메뉴 건너뛰기




Volumn 24, Issue 17, 2014, Pages 1958-1968

Endogenous species of mammalian nonmuscle myosin IIA and IIB include activated monomers and heteropolymers

Author keywords

[No Author keywords available]

Indexed keywords

ISOPROTEIN; MYOSIN IIA; MYOSIN IIB;

EID: 84908053868     PISSN: 09609822     EISSN: 18790445     Source Type: Journal    
DOI: 10.1016/j.cub.2014.07.070     Document Type: Article
Times cited : (99)

References (48)
  • 1
    • 80053367989 scopus 로고    scopus 로고
    • Distinct and redundant roles of the non-muscle myosin II isoforms and functional domains
    • A. Wang, X. Ma, M.A. Conti, and R.S. Adelstein Distinct and redundant roles of the non-muscle myosin II isoforms and functional domains Biochem. Soc. Trans. 39 2011 1131 1135
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 1131-1135
    • Wang, A.1    Ma, X.2    Conti, M.A.3    Adelstein, R.S.4
  • 7
    • 84894363564 scopus 로고    scopus 로고
    • A role for myosin II in mammalian mitochondrial fission
    • F. Korobova, T.J. Gauvin, and H.N. Higgs A role for myosin II in mammalian mitochondrial fission Curr. Biol. 24 2014 409 414
    • (2014) Curr. Biol. , vol.24 , pp. 409-414
    • Korobova, F.1    Gauvin, T.J.2    Higgs, H.N.3
  • 8
    • 0024576739 scopus 로고
    • Effect of multiple phosphorylations of smooth muscle and cytoplasmic myosins on movement in an in vitro motility assay
    • S. Umemoto, A.R. Bengur, and J.R. Sellers Effect of multiple phosphorylations of smooth muscle and cytoplasmic myosins on movement in an in vitro motility assay J. Biol. Chem. 264 1989 1431 1436
    • (1989) J. Biol. Chem. , vol.264 , pp. 1431-1436
    • Umemoto, S.1    Bengur, A.R.2    Sellers, J.R.3
  • 9
    • 0016826285 scopus 로고
    • Human platelet myosin. II. in vitro assembly and structure of myosin filaments
    • R. Niederman, and T.D. Pollard Human platelet myosin. II. In vitro assembly and structure of myosin filaments J. Cell Biol. 67 1975 72 92
    • (1975) J. Cell Biol. , vol.67 , pp. 72-92
    • Niederman, R.1    Pollard, T.D.2
  • 10
    • 84863767949 scopus 로고    scopus 로고
    • Functions of nonmuscle myosin II in assembly of the cellular contractile system
    • M. Shutova, C. Yang, J.M. Vasiliev, and T. Svitkina Functions of nonmuscle myosin II in assembly of the cellular contractile system PLoS ONE 7 2012 e40814
    • (2012) PLoS ONE , vol.7 , pp. 40814
    • Shutova, M.1    Yang, C.2    Vasiliev, J.M.3    Svitkina, T.4
  • 11
    • 0030777766 scopus 로고    scopus 로고
    • Analysis of the actin-myosin II system in fish epidermal keratocytes: Mechanism of cell body translocation
    • T.M. Svitkina, A.B. Verkhovsky, K.M. McQuade, and G.G. Borisy Analysis of the actin-myosin II system in fish epidermal keratocytes: mechanism of cell body translocation J. Cell Biol. 139 1997 397 415
    • (1997) J. Cell Biol. , vol.139 , pp. 397-415
    • Svitkina, T.M.1    Verkhovsky, A.B.2    McQuade, K.M.3    Borisy, G.G.4
  • 12
    • 0028818253 scopus 로고
    • Myosin II filament assemblies in the active lamella of fibroblasts: Their morphogenesis and role in the formation of actin filament bundles
    • A.B. Verkhovsky, T.M. Svitkina, and G.G. Borisy Myosin II filament assemblies in the active lamella of fibroblasts: their morphogenesis and role in the formation of actin filament bundles J. Cell Biol. 131 1995 989 1002
    • (1995) J. Cell Biol. , vol.131 , pp. 989-1002
    • Verkhovsky, A.B.1    Svitkina, T.M.2    Borisy, G.G.3
  • 13
    • 0027259061 scopus 로고
    • Gradients in the concentration and assembly of myosin II in living fibroblasts during locomotion and fiber transport
    • J. Kolega, and D.L. Taylor Gradients in the concentration and assembly of myosin II in living fibroblasts during locomotion and fiber transport Mol. Biol. Cell 4 1993 819 836
    • (1993) Mol. Biol. Cell , vol.4 , pp. 819-836
    • Kolega, J.1    Taylor, D.L.2
  • 14
    • 63049120202 scopus 로고    scopus 로고
    • Multiple regulatory steps control mammalian nonmuscle myosin II assembly in live cells
    • M.T. Breckenridge, N.G. Dulyaninova, and T.T. Egelhoff Multiple regulatory steps control mammalian nonmuscle myosin II assembly in live cells Mol. Biol. Cell 20 2009 338 347
    • (2009) Mol. Biol. Cell , vol.20 , pp. 338-347
    • Breckenridge, M.T.1    Dulyaninova, N.G.2    Egelhoff, T.T.3
  • 15
    • 0344012487 scopus 로고    scopus 로고
    • Asymmetric distribution of myosin IIB in migrating endothelial cells is regulated by a rho-dependent kinase and contributes to tail retraction
    • J. Kolega Asymmetric distribution of myosin IIB in migrating endothelial cells is regulated by a rho-dependent kinase and contributes to tail retraction Mol. Biol. Cell 14 2003 4745 4757
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4745-4757
    • Kolega, J.1
  • 16
    • 0027999246 scopus 로고
    • Differential localization of myosin-II isozymes in human cultured cells and blood cells
    • P. Maupin, C.L. Phillips, R.S. Adelstein, and T.D. Pollard Differential localization of myosin-II isozymes in human cultured cells and blood cells J. Cell Sci. 107 1994 3077 3090
    • (1994) J. Cell Sci. , vol.107 , pp. 3077-3090
    • Maupin, P.1    Phillips, C.L.2    Adelstein, R.S.3    Pollard, T.D.4
  • 17
    • 79955516270 scopus 로고    scopus 로고
    • Myosin IIA/IIB restrict adhesive and protrusive signaling to generate front-back polarity in migrating cells
    • M. Vicente-Manzanares, K. Newell-Litwa, A.I. Bachir, L.A. Whitmore, and A.R. Horwitz Myosin IIA/IIB restrict adhesive and protrusive signaling to generate front-back polarity in migrating cells J. Cell Biol. 193 2011 381 396
    • (2011) J. Cell Biol. , vol.193 , pp. 381-396
    • Vicente-Manzanares, M.1    Newell-Litwa, K.2    Bachir, A.I.3    Whitmore, L.A.4    Horwitz, A.R.5
  • 18
    • 0016776250 scopus 로고
    • Electron microscopy of synthetic myosin filaments. Evidence for cross-bridge. Flexibility and copolymer formation
    • T.D. Pollard Electron microscopy of synthetic myosin filaments. Evidence for cross-bridge. Flexibility and copolymer formation J. Cell Biol. 67 1975 93 104
    • (1975) J. Cell Biol. , vol.67 , pp. 93-104
    • Pollard, T.D.1
  • 19
    • 79952285028 scopus 로고    scopus 로고
    • Dynamic assembly properties of nonmuscle myosin II isoforms revealed by combination of fluorescence correlation spectroscopy and fluorescence cross-correlation spectroscopy
    • M. Mitsuhashi, H. Sakata, M. Kinjo, M. Yazawa, and M. Takahashi Dynamic assembly properties of nonmuscle myosin II isoforms revealed by combination of fluorescence correlation spectroscopy and fluorescence cross-correlation spectroscopy J. Biochem. 149 2011 253 263
    • (2011) J. Biochem. , vol.149 , pp. 253-263
    • Mitsuhashi, M.1    Sakata, H.2    Kinjo, M.3    Yazawa, M.4    Takahashi, M.5
  • 20
    • 70350448422 scopus 로고    scopus 로고
    • Myosin II recruitment during cytokinesis independent of centralspindlin-mediated phosphorylation
    • J.R. Beach, and T.T. Egelhoff Myosin II recruitment during cytokinesis independent of centralspindlin-mediated phosphorylation J. Biol. Chem. 284 2009 27377 27383
    • (2009) J. Biol. Chem. , vol.284 , pp. 27377-27383
    • Beach, J.R.1    Egelhoff, T.T.2
  • 22
    • 82155184487 scopus 로고    scopus 로고
    • Phosphorylation of the myosin IIA tailpiece regulates single myosin IIA molecule association with lytic granules to promote NK-cell cytotoxicity
    • K.B. Sanborn, E.M. Mace, G.D. Rak, A. Difeo, J.A. Martignetti, A. Pecci, J.B. Bussel, R. Favier, and J.S. Orange Phosphorylation of the myosin IIA tailpiece regulates single myosin IIA molecule association with lytic granules to promote NK-cell cytotoxicity Blood 118 2011 5862 5871
    • (2011) Blood , vol.118 , pp. 5862-5871
    • Sanborn, K.B.1    Mace, E.M.2    Rak, G.D.3    Difeo, A.4    Martignetti, J.A.5    Pecci, A.6    Bussel, J.B.7    Favier, R.8    Orange, J.S.9
  • 23
    • 22244458555 scopus 로고    scopus 로고
    • Characterization of myosin-II binding to Golgi stacks in vitro
    • K.R. Fath Characterization of myosin-II binding to Golgi stacks in vitro Cell Motil. Cytoskeleton 60 2005 222 235
    • (2005) Cell Motil. Cytoskeleton , vol.60 , pp. 222-235
    • Fath, K.R.1
  • 24
    • 0031615095 scopus 로고    scopus 로고
    • Correlative light and electron microscopy of the cytoskeleton of cultured cells
    • T.M. Svitkina, and G.G. Borisy Correlative light and electron microscopy of the cytoskeleton of cultured cells Methods Enzymol. 298 1998 570 592
    • (1998) Methods Enzymol. , vol.298 , pp. 570-592
    • Svitkina, T.M.1    Borisy, G.G.2
  • 25
    • 0027524780 scopus 로고
    • Non-sarcomeric mode of myosin II organization in the fibroblast lamellum
    • A.B. Verkhovsky, and G.G. Borisy Non-sarcomeric mode of myosin II organization in the fibroblast lamellum J. Cell Biol. 123 1993 637 652
    • (1993) J. Cell Biol. , vol.123 , pp. 637-652
    • Verkhovsky, A.B.1    Borisy, G.G.2
  • 26
    • 84887830790 scopus 로고    scopus 로고
    • Characterization of three full-length human nonmuscle myosin II paralogs
    • N. Billington, A. Wang, J. Mao, R.S. Adelstein, and J.R. Sellers Characterization of three full-length human nonmuscle myosin II paralogs J. Biol. Chem. 288 2013 33398 33410
    • (2013) J. Biol. Chem. , vol.288 , pp. 33398-33410
    • Billington, N.1    Wang, A.2    Mao, J.3    Adelstein, R.S.4    Sellers, J.R.5
  • 27
    • 84886286196 scopus 로고    scopus 로고
    • Molecular mechanisms of cellular mechanosensing
    • T. Luo, K. Mohan, P.A. Iglesias, and D.N. Robinson Molecular mechanisms of cellular mechanosensing Nat. Mater. 12 2013 1064 1071
    • (2013) Nat. Mater. , vol.12 , pp. 1064-1071
    • Luo, T.1    Mohan, K.2    Iglesias, P.A.3    Robinson, D.N.4
  • 28
    • 18244385740 scopus 로고    scopus 로고
    • Regulation of myosin-IIA assembly and Mts1 binding by heavy chain phosphorylation
    • N.G. Dulyaninova, V.N. Malashkevich, S.C. Almo, and A.R. Bresnick Regulation of myosin-IIA assembly and Mts1 binding by heavy chain phosphorylation Biochemistry 44 2005 6867 6876
    • (2005) Biochemistry , vol.44 , pp. 6867-6876
    • Dulyaninova, N.G.1    Malashkevich, V.N.2    Almo, S.C.3    Bresnick, A.R.4
  • 29
    • 33745625368 scopus 로고    scopus 로고
    • PAK1 and aPKCzeta regulate myosin II-B phosphorylation: A novel signaling pathway regulating filament assembly
    • L. Even-Faitelson, and S. Ravid PAK1 and aPKCzeta regulate myosin II-B phosphorylation: a novel signaling pathway regulating filament assembly Mol. Biol. Cell 17 2006 2869 2881
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2869-2881
    • Even-Faitelson, L.1    Ravid, S.2
  • 31
    • 84864978141 scopus 로고    scopus 로고
    • Nonmuscle myosin II is required for internalization of the epidermal growth factor receptor and modulation of downstream signaling
    • J.H. Kim, A. Wang, M.A. Conti, and R.S. Adelstein Nonmuscle myosin II is required for internalization of the epidermal growth factor receptor and modulation of downstream signaling J. Biol. Chem. 287 2012 27345 27358
    • (2012) J. Biol. Chem. , vol.287 , pp. 27345-27358
    • Kim, J.H.1    Wang, A.2    Conti, M.A.3    Adelstein, R.S.4
  • 32
    • 79551561145 scopus 로고    scopus 로고
    • Association between α4 integrin cytoplasmic tail and non-muscle myosin IIA regulates cell migration
    • L.A. Rivera Rosado, T.A. Horn, S.C. McGrath, R.J. Cotter, and J.T. Yang Association between α4 integrin cytoplasmic tail and non-muscle myosin IIA regulates cell migration J. Cell Sci. 124 2011 483 492
    • (2011) J. Cell Sci. , vol.124 , pp. 483-492
    • Rivera Rosado, L.A.1    Horn, T.A.2    McGrath, S.C.3    Cotter, R.J.4    Yang, J.T.5
  • 33
    • 0029782819 scopus 로고    scopus 로고
    • Xenopus nonmuscle myosin heavy chain isoforms have different subcellular localizations and enzymatic activities
    • C.A. Kelley, J.R. Sellers, D.L. Gard, D. Bui, R.S. Adelstein, and I.C. Baines Xenopus nonmuscle myosin heavy chain isoforms have different subcellular localizations and enzymatic activities J. Cell Biol. 134 1996 675 687
    • (1996) J. Cell Biol. , vol.134 , pp. 675-687
    • Kelley, C.A.1    Sellers, J.R.2    Gard, D.L.3    Bui, D.4    Adelstein, R.S.5    Baines, I.C.6
  • 34
    • 58049220355 scopus 로고    scopus 로고
    • The C-terminal tail region of nonmuscle myosin II directs isoform-specific distribution in migrating cells
    • J.C. Sandquist, and A.R. Means The C-terminal tail region of nonmuscle myosin II directs isoform-specific distribution in migrating cells Mol. Biol. Cell 19 2008 5156 5167
    • (2008) Mol. Biol. Cell , vol.19 , pp. 5156-5167
    • Sandquist, J.C.1    Means, A.R.2
  • 35
    • 33644865885 scopus 로고    scopus 로고
    • Protein kinase Cgamma regulates myosin IIB phosphorylation, cellular localization, and filament assembly
    • M. Rosenberg, and S. Ravid Protein kinase Cgamma regulates myosin IIB phosphorylation, cellular localization, and filament assembly Mol. Biol. Cell 17 2006 1364 1374
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1364-1374
    • Rosenberg, M.1    Ravid, S.2
  • 36
    • 84857217053 scopus 로고    scopus 로고
    • The tumor suppressor Lgl1 regulates NMII-A cellular distribution and focal adhesion morphology to optimize cell migration
    • I. Dahan, A. Yearim, Y. Touboul, and S. Ravid The tumor suppressor Lgl1 regulates NMII-A cellular distribution and focal adhesion morphology to optimize cell migration Mol. Biol. Cell 23 2012 591 601
    • (2012) Mol. Biol. Cell , vol.23 , pp. 591-601
    • Dahan, I.1    Yearim, A.2    Touboul, Y.3    Ravid, S.4
  • 37
    • 0043032436 scopus 로고    scopus 로고
    • Characterization of the metastasis-associated protein, S100A4. Roles of calcium binding and dimerization in cellular localization and interaction with myosin
    • E.J. Kim, and D.M. Helfman Characterization of the metastasis-associated protein, S100A4. Roles of calcium binding and dimerization in cellular localization and interaction with myosin J. Biol. Chem. 278 2003 30063 30073
    • (2003) J. Biol. Chem. , vol.278 , pp. 30063-30073
    • Kim, E.J.1    Helfman, D.M.2
  • 38
    • 33744931917 scopus 로고    scopus 로고
    • The S100A4 metastasis factor regulates cellular motility via a direct interaction with myosin-IIA
    • Z.H. Li, and A.R. Bresnick The S100A4 metastasis factor regulates cellular motility via a direct interaction with myosin-IIA Cancer Res. 66 2006 5173 5180
    • (2006) Cancer Res. , vol.66 , pp. 5173-5180
    • Li, Z.H.1    Bresnick, A.R.2
  • 40
    • 33847354235 scopus 로고    scopus 로고
    • Regulation of protrusion, adhesion dynamics, and polarity by myosins IIA and IIB in migrating cells
    • M. Vicente-Manzanares, J. Zareno, L. Whitmore, C.K. Choi, and A.F. Horwitz Regulation of protrusion, adhesion dynamics, and polarity by myosins IIA and IIB in migrating cells J. Cell Biol. 176 2007 573 580
    • (2007) J. Cell Biol. , vol.176 , pp. 573-580
    • Vicente-Manzanares, M.1    Zareno, J.2    Whitmore, L.3    Choi, C.K.4    Horwitz, A.F.5
  • 41
    • 77649103340 scopus 로고    scopus 로고
    • Myosin II motor proteins with different functions determine the fate of lamellipodia extension during cell spreading
    • V. Betapudi Myosin II motor proteins with different functions determine the fate of lamellipodia extension during cell spreading PLoS ONE 5 2010 e8560
    • (2010) PLoS ONE , vol.5 , pp. 8560
    • Betapudi, V.1
  • 42
    • 33646410929 scopus 로고    scopus 로고
    • Distinct roles of nonmuscle myosin II isoforms in the regulation of MDA-MB-231 breast cancer cell spreading and migration
    • V. Betapudi, L.S. Licate, and T.T. Egelhoff Distinct roles of nonmuscle myosin II isoforms in the regulation of MDA-MB-231 breast cancer cell spreading and migration Cancer Res. 66 2006 4725 4733
    • (2006) Cancer Res. , vol.66 , pp. 4725-4733
    • Betapudi, V.1    Licate, L.S.2    Egelhoff, T.T.3
  • 43
    • 0037144811 scopus 로고    scopus 로고
    • Myosin 1c and myosin IIB serve opposing roles in lamellipodial dynamics of the neuronal growth cone
    • T.J. Diefenbach, V.M. Latham, D. Yimlamai, C.A. Liu, I.M. Herman, and D.G. Jay Myosin 1c and myosin IIB serve opposing roles in lamellipodial dynamics of the neuronal growth cone J. Cell Biol. 158 2002 1207 1217
    • (2002) J. Cell Biol. , vol.158 , pp. 1207-1217
    • Diefenbach, T.J.1    Latham, V.M.2    Yimlamai, D.3    Liu, C.A.4    Herman, I.M.5    Jay, D.G.6
  • 45
    • 33845993635 scopus 로고    scopus 로고
    • Rho kinase differentially regulates phosphorylation of nonmuscle myosin II isoforms A and B during cell rounding and migration
    • J.C. Sandquist, K.I. Swenson, K.A. Demali, K. Burridge, and A.R. Means Rho kinase differentially regulates phosphorylation of nonmuscle myosin II isoforms A and B during cell rounding and migration J. Biol. Chem. 281 2006 35873 35883
    • (2006) J. Biol. Chem. , vol.281 , pp. 35873-35883
    • Sandquist, J.C.1    Swenson, K.I.2    Demali, K.A.3    Burridge, K.4    Means, A.R.5
  • 46
    • 84884823694 scopus 로고    scopus 로고
    • Correlative light and electron microscopy studies of cytoskeletal dynamics
    • Third Edition J.E. Celis, Elsevier Amsterdam
    • T.M. Svitkina, and G.G. Borisy Correlative light and electron microscopy studies of cytoskeletal dynamics Third Edition J.E. Celis, Cell Biology: A Laboratory Handbook Volume 3 2006 Elsevier Amsterdam 277 285
    • (2006) Cell Biology: A Laboratory Handbook , vol.3 , pp. 277-285
    • Svitkina, T.M.1    Borisy, G.G.2
  • 47
    • 33847213114 scopus 로고    scopus 로고
    • Electron microscopic analysis of the leading edge in migrating cells
    • T. Svitkina Electron microscopic analysis of the leading edge in migrating cells Methods Cell Biol. 79 2007 295 319
    • (2007) Methods Cell Biol. , vol.79 , pp. 295-319
    • Svitkina, T.1
  • 48
    • 77950908179 scopus 로고    scopus 로고
    • Imaging cytoskeleton components by electron microscopy
    • T. Svitkina Imaging cytoskeleton components by electron microscopy Methods Mol. Biol. 586 2009 187 206
    • (2009) Methods Mol. Biol. , vol.586 , pp. 187-206
    • Svitkina, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.