II and tropomyosin-actin filaments. Depletion of Caldesmon results in aberrant lateral movement of myosin-II filaments along actin bundles, leading to irregular myosin distribution within stress fibers. This manifests as defects in stress fiber network organization and contractility, and accompanied problems in cell morphogenesis, migration, invasion, and mechanosensing. These results identify Caldesmon as critical factor that ensures regular myosin-II spacing within non-muscle cell actomyosin bundles, and reveal how stress fiber networks are controlled through dynamic cross-linking of tropomyosin-actin and myosin filaments.
Contractile actomyosin bundles are key force-producing and mechanosensing elements in muscle and non-muscle tissues. Whereas the organization of muscle myofibrils and mechanism regulating their contractility are relatively well-established, the principles by which myosin-II activity and force-balance are regulated in non-muscle cells have remained elusive. We show that Caldesmon, an important component of smooth muscle and non-muscle cell actomyosin bundles, is an elongated protein that functions as a dynamic cross-linker between myosin-II and tropomyosin-actin filaments. Depletion of Caldesmon results in aberrant lateral movement of myosin-II filaments along actin bundles, leading to irregular myosin distribution within stress fibers. This manifests as defects in stress fiber network organization and contractility, and accompanied problems in cell morphogenesis, migration, invasion, and mechanosensing. These results identify Caldesmon as critical factor that ensures regular myosin-II spacing within non-muscle cell actomyosin bundles, and reveal how stress fiber networks are controlled through dynamic cross-linking of tropomyosin-actin and myosin filaments.In this study the authors report that Caldesmon controls force-balance and architecture of stress fibers through dynamic cross-linking of actin and myosin filaments. Caldesmon depletion led to consequent problems in cell morphogenesis, motility and mechanosensing.
In this study the authors report that Caldesmon controls force-balance and architecture of stress fibers through dynamic cross-linking of actin and myosin filaments. Caldesmon depletion led to consequent problems in cell morphogenesis, motility and mechanosensing.
ArticleNumber 6032
Author Kumari, Reena
Engel, Ulrike
Kumar, Sanjay
Lappalainen, Pekka
Tojkander, Sari
Ciuba, Katarzyna
Tran, Vivien D.
Kokate, Shrikant B.
Kogan, Konstantin
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  surname: Lappalainen
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/36229430$$D View this record in MEDLINE/PubMed
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Snippet Contractile actomyosin bundles are key force-producing and mechanosensing elements in muscle and non-muscle tissues. Whereas the organization of muscle...
Abstract Contractile actomyosin bundles are key force-producing and mechanosensing elements in muscle and non-muscle tissues. Whereas the organization of...
In this study the authors report that Caldesmon controls force-balance and architecture of stress fibers through dynamic cross-linking of actin and myosin...
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Actin
Actin Cytoskeleton - metabolism
Actins - metabolism
Actomyosin
Actomyosin - metabolism
Calmodulin-Binding Proteins - metabolism
Cell migration
Crosslinking
Depletion
Fibers
Filaments
Humanities and Social Sciences
Morphogenesis
multidisciplinary
Muscle contraction
Muscle, Smooth - metabolism
Muscles
Myofibrils
Myosin
Myosin Type II - metabolism
Myosins - metabolism
Science
Science (multidisciplinary)
Smooth muscle
Stress
Stress Fibers - metabolism
Tropomyosin
Tropomyosin - metabolism
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Title Caldesmon controls stress fiber force-balance through dynamic cross-linking of myosin II and actin-tropomyosin filaments
URI https://link.springer.com/article/10.1038/s41467-022-33688-w
https://www.ncbi.nlm.nih.gov/pubmed/36229430
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https://pubmed.ncbi.nlm.nih.gov/PMC9561149
https://doaj.org/article/516263fa89db4757a6baba27de7c6109
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