Conformational transitions and interactions underlying the function of membrane embedded receptor protein kinases

Among membrane receptors, the single-span receptor protein kinases occupy a broad but specific functional niche determined by distinctive features of the underlying transmembrane signaling mechanisms that are briefly overviewed on the basis of some of the most representative examples, followed by a...

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Published inBiochimica et biophysica acta. Biomembranes Vol. 1859; no. 9; pp. 1417 - 1429
Main Authors Bocharov, Eduard V., Sharonov, Georgy V., Bocharova, Olga V., Pavlov, Konstantin V.
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.09.2017
Subjects
Cell Membrane - chemistry
Cell Membrane - genetics
Cytoskeleton - chemistry
Cytoskeleton - genetics
cytoskeleton remodeling
Dimerization
lipid raft
Membrane Lipids - chemistry
Membrane Lipids - metabolism
Membrane Proteins - chemistry
Membrane Proteins - genetics
Membrane Proteins - metabolism
Protein Conformation
protein-lipid and protein-protein interactions
Receptor Protein-Tyrosine Kinases - chemistry
Receptor Protein-Tyrosine Kinases - genetics
Receptor Protein-Tyrosine Kinases - metabolism
receptor tyrosine kinase
Signal Transduction
single-span membrane protein
JM
PS
Lo
cytoskeleton remodeling
signal transduction
ECD
single-span membrane protein
RTK
TMD
ICD
GPI-AP
PA
lipid raft
TKL
IDP
protein-lipid and protein-protein interactions
PIP
Ld
receptor tyrosine kinase
SH2
Online AccessGet full text

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Abstract Among membrane receptors, the single-span receptor protein kinases occupy a broad but specific functional niche determined by distinctive features of the underlying transmembrane signaling mechanisms that are briefly overviewed on the basis of some of the most representative examples, followed by a more detailed discussion of several hierarchical levels of organization and interactions involved. All these levels, including single-molecule interactions (e.g., dimerization, liganding, chemical modifications), local processes (e.g. lipid membrane perturbations, cytoskeletal interactions), and larger scale phenomena (e.g., effects of membrane surface shape or electrochemical potential gradients) appear to be closely integrated to achieve the observed diversity of the receptor functioning. Different species of receptor protein kinases meet their specific functional demands through different structural features defining their responses to stimulation, but certain common patterns exist. Signaling by receptor protein kinases is typically associated with the receptor dimerization and clustering, ligand-induced rearrangements of receptor domains through allosteric conformational transitions with involvement of lipids, release of the sequestered lipids, restriction of receptor diffusion, cytoskeleton and membrane shape remodeling. Understanding of complexity and continuity of the signaling processes can help identifying currently neglected opportunities for influencing the receptor signaling with potential therapeutic implications. This article is part of a Special Issue entitled: Interactions between membrane receptors in cellular membranes edited by Kalina Hristova. [Display omitted] •The structural traits of single-span receptors define their specific functional niche•Diverse levels of functional integration are inherent to receptor protein kinases•Lipid membrane is inalienable part of the self-consistent signaling system•Cytoskeleton remodeling and membrane shaping attune receptor protein kinase activity
AbstractList Among membrane receptors, the single-span receptor protein kinases occupy a broad but specific functional niche determined by distinctive features of the underlying transmembrane signaling mechanisms that are briefly overviewed on the basis of some of the most representative examples, followed by a more detailed discussion of several hierarchical levels of organization and interactions involved. All these levels, including single-molecule interactions (e.g., dimerization, liganding, chemical modifications), local processes (e.g. lipid membrane perturbations, cytoskeletal interactions), and larger scale phenomena (e.g., effects of membrane surface shape or electrochemical potential gradients) appear to be closely integrated to achieve the observed diversity of the receptor functioning. Different species of receptor protein kinases meet their specific functional demands through different structural features defining their responses to stimulation, but certain common patterns exist. Signaling by receptor protein kinases is typically associated with the receptor dimerization and clustering, ligand-induced rearrangements of receptor domains through allosteric conformational transitions with involvement of lipids, release of the sequestered lipids, restriction of receptor diffusion, cytoskeleton and membrane shape remodeling. Understanding of complexity and continuity of the signaling processes can help identifying currently neglected opportunities for influencing the receptor signaling with potential therapeutic implications. This article is part of a Special Issue entitled: Interactions between membrane receptors in cellular membranes edited by Kalina Hristova.
Among membrane receptors, the single-span receptor protein kinases occupy a broad but specific functional niche determined by distinctive features of the underlying transmembrane signaling mechanisms that are briefly overviewed on the basis of some of the most representative examples, followed by a more detailed discussion of several hierarchical levels of organization and interactions involved. All these levels, including single-molecule interactions (e.g., dimerization, liganding, chemical modifications), local processes (e.g. lipid membrane perturbations, cytoskeletal interactions), and larger scale phenomena (e.g., effects of membrane surface shape or electrochemical potential gradients) appear to be closely integrated to achieve the observed diversity of the receptor functioning. Different species of receptor protein kinases meet their specific functional demands through different structural features defining their responses to stimulation, but certain common patterns exist. Signaling by receptor protein kinases is typically associated with the receptor dimerization and clustering, ligand-induced rearrangements of receptor domains through allosteric conformational transitions with involvement of lipids, release of the sequestered lipids, restriction of receptor diffusion, cytoskeleton and membrane shape remodeling. Understanding of complexity and continuity of the signaling processes can help identifying currently neglected opportunities for influencing the receptor signaling with potential therapeutic implications. This article is part of a Special Issue entitled: Interactions between membrane receptors in cellular membranes edited by Kalina Hristova. [Display omitted] •The structural traits of single-span receptors define their specific functional niche•Diverse levels of functional integration are inherent to receptor protein kinases•Lipid membrane is inalienable part of the self-consistent signaling system•Cytoskeleton remodeling and membrane shaping attune receptor protein kinase activity
Author Bocharova, Olga V.
Pavlov, Konstantin V.
Sharonov, Georgy V.
Bocharov, Eduard V.
Author_xml – sequence: 1
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  surname: Sharonov
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  givenname: Olga V.
  surname: Bocharova
  fullname: Bocharova, Olga V.
– sequence: 4
  givenname: Konstantin V.
  surname: Pavlov
  fullname: Pavlov, Konstantin V.
BackLink https://www.ncbi.nlm.nih.gov/pubmed/28131853$$D View this record in MEDLINE/PubMed
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cytoskeleton remodeling
signal transduction
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single-span membrane protein
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ICD
GPI-AP
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lipid raft
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IDP
protein-lipid and protein-protein interactions
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Bennasroune, Fickova, Gardin, Dirrig-Grosch, Aunis, Cremel, Hubert (bb0230) 2004; 15
Low-Nam, Lidke, Cutler, Roovers, van Bergen en Henegouwen, Wilson, Lidke (bb0705) 2011; 18
McLaughlin, Smith, Hayman, Murray (bb0440) 2005; 126
Bruntz, Lindsley, Brown (bb0670) 2014; 66
Mancini, Koch, Stefan, Niemann, Tamura (bb0800) 2000; 482
Pellegrini, Burke, von Delft, Mulloy, Blundell (bb0260) 2000; 407
Lidke, Lidke, Rieger, Jovin, Arndt-Jovin (bb0740) 2005; 170
Kavran, McCabe, Byrne, Connacher, Wang, Ramek, Sarabipour, Shan, Shaw, Hristova, Cole, Leahy (bb0295) 2014; 3
Yaron, Cordova, Sprinzak (bb0510) 2014; 107
Bocharov, Mineev, Goncharuk, Arseniev (bb0210) 2012; 1818
Ariotti, Liang, Xu, Zhang, Yonekubo, Inder, Du, Parton, Hancock, Plowman (bb0385) 2010; 30
Bugge, Papaleo, Haxholm, Hopper, Robinson, Olsen, Lindorff-Larsen, Kragelund (bb0130) 2016; 7
Cymer, Schneider (bb0100) 2010; 4
Manni, Mineev, Usmanova, Lyukmanova, Shulepko, Kirpichnikov, Winter, Matkovic, Deupi, Arseniev, Ballmer-Hofer (bb0280) 2014; 22
Jin, Sison, Li, Tian, Wnuk, Sung, Jeansson, Zhang, Tucholska, Jones, Kerjaschki, Shibuya, Fantus, Nagy, Gerber, Ferrara, Pawson, Quaggin (bb0635) 2012; 151
den Hartigh, van Bergen en Henegouwen, Verkleij, Boonstra (bb0780) 1992; 119
Li, Wimley, Hristova (bb0030) 2012; 1818
Cymer, Veerappan, Schneider (bb0040) 2012; 1818
Lelimousin, Limongelli, Sansom (bb0120) 2016; 138
Shibuya, Sarabipour, Ballmer-Hofer, Hristova (bb0270) 2013; 5
Casaletto, McClatchey (bb0465) 2012; 12
Kolter (bb0625) 2012; 2012
Buccione, Orth, McNiven (bb0850) 2004; 5
McClatchey (bb0815) 2014; 127
Rahman, Akhtar, Jamil, Banik, Asaduzzaman (bb0025) 2015; 3
Goh, Sorkin (bb0365) 2013; 5
Uversky (bb0115) 2015; 589
McLaughlin, Murray (bb0675) 2005; 438
Sigismund, Confalonieri, Ciliberto, Polo, Scita, Di (bb0870) 2012; 92
Nikolov, Xu, Himanen (bb0345) 2013; 1834
Saha, Lee, Polley, Groves, Rao, Mayor (bb0555) 2015; 26
Ligensa, Krauss, Demuth, Schumacher, Camonis, Jaques, Weidner (bb0810) 2001; 276
Belov, Mohammadi (bb0090) 2012; 5
Walters, DeGrado (bb0050) 2006; 103
Sparr, Ash, Nazarov, Rijkers, Hemminga, Tieleman, Killian (bb0595) 2005; 280
Mineev, Panova, Bocharova, Bocharov, Arseniev (bb0125) 2015; 54
Nussinov, Jang, Tsai (bb0480) 2015; 90
Rangamani, Lipshtat, Azeloglu, Calizo, Hu, Ghassemi, Hone, Scarlata, Neves, Iyengar (bb0875) 2013; 154
Jadwin, Oh, Curran, Ogiue-Ikeda, Jia, White, Machida, Yu, Mayer (bb0490) 2016; 5
Jura, Endres, Engel, Deindl, Das, Lamers, Wemmer, Zhang, Kuriyan (bb0185) 2009; 137
Waters, Brooks (bb0305) 2015; 466
Bocharov, Pavlov, Blommers, Arvinte, Arseniev (bb0325) 2008; 273
Arkhipov, Shan, Kim, Shaw (bb0395) 2014; 10
Egea, Nissen, Dufour, Sahin, Greer, Kullander, Mrsic-Flogel, Greenberg, Kiehn, Vanderhaeghen, Klein (bb0505) 2005; 47
Daumas, Destainville, Millot, Lopez, Dean, Salomé (bb0765) 2003; 84
Sinclair, Denton, Schepartz (bb0245) 2014; 136
Lee, Saha, Polley, Huang, Mayor, Rao, Groves (bb0565) 2015; 119
Mattila, Batista, Treanor (bb0735) 2016; 212
Volinsky, Kholodenko (bb0015) 2013; 5
Lemmon, Schlessinger, Ferguson (bb0160) 2014; 6
Milovanovic, Honigmann, Koike, Göttfert, Pähler, Junius, Müllar, Diederichsen, Janshoff, Grubmüller, Risselada, Eggeling, Hell, van den Bogaart, Jahn (bb0620) 2015; 6
Goichberg, Kannappan, Cimini, Bai, Sanada, Sorrentino, Signore, Kajstura, Rota, Anversa, Leri (bb0475) 2013; 128
Brown (bb0545) 2006; 21
Coskun, Simons (bb0610) 2011; 19
Dustin, Groves (bb0730) 2012; 41
Jülich, Mould, Koper, Holley (bb0840) 2009; 136
Schmick, Bastiaens (bb0860) 2014; 156
Yano, Kondo, Kitani, Yamamoto, Matsuzaki (bb0535) 2015; 54
Sarabipour, Hristova (bb0265) 2016; 7
Kleiman, Maiwald, Conzelmann, Lauffenburger, Sorger (bb0495) 2011; 43
Mineo, Gill, Anderson (bb0615) 1999; 274
Kovacs, Zorn, Huang, Barros, Kuriyan (bb0165) 2015; 84
O'Donoghue, Pielak, Smoligovets, Lin, Groves (bb0750) 2013; 2
Delcourt, Bockaert, Marin (bb0020) 2007; 28
Bocharov, Korzhnev, Blommers, Arvinte, Orekhov, Billeter, Arseniev (bb0320) 2002; 277
Yu, Smoligovets, Groves (bb0775) 2013; 126
MacKenzie (bb0045) 2006; 106
Harding, Hancock (bb0650) 2008; 18
Yamamoto, Higasa, Sakaguchi, Shien, Soh, Ichimura, Furukawa, Hashida, Tsukuda, Takigawa, Matsuo, Kiura, Miyoshi, Matsuda, Toyooka (bb0425) 2014; 106
Mielke, Taghibiglou, Liu, Zhang, Jia, Adeli, Wang (bb0470) 2005; 93
Owen, Williamson, Magenau, Gaus (bb0550) 2012; 3
Kholodenko, Hancock, Kolch (bb0655) 2010; 11
Bocharov, Mineev, Pavlov, Akimov, Kuznetsov, Efremov, Arseniev (bb0070) 2017; 1859
Carpenter, Liao (bb0155) 2013; 5
Zhou, Hancock (bb0645) 2015; 1853
Ehrlich, Horbelt, Marom, Knaus, Henis (bb0315) 2011; 23
Warner, Wybenga-Groot, Pawson (bb0355) 2008; 275
Hinck, Mueller, Springer (bb0150) 2016
Hubbard (bb0285) 2013; 5
Pike (bb0580) 2005; 1746
Thurner, Gsandtner, Kudlacek, Choquet, Nanoff, Freissmuth, Zezula (bb0770) 2014; 289
Matsushita, Tamagaki, Miyazawa, Aimoto, Smith, Sato (bb0415) 2013; 110
Boggon, Eck (bb0640) 2004; 23
Bragin, Mineev, Bocharova, Volynsky, Bocharov, Arseniev (bb0220) 2016; 428
Adak, Yang, Macdonald-Obermann, Pike (bb0460) 2011; 286
Patel, Murray, Insel (bb0695) 2008; 48
Kusumi, Tsunoyama, Hirosawa, Kasai, Fujiwara (bb0720) 2014; 10
Suzuki (bb0575) 2015; 317
Bessman, Bagchi, Ferguson, Lemmon (bb0180) 2014; 9
Raghupathy, Anilkumar, Polley, Singh, Yadav, Johnson, Suryawanshi, Saikam, Sawant, Panda, Guo, Vishwakarma, Rao, Mayor (bb0665) 2015; 161
Lu, Mi, Schürpf, Walz, Springer (bb0450) 2012; 287
Endres, Das, Smith, Arkhipov, Kovacs, Huang, Pelton, Shan, Shaw, Wemmer, Groves, Kuriyan (bb0225) 2013; 152
Brooks, Dai, O'Mara, Abankwa, Chhabra, Pelekanos, Gardon, Tunny, Blucher, Morton, Parker, Sierecki, Gambin, Gomez, Alexandrov, Wilson, Doxastakis, Mark, Waters (bb0310) 2014; 344
Bocharov, Mayzel, Volynsky, Mineev, Tkach, Ermolyuk, Schulga, Efremov, Arseniev (bb0605) 2010; 98
Delos, Garay, Antonescu (bb0590) 2015; 27
Ou, Schrock, Bocharov, Klempner, Haddad, Steinecker, Johnson, Gitlitz, Chung, Campregher, Ross, Stephens, Miller, Suh, Ali, Velcheti (bb0430) 2016
Horner, Antonenko, Pohl (bb0405) 2009; 96
Kusumi, Sako, Yamamoto (bb0725) 1993; 65
Velghe, Van, Polyansky, Chand, Montano-Almendras, Charni, Hallberg, Essaghir, Demoulin (bb0600) 2014; 33
Seiradake, Schaupp, del Toro Ruiz, Kaufmann, Mitakidis, Harlos, Aricescu, Klein, Jones (bb0500) 2013; 20
Borg, Marchetto, Le, Ollendorff, Jaulin-Bastard, Saito, Fournier, Adélaïde, Margolis, Birnbaum (bb0795) 2000; 2
Subbaiah, Kranjec, Thomas, Banks (bb0785) 2011; 439
Wu, Li, Craddock, Foreman, Mulvihill, Ji, Miller, Hubbard (bb0290) 2008; 27
Bethani, Skånland, Dikic, Acker-Palmer (bb0335) 2010; 29
Julien, Bobowski, Steenackers, Le, Delannoy (bb0520) 2013; 2
Miaczynska (bb0690) 2013; 5
Lee, Miyazaki, Romeo, Shoelson (bb0300) 2014; 289
James, Beauchamp, Manchanda, Kazlauskas, Ramesh (bb0805) 2004; 117
Landau, Ben-Tal (bb0095) 2008; 1785
Arpel, Sawma, Spenlé, Fritz, Meyer, Garnier, Velázquez-Quesada, Hussenet, Aci-Sèche, Baumlin, Genest, Brasse, Hubert, Crémel, Orend, Laquerrière, Bagnard (bb0235) 2014; 8
Tamagaki, Furukawa, Yamaguchi, Hojo, Aimoto, Smith, Sato (bb0420) 2014; 53
Marchetti, Callegari, Luin, Signore, Vi
Lu (10.1016/j.bbamem.2017.01.025_bb0445) 2010; 30
Julien (10.1016/j.bbamem.2017.01.025_bb0520) 2013; 2
Kovacs (10.1016/j.bbamem.2017.01.025_bb0165) 2015; 84
Owen (10.1016/j.bbamem.2017.01.025_bb0550) 2012; 3
Chaikuad (10.1016/j.bbamem.2017.01.025_bb0330) 2016
Cymer (10.1016/j.bbamem.2017.01.025_bb0100) 2010; 4
Lee (10.1016/j.bbamem.2017.01.025_bb0300) 2014; 289
Yang (10.1016/j.bbamem.2017.01.025_bb0825) 2016; 16
Walters (10.1016/j.bbamem.2017.01.025_bb0050) 2006; 103
Bocharov (10.1016/j.bbamem.2017.01.025_bb0210) 2012; 1818
Salaita (10.1016/j.bbamem.2017.01.025_bb0745) 2010; 327
Mielke (10.1016/j.bbamem.2017.01.025_bb0470) 2005; 93
Fagotto (10.1016/j.bbamem.2017.01.025_bb0835) 2013; 27
Horner (10.1016/j.bbamem.2017.01.025_bb0405) 2009; 96
James (10.1016/j.bbamem.2017.01.025_bb0805) 2004; 117
Gauthier (10.1016/j.bbamem.2017.01.025_bb0865) 2012; 22
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Arpel (10.1016/j.bbamem.2017.01.025_bb0235) 2014; 8
Bruntz (10.1016/j.bbamem.2017.01.025_bb0670) 2014; 66
He (10.1016/j.bbamem.2017.01.025_bb0075) 2012; 1818
Ou (10.1016/j.bbamem.2017.01.025_bb0430) 2016
Schmick (10.1016/j.bbamem.2017.01.025_bb0860) 2014; 156
Sharonov (10.1016/j.bbamem.2017.01.025_bb0350) 2014; 289
Oh (10.1016/j.bbamem.2017.01.025_bb0485) 2012; 109
Kolter (10.1016/j.bbamem.2017.01.025_bb0625) 2012; 2012
Hedger (10.1016/j.bbamem.2017.01.025_bb0525) 2016; 1858
Hinck (10.1016/j.bbamem.2017.01.025_bb0150) 2016
Lu (10.1016/j.bbamem.2017.01.025_bb0450) 2012; 287
Velghe (10.1016/j.bbamem.2017.01.025_bb0600) 2014; 33
Bublil (10.1016/j.bbamem.2017.01.025_bb0240) 2016; 55
Klein (10.1016/j.bbamem.2017.01.025_bb0830) 2012; 139
Kovács (10.1016/j.bbamem.2017.01.025_bb0880) 2016; 6
Casaletto (10.1016/j.bbamem.2017.01.025_bb0465) 2012; 12
Yu (10.1016/j.bbamem.2017.01.025_bb0775) 2013; 126
Warner (10.1016/j.bbamem.2017.01.025_bb0355) 2008; 275
Wu (10.1016/j.bbamem.2017.01.025_bb0290) 2008; 27
Buccione (10.1016/j.bbamem.2017.01.025_bb0850) 2004; 5
Bocharov (10.1016/j.bbamem.2017.01.025_bb0215) 2016; 1858
Bethani (10.1016/j.bbamem.2017.01.025_bb0335) 2010; 29
Ariotti (10.1016/j.bbamem.2017.01.025_bb0385) 2010; 30
Belov (10.1016/j.bbamem.2017.01.025_bb0090) 2012; 5
Mineo (10.1016/j.bbamem.2017.01.025_bb0615) 1999; 274
Goichberg (10.1016/j.bbamem.2017.01.025_bb0475) 2013; 128
Horner (10.1016/j.bbamem.2017.01.025_bb0410) 2013; 110
Lelimousin (10.1016/j.bbamem.2017.01.025_bb0120) 2016; 138
Plotnikov (10.1016/j.bbamem.2017.01.025_bb0255) 1999; 98
Macdonald-Obermann (10.1016/j.bbamem.2017.01.025_bb0455) 2009; 284
Tao (10.1016/j.bbamem.2017.01.025_bb0170) 2008; 121
Thurner (10.1016/j.bbamem.2017.01.025_bb0770) 2014; 289
Suzuki (10.1016/j.bbamem.2017.01.025_bb0575) 2015; 317
Ligensa (10.1016/j.bbamem.2017.01.025_bb0810) 2001; 276
Saha (10.1016/j.bbamem.2017.01.025_bb0555) 2015; 26
Bragin (10.1016/j.bbamem.2017.01.025_bb0220) 2016; 428
Hedger (10.1016/j.bbamem.2017.01.025_bb0055) 2015; 5
Harding (10.1016/j.bbamem.2017.01.025_bb0650) 2008; 18
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Fleishman (10.1016/j.bbamem.2017.01.025_bb0195) 2002; 99
Marchetti (10.1016/j.bbamem.2017.01.025_bb0710) 2013; 126
Kavran (10.1016/j.bbamem.2017.01.025_bb0295) 2014; 3
Mineev (10.1016/j.bbamem.2017.01.025_bb0205) 2010; 400
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Li (10.1016/j.bbamem.2017.01.025_bb0030) 2012; 1818
Haxholm (10.1016/j.bbamem.2017.01.025_bb0135) 2015; 468
Belov (10.1016/j.bbamem.2017.01.025_bb0250) 2013; 5
Jin (10.1016/j.bbamem.2017.01.025_bb0635) 2012; 151
Coskun (10.1016/j.bbamem.2017.01.025_bb0515) 2011; 108
Rangamani (10.1016/j.bbamem.2017.01.025_bb0875) 2013; 154
Saarikangas (10.1016/j.bbamem.2017.01.025_bb0680) 2010; 90
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O'Donoghue (10.1016/j.bbamem.2017.01.025_bb0750) 2013; 2
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Guo (10.1016/j.bbamem.2017.01.025_bb0370) 2016; 116
Uversky (10.1016/j.bbamem.2017.01.025_bb0115) 2015; 589
Low-Nam (10.1016/j.bbamem.2017.01.025_bb0705) 2011; 18
Tamagaki (10.1016/j.bbamem.2017.01.025_bb0420) 2014; 53
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Suzuki (10.1016/j.bbamem.2017.01.025_bb0660) 2012; 7
Bugge (10.1016/j.bbamem.2017.01.025_bb0130) 2016; 7
Lemmon (10.1016/j.bbamem.2017.01.025_bb0010) 2010; 141
Shibuya (10.1016/j.bbamem.2017.01.025_rf0270) 2013; 5
Yaron (10.1016/j.bbamem.2017.01.025_bb0510) 2014; 107
Bocharov (10.1016/j.bbamem.2017.01.025_bb0070) 2017; 1859
Rosenzweig (10.1016/j.bbamem.2017.01.025_bb0360) 2012; 83
McClatchey (10.1016/j.bbamem.2017.01.025_bb0815) 2014; 127
Himanen (10.1016/j.bbamem.2017.01.025_bb0390) 2010; 107
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Li (10.1016/j.bbamem.2017.01.025_bb0685) 2008; 20
Lemmon (10.1016/j.bbamem.2017.01.025_bb0160) 2014; 6
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Patel (10.1016/j.bbamem.2017.01.025_bb0695) 2008; 48
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Bocharov (10.1016/j.bbamem.2017.01.025_bb0325) 2008; 273
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Yamamoto (10.1016/j.bbamem.2017.01.025_bb0425) 2014; 106
Boggon (10.1016/j.bbamem.2017.01.025_bb0640) 2004; 23
Volinsky (10.1016/j.bbamem.2017.01.025_bb0015) 2013; 5
Nevoltris (10.1016/j.bbamem.2017.01.025_bb0175) 2015; 9
Kinoshita (10.1016/j.bbamem.2017.01.025_bb0630) 2014; 90
Dustin (10.1016/j.bbamem.2017.01.025_bb0730) 2012; 41
Kleiman (10.1016/j.bbamem.2017.01.025_bb0495) 2011; 43
Zhou (10.1016/j.bbamem.2017.01.025_bb0645) 2015; 1853
Jaqaman (10.1016/j.bbamem.2017.01.025_bb0760) 2011; 146
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Goh (10.1016/j.bbamem.2017.01.025_bb0365) 2013; 5
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Lidke (10.1016/j.bbamem.2017.01.025_bb0740) 2005; 170
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Hubbard (10.1016/j.bbamem.2017.01.025_bb0285) 2013; 5
Mineev (10.1016/j.bbamem.2017.01.025_bb0125) 2015; 54
Arkhipov (10.1016/j.bbamem.2017.01.025_bb0110) 2013; 152
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Brooks (10.1016/j.bbamem.2017.01.025_bb0310) 2014; 344
Waters (10.1016/j.bbamem.2017.01.025_bb0305) 2015; 466
Shochat (10.1016/j.bbamem.2017.01.025_bb0435) 2014; 124
Raghupathy (10.1016/j.bbamem.2017.01.025_bb0665) 2015; 161
Teese (10.1016/j.bbamem.2017.01.025_bb0065) 2015; 54
McLaughlin (10.1016/j.bbamem.2017.01.025_bb0440) 2005; 126
Delcourt (10.1016/j.bbamem.2017.01.025_bb0020) 2007; 28
Schmidt (10.1016/j.bbamem.2017.01.025_bb0060) 2016; 291
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Bocharov (10.1016/j.bbamem.2017.01.025_bb0105) 2013; 21
Sinclair (10.1016/j.bbamem.2017.01.025_bb0245) 2014; 136
Jura (10.1016/j.bbamem.2017.01.025_bb0185) 2009; 137
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Rahman (10.1016/j.bbamem.2017.01.025_bb0025) 2015; 3
Sarabipour (10.1016/j.bbamem.2017.01.025_bb0275) 2016; 5
Lee (10.1016/j.bbamem.2017.01.025_bb0565) 2015; 119
Chung (10.1016/j.bbamem.2017.01.025_bb0700) 2010; 464
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Winter (10.1016/j.bbamem.2017.01.025_bb0715) 2012; 1818
Endres (10.1016/j.bbamem.2017.01.025_bb0225) 2013; 152
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Hoon (10.1016/j.bbamem.2017.01.025_bb0855) 2012; 32
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Subbaiah (10.1016/j.bbamem.2017.01.025_bb0785) 2011; 439
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Delos (10.1016/j.bbamem.2017.01.025_bb0590) 2015; 27
Sharonov (10.1016/j.bbamem.2017.01.025_bb0570) 2016; 81
Kaizuka (10.1016/j.bbamem.2017.01.025_bb0755) 2007; 104
Köster (10.1016/j.bbamem.2017.01.025_bb0560) 2016; 113
Bocharov (10.1016/j.bbamem.2017.01.025_bb0320) 2002; 277
Landau (10.1016/j.bbamem.2017.01.025_bb0095) 2008; 1785
Yano (10.1016/j.bbamem.2017.01.025_bb0535) 2015; 54
Torres (10.1016/j.bbamem.2017.01.025_bb0790) 1998; 21
Trenker (10.1016/j.bbamem.2017.01.025_bb0005) 2016; 39
Coskun (10.1016/j.bbamem.2017.01.025_bb0610) 2011; 19
Nikolov (10.1016/j.bbamem.2017.01.025_bb0345) 2013; 1834
Bocharov (10.1016/j.bbamem.2017.01.025_bb0605) 2010; 98
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Kusumi (10.1016/j.bbamem.2017.01.025_bb0720) 2014; 10
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Chavent (10.1016/j.bbamem.2017.01.025_bb0400) 2016; 24
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Snippet Among membrane receptors, the single-span receptor protein kinases occupy a broad but specific functional niche determined by distinctive features of the...
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SubjectTerms Cell Membrane - chemistry
Cell Membrane - genetics
Cytoskeleton - chemistry
Cytoskeleton - genetics
cytoskeleton remodeling
Dimerization
lipid raft
Membrane Lipids - chemistry
Membrane Lipids - metabolism
Membrane Proteins - chemistry
Membrane Proteins - genetics
Membrane Proteins - metabolism
Protein Conformation
protein-lipid and protein-protein interactions
Receptor Protein-Tyrosine Kinases - chemistry
Receptor Protein-Tyrosine Kinases - genetics
Receptor Protein-Tyrosine Kinases - metabolism
receptor tyrosine kinase
Signal Transduction
single-span membrane protein
Title Conformational transitions and interactions underlying the function of membrane embedded receptor protein kinases
URI https://dx.doi.org/10.1016/j.bbamem.2017.01.025
https://www.ncbi.nlm.nih.gov/pubmed/28131853
https://search.proquest.com/docview/1862938720
Volume 1859
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