메뉴 건너뛰기




Volumn 334, Issue 1, 2015, Pages 2-9

Myosin II isoform co-assembly and differential regulation in mammalian systems

Author keywords

Filament assembly; Isoform; Nonmuscle myosin II

Indexed keywords

MYOSIN II; NM2A PROTEIN; NM2B PROTEIN; PROTEIN; UNCLASSIFIED DRUG; ISOPROTEIN;

EID: 84929272090     PISSN: 00144827     EISSN: 10902422     Source Type: Journal    
DOI: 10.1016/j.yexcr.2015.01.012     Document Type: Review
Times cited : (49)

References (81)
  • 1
    • 0016795902 scopus 로고
    • Phosphorylation of platelet myosin increases actin-activated myosin ATPase activity
    • Adelstein R.S., Conti M.A. Phosphorylation of platelet myosin increases actin-activated myosin ATPase activity. Nature 1975, 256:597-598.
    • (1975) Nature , vol.256 , pp. 597-598
    • Adelstein, R.S.1    Conti, M.A.2
  • 2
    • 84919482922 scopus 로고    scopus 로고
    • Mesenchymal chemotaxis requires selective inactivation of myosin II at the leading edge via a noncanonical PLCgamma/PKCalpha pathway
    • Asokan S.B., Johnson H.E., Rahman A., King S.J., Rotty J.D., Lebedeva I.P., Haugh J.M., Bear J.E. Mesenchymal chemotaxis requires selective inactivation of myosin II at the leading edge via a noncanonical PLCgamma/PKCalpha pathway. Dev. Cell 2014, 31:747-760.
    • (2014) Dev. Cell , vol.31 , pp. 747-760
    • Asokan, S.B.1    Johnson, H.E.2    Rahman, A.3    King, S.J.4    Rotty, J.D.5    Lebedeva, I.P.6    Haugh, J.M.7    Bear, J.E.8
  • 4
    • 21244469821 scopus 로고    scopus 로고
    • Vertebrate nonmuscle myosin II isoforms rescue small interfering RNA-induced defects in COS-7 cell cytokinesis
    • Bao J., Jana S.S., Adelstein R.S. Vertebrate nonmuscle myosin II isoforms rescue small interfering RNA-induced defects in COS-7 cell cytokinesis. J. Biol. Chem. 2005, 280:19594-19599.
    • (2005) J. Biol. Chem. , vol.280 , pp. 19594-19599
    • Bao, J.1    Jana, S.S.2    Adelstein, R.S.3
  • 5
    • 34547573606 scopus 로고    scopus 로고
    • Replacement of nonmuscle myosin II-B with II-A rescues brain but not cardiac defects in mice
    • Bao J., Ma X., Liu C., Adelstein R.S. Replacement of nonmuscle myosin II-B with II-A rescues brain but not cardiac defects in mice. J. Biol. Chem. 2007, 282:22102-22111.
    • (2007) J. Biol. Chem. , vol.282 , pp. 22102-22111
    • Bao, J.1    Ma, X.2    Liu, C.3    Adelstein, R.S.4
  • 6
    • 70350448422 scopus 로고    scopus 로고
    • Myosin II recruitment during cytokinesis independent of centralspindlin-mediated phosphorylation
    • Beach J.R., Egelhoff T.T. Myosin II recruitment during cytokinesis independent of centralspindlin-mediated phosphorylation. J. Biol. Chem. 2009, 284:27377-27383.
    • (2009) J. Biol. Chem. , vol.284 , pp. 27377-27383
    • Beach, J.R.1    Egelhoff, T.T.2
  • 8
    • 82455168277 scopus 로고    scopus 로고
    • Analysis of the role of Ser1/Ser2/Thr9 phosphorylation on myosin II assembly and function in live cells
    • Beach J.R., Licate L.S., Crish J.F., Egelhoff T.T. Analysis of the role of Ser1/Ser2/Thr9 phosphorylation on myosin II assembly and function in live cells. BMC Cell Biol. 2011, 12:52.
    • (2011) BMC Cell Biol. , vol.12 , pp. 52
    • Beach, J.R.1    Licate, L.S.2    Crish, J.F.3    Egelhoff, T.T.4
  • 10
    • 0032502746 scopus 로고    scopus 로고
    • Transcriptional regulation of the human nonmuscle myosin II heavy chain-A gene. Identification of three clustered cis-elements in intron-1 which modulate transcription in a cell type- and differentiation state-dependent manner
    • Beohar N., Kawamoto S. Transcriptional regulation of the human nonmuscle myosin II heavy chain-A gene. Identification of three clustered cis-elements in intron-1 which modulate transcription in a cell type- and differentiation state-dependent manner. J. Biol. Chem. 1998, 273:9168-9178.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9168-9178
    • Beohar, N.1    Kawamoto, S.2
  • 11
    • 2942587231 scopus 로고    scopus 로고
    • Myosin-dependent junction remodelling controls planar cell intercalation and axis elongation
    • Bertet C., Sulak L., Lecuit T. Myosin-dependent junction remodelling controls planar cell intercalation and axis elongation. Nature 2004, 429:667-671.
    • (2004) Nature , vol.429 , pp. 667-671
    • Bertet, C.1    Sulak, L.2    Lecuit, T.3
  • 12
    • 84887830790 scopus 로고    scopus 로고
    • Characterization of three full-length human nonmuscle myosin II paralogs
    • Billington N., Wang A., Mao J., Adelstein R.S., Sellers J.R. Characterization of three full-length human nonmuscle myosin II paralogs. J. Biol. Chem. 2013, 288:33398-33410.
    • (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
  • 13
    • 79953202923 scopus 로고    scopus 로고
    • Temporal spatial expression and function of non-muscle myosin II isoforms IIA and IIB in scar remodeling
    • Bond J.E., Ho T.Q., Selim M.A., Hunter C.L., Bowers E.V., Levinson H. Temporal spatial expression and function of non-muscle myosin II isoforms IIA and IIB in scar remodeling. Lab. Investig. 2011, 91:499-508.
    • (2011) Lab. Investig. , vol.91 , pp. 499-508
    • Bond, J.E.1    Ho, T.Q.2    Selim, M.A.3    Hunter, C.L.4    Bowers, E.V.5    Levinson, H.6
  • 14
    • 63049120202 scopus 로고    scopus 로고
    • Multiple regulatory steps control mammalian nonmuscle myosin II assembly in live cells
    • Breckenridge M.T., Dulyaninova N.G., Egelhoff T.T. Multiple regulatory steps control mammalian nonmuscle myosin II assembly in live cells. Mol. Biol. Cell 2009, 20:338-347.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 338-347
    • Breckenridge, M.T.1    Dulyaninova, N.G.2    Egelhoff, T.T.3
  • 16
    • 11244259124 scopus 로고    scopus 로고
    • IRF-2 is involved in up-regulation of nonmuscle myosin heavy chain II-A gene expression during phorbol ester-induced promyelocytic HL-60 differentiation
    • Chung M.C., Kawamoto S. IRF-2 is involved in up-regulation of nonmuscle myosin heavy chain II-A gene expression during phorbol ester-induced promyelocytic HL-60 differentiation. J. Biol. Chem. 2004, 279:56042-56052.
    • (2004) J. Biol. Chem. , vol.279 , pp. 56042-56052
    • Chung, M.C.1    Kawamoto, S.2
  • 17
    • 0035979375 scopus 로고    scopus 로고
    • TFEC can function as a transcriptional activator of the nonmuscle myosin II heavy chain-A gene in transfected cells
    • Chung M.C., Kim H.K., Kawamoto S. TFEC can function as a transcriptional activator of the nonmuscle myosin II heavy chain-A gene in transfected cells. Biochemistry 2001, 40:8887-8897.
    • (2001) Biochemistry , vol.40 , pp. 8887-8897
    • Chung, M.C.1    Kim, H.K.2    Kawamoto, S.3
  • 18
    • 4744364577 scopus 로고    scopus 로고
    • Defects in cell adhesion and the visceral endoderm following ablation of nonmuscle myosin heavy chain II-A in mice
    • Conti M.A., Even-Ram S., Liu C., Yamada K.M., Adelstein R.S. Defects in cell adhesion and the visceral endoderm following ablation of nonmuscle myosin heavy chain II-A in mice. J. Biol. Chem. 2004, 279:41263-41266.
    • (2004) J. Biol. Chem. , vol.279 , pp. 41263-41266
    • Conti, M.A.1    Even-Ram, S.2    Liu, C.3    Yamada, K.M.4    Adelstein, R.S.5
  • 19
    • 84860852501 scopus 로고    scopus 로고
    • S100P dissociates myosin IIA filaments and focal adhesion sites to reduce cell adhesion and enhance cell migration
    • Du M., Wang G., Ismail T.M., Gross S., Fernig D.G., Barraclough R., Rudland P.S. S100P dissociates myosin IIA filaments and focal adhesion sites to reduce cell adhesion and enhance cell migration. J. Biol. Chem. 2012, 287:15330-15344.
    • (2012) J. Biol. Chem. , vol.287 , pp. 15330-15344
    • Du, M.1    Wang, G.2    Ismail, T.M.3    Gross, S.4    Fernig, D.G.5    Barraclough, R.6    Rudland, P.S.7
  • 20
    • 84919907686 scopus 로고    scopus 로고
    • The heavy chain has its day: regulation of myosin-II assembly
    • Dulyaninova N.G., Bresnick A.R. The heavy chain has its day: regulation of myosin-II assembly. Bioarchitecture 2013, 3:77-85.
    • (2013) Bioarchitecture , vol.3 , pp. 77-85
    • Dulyaninova, N.G.1    Bresnick, A.R.2
  • 21
    • 34547757869 scopus 로고    scopus 로고
    • Myosin-IIA heavy-chain phosphorylation regulates the motility of MDA-MB-231 carcinoma cells
    • Dulyaninova N.G., House R.P., Betapudi V., Bresnick A.R. Myosin-IIA heavy-chain phosphorylation regulates the motility of MDA-MB-231 carcinoma cells. Mol. Biol. Cell 2007, 18:3144-3155.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3144-3155
    • Dulyaninova, N.G.1    House, R.P.2    Betapudi, V.3    Bresnick, A.R.4
  • 22
    • 18244385740 scopus 로고    scopus 로고
    • Regulation of myosin-IIA assembly and Mts1 binding by heavy chain phosphorylation
    • Dulyaninova N.G., Malashkevich V.N., Almo S.C., Bresnick A.R. Regulation of myosin-IIA assembly and Mts1 binding by heavy chain phosphorylation. Biochemistry 2005, 44:6867-6876.
    • (2005) Biochemistry , vol.44 , pp. 6867-6876
    • Dulyaninova, N.G.1    Malashkevich, V.N.2    Almo, S.C.3    Bresnick, A.R.4
  • 24
    • 0027372314 scopus 로고
    • Dictyostelium myosin heavy chain phosphorylation sites regulate myosin filament assembly and localization in vivo
    • Egelhoff T.T., Lee R.J., Spudich J.A. Dictyostelium myosin heavy chain phosphorylation sites regulate myosin filament assembly and localization in vivo. Cell 1993, 75:363-371.
    • (1993) Cell , vol.75 , pp. 363-371
    • Egelhoff, T.T.1    Lee, R.J.2    Spudich, J.A.3
  • 26
    • 84859475063 scopus 로고    scopus 로고
    • Time-lapse two-color 3D imaging of live cells with doubled resolution using structured illumination
    • Fiolka R., Shao L., Rego E.H., Davidson M.W., Gustafsson M.G. Time-lapse two-color 3D imaging of live cells with doubled resolution using structured illumination. Proc. Natl. Acad. Sci. USA 2012, 109:5311-5315.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 5311-5315
    • Fiolka, R.1    Shao, L.2    Rego, E.H.3    Davidson, M.W.4    Gustafsson, M.G.5
  • 27
    • 29044448970 scopus 로고    scopus 로고
    • Nonmuscle myosin II generates forces that transmit tension and drive contraction in multiple tissues during dorsal closure
    • Franke J.D., Montague R.A., Kiehart D.P. Nonmuscle myosin II generates forces that transmit tension and drive contraction in multiple tissues during dorsal closure. Curr. Biol. 2005, 15:2208-2221.
    • (2005) Curr. Biol. , vol.15 , pp. 2208-2221
    • Franke, J.D.1    Montague, R.A.2    Kiehart, D.P.3
  • 32
    • 4444303564 scopus 로고    scopus 로고
    • Role of protein phosphatase type 1 in contractile functions: myosin phosphatase
    • Hartshorne D.J., Ito M., Erdodi F. Role of protein phosphatase type 1 in contractile functions: myosin phosphatase. J. Biol. Chem. 2004, 279:37211-37214.
    • (2004) J. Biol. Chem. , vol.279 , pp. 37211-37214
    • Hartshorne, D.J.1    Ito, M.2    Erdodi, F.3
  • 33
    • 0018093924 scopus 로고
    • Evidence for a cyclic nucleotide-dependant phosphorylation of retinal myosin
    • Hesketh J.E., Virmaux N., Mandel P. Evidence for a cyclic nucleotide-dependant phosphorylation of retinal myosin. FEBS Lett. 1978, 94:357-360.
    • (1978) FEBS Lett. , vol.94 , pp. 357-360
    • Hesketh, J.E.1    Virmaux, N.2    Mandel, P.3
  • 34
    • 80052063518 scopus 로고    scopus 로고
    • Myosin IIb activity and phosphorylation status determines dendritic spine and post-synaptic density morphology
    • Hodges J.L., Newell-Litwa K., Asmussen H., Vicente-Manzanares M., Horwitz A.R. Myosin IIb activity and phosphorylation status determines dendritic spine and post-synaptic density morphology. PLoS One 2011, 6:e24149.
    • (2011) PLoS One , vol.6 , pp. e24149
    • Hodges, J.L.1    Newell-Litwa, K.2    Asmussen, H.3    Vicente-Manzanares, M.4    Horwitz, A.R.5
  • 35
    • 0023655566 scopus 로고
    • Phosphorylation of the 20,000-dalton light chain of smooth muscle myosin by the calcium-activated, phospholipid-dependent protein kinase. Phosphorylation sites and effects of phosphorylation
    • Ikebe M., Hartshorne D.J., Elzinga M. Phosphorylation of the 20,000-dalton light chain of smooth muscle myosin by the calcium-activated, phospholipid-dependent protein kinase. Phosphorylation sites and effects of phosphorylation. J. Biol. Chem. 1987, 262:9569-9573.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9569-9573
    • Ikebe, M.1    Hartshorne, D.J.2    Elzinga, M.3
  • 36
    • 19644382735 scopus 로고    scopus 로고
    • Differential roles for actin polymerization and a myosin II motor in assembly of the epithelial apical junctional complex
    • Ivanov A.I., Hunt D., Utech M., Nusrat A., Parkos C.A. Differential roles for actin polymerization and a myosin II motor in assembly of the epithelial apical junctional complex. Mol. Biol. Cell 2005, 16:2636-2650.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2636-2650
    • Ivanov, A.I.1    Hunt, D.2    Utech, M.3    Nusrat, A.4    Parkos, C.A.5
  • 37
    • 35548961325 scopus 로고    scopus 로고
    • Mammalian SEPT2 is required for scaffolding nonmuscle myosin II and its kinases
    • Joo E., Surka M.C., Trimble W.S. Mammalian SEPT2 is required for scaffolding nonmuscle myosin II and its kinases. Dev. Cell 2007, 13:677-690.
    • (2007) Dev. Cell , vol.13 , pp. 677-690
    • Joo, E.1    Surka, M.C.2    Trimble, W.S.3
  • 38
    • 0026029783 scopus 로고
    • Chicken nonmuscle myosin heavy chains: differential expression of two mRNAs and evidence for two different polypeptides
    • Kawamoto S., Adelstein R.S. Chicken nonmuscle myosin heavy chains: differential expression of two mRNAs and evidence for two different polypeptides. J. Cell Biol. 1991, 112:915-924.
    • (1991) J. Cell Biol. , vol.112 , pp. 915-924
    • Kawamoto, S.1    Adelstein, R.S.2
  • 39
    • 0029782819 scopus 로고    scopus 로고
    • Xenopus nonmuscle myosin heavy chain isoforms have different subcellular localizations and enzymatic activities
    • Kelley C.A., Sellers J.R., Gard D.L., Bui D., Adelstein R.S., Baines I.C. Xenopus nonmuscle myosin heavy chain isoforms have different subcellular localizations and enzymatic activities. J. Cell Biol. 1996, 134:675-687.
    • (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
  • 40
    • 84859990136 scopus 로고    scopus 로고
    • Crystal structure of the S100A4-nonmuscle myosin IIA tail fragment complex reveals an asymmetric target binding mechanism
    • Kiss B., Duelli A., Radnai L., Kekesi K.A., Katona G., Nyitray L. Crystal structure of the S100A4-nonmuscle myosin IIA tail fragment complex reveals an asymmetric target binding mechanism. Proc. Natl. Acad. Sci. USA 2012, 109:6048-6053.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 6048-6053
    • Kiss, B.1    Duelli, A.2    Radnai, L.3    Kekesi, K.A.4    Katona, G.5    Nyitray, L.6
  • 41
    • 0031711721 scopus 로고    scopus 로고
    • Cytoplasmic dynamics of myosin IIA and IIB: spatial "sorting" of isoforms in locomoting cells
    • Kolega J. Cytoplasmic dynamics of myosin IIA and IIB: spatial "sorting" of isoforms in locomoting cells. J. Cell Sci. 1998, 111(Pt 15):2085-2095.
    • (1998) J. Cell Sci. , vol.111 , pp. 2085-2095
    • Kolega, J.1
  • 42
    • 37049018419 scopus 로고    scopus 로고
    • The phosphorylation of myosin II at the Ser1 and Ser2 is critical for normal platelet-derived growth factor induced reorganization of myosin filaments
    • Komatsu S., Ikebe M. The phosphorylation of myosin II at the Ser1 and Ser2 is critical for normal platelet-derived growth factor induced reorganization of myosin filaments. Mol. Biol. Cell 2007, 18:5081-5090.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 5081-5090
    • Komatsu, S.1    Ikebe, M.2
  • 43
    • 84894363564 scopus 로고    scopus 로고
    • A role for myosin II in mammalian mitochondrial fission
    • Korobova F., Gauvin T.J., Higgs H.N. A role for myosin II in mammalian mitochondrial fission. Curr. Biol. 2014, 24:409-414.
    • (2014) Curr. Biol. , vol.24 , pp. 409-414
    • Korobova, F.1    Gauvin, T.J.2    Higgs, H.N.3
  • 44
    • 79953303384 scopus 로고    scopus 로고
    • Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for beta-Pix in negative regulation of focal adhesion maturation
    • Kuo J.C., Han X., Hsiao C.T., Yates J.R., Waterman C.M. Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for beta-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 2011, 13:383-393.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 383-393
    • Kuo, J.C.1    Han, X.2    Hsiao, C.T.3    Yates, J.R.4    Waterman, C.M.5
  • 45
    • 84882749769 scopus 로고    scopus 로고
    • Arf guanine nucleotide-exchange factors BIG1 and BIG2 regulate nonmuscle myosin IIA activity by anchoring myosin phosphatase complex
    • Le K., Li C.C., Ye G., Moss J., Vaughan M. Arf guanine nucleotide-exchange factors BIG1 and BIG2 regulate nonmuscle myosin IIA activity by anchoring myosin phosphatase complex. Proc. Natl. Acad. Sci. USA 2013, 110:E3162-E3170.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. E3162-E3170
    • Le, K.1    Li, C.C.2    Ye, G.3    Moss, J.4    Vaughan, M.5
  • 46
    • 0028007599 scopus 로고
    • Molecular genetic truncation analysis of filament assembly and phosphorylation domains of Dictyostelium myosin heavy chain
    • Lee R.J., Egelhoff T.T., Spudich J.A. Molecular genetic truncation analysis of filament assembly and phosphorylation domains of Dictyostelium myosin heavy chain. J. Cell Sci. 1994, 107:2875-2886.
    • (1994) J. Cell Sci. , vol.107 , pp. 2875-2886
    • Lee, R.J.1    Egelhoff, T.T.2    Spudich, J.A.3
  • 47
    • 33744931917 scopus 로고    scopus 로고
    • The S100A4 metastasis factor regulates cellular motility via a direct interaction with myosin-IIA
    • Li Z.H., Bresnick A.R. The S100A4 metastasis factor regulates cellular motility via a direct interaction with myosin-IIA. Cancer Res. 2006, 66:5173-5180.
    • (2006) Cancer Res. , vol.66 , pp. 5173-5180
    • Li, Z.H.1    Bresnick, A.R.2
  • 49
    • 0344198168 scopus 로고    scopus 로고
    • Mts1 regulates the assembly of nonmuscle myosin-IIA
    • Li Z.H., Spektor A., Varlamova O., Bresnick A.R. Mts1 regulates the assembly of nonmuscle myosin-IIA. Biochemistry 2003, 42:14258-14266.
    • (2003) Biochemistry , vol.42 , pp. 14258-14266
    • Li, Z.H.1    Spektor, A.2    Varlamova, O.3    Bresnick, A.R.4
  • 50
    • 0025148218 scopus 로고
    • Replacement of threonine residues by serine and alanine in a phosphorylatable heavy chain fragment of Dictyostelium myosin II
    • Luck-Vielmetter D., Schleicher M., Grabatin B., Wippler J., Gerisch G. Replacement of threonine residues by serine and alanine in a phosphorylatable heavy chain fragment of Dictyostelium myosin II. FEBS Lett. 1990, 269:239-243.
    • (1990) FEBS Lett. , vol.269 , pp. 239-243
    • Luck-Vielmetter, D.1    Schleicher, M.2    Grabatin, B.3    Wippler, J.4    Gerisch, G.5
  • 52
    • 40849097955 scopus 로고    scopus 로고
    • Myosin phosphatase target subunit: many roles in cell function
    • Matsumura F., Hartshorne D.J. Myosin phosphatase target subunit: many roles in cell function. Biochem. Res. Commun. 2008, 369:149-156.
    • (2008) Biochem. Res. Commun. , vol.369 , pp. 149-156
    • Matsumura, F.1    Hartshorne, D.J.2
  • 54
    • 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
    • Mitsuhashi M., Sakata H., Kinjo M., Yazawa M., Takahashi M. Dynamic assembly properties of nonmuscle myosin II isoforms revealed by combination of fluorescence correlation spectroscopy and fluorescence cross-correlation spectroscopy. J. Biochem. 2011, 149:253-263.
    • (2011) J. Biochem. , vol.149 , pp. 253-263
    • Mitsuhashi, M.1    Sakata, H.2    Kinjo, M.3    Yazawa, M.4    Takahashi, M.5
  • 55
    • 0017410520 scopus 로고
    • Phosphorylation of fibroblast myosin
    • Muhlrad A., Oplatka A. Phosphorylation of fibroblast myosin. FEBS Lett. 1977, 77:37-40.
    • (1977) FEBS Lett. , vol.77 , pp. 37-40
    • Muhlrad, A.1    Oplatka, A.2
  • 56
    • 0026004295 scopus 로고
    • Studies on the distribution of cellular myosin with antibodies to isoform-specific synthetic peptides
    • Murakami N., Mehta P., Elzinga M. Studies on the distribution of cellular myosin with antibodies to isoform-specific synthetic peptides. FEBS Lett. 1991, 278:23-25.
    • (1991) FEBS Lett. , vol.278 , pp. 23-25
    • Murakami, N.1    Mehta, P.2    Elzinga, M.3
  • 57
    • 0028825025 scopus 로고
    • Phospholipid binding, phosphorylation by protein kinase C, and filament assembly of the COOH terminal heavy chain fragments of nonmuscle myosin II isoforms MIIA and MIIB
    • Murakami N., Singh S.S., Chauhan V.P., Elzinga M. Phospholipid binding, phosphorylation by protein kinase C, and filament assembly of the COOH terminal heavy chain fragments of nonmuscle myosin II isoforms MIIA and MIIB. Biochemistry 1995, 34:16046-16055.
    • (1995) Biochemistry , vol.34 , pp. 16046-16055
    • Murakami, N.1    Singh, S.S.2    Chauhan, V.P.3    Elzinga, M.4
  • 60
    • 0016776250 scopus 로고
    • Electron microscopy of synthetic myosin filaments. Evidence for cross-bridge. Flexibility and copolymer formation
    • Pollard T.D. Electron microscopy of synthetic myosin filaments. Evidence for cross-bridge. Flexibility and copolymer formation. J. Cell Biol. 1975, 67:93-104.
    • (1975) J. Cell Biol. , vol.67 , pp. 93-104
    • Pollard, T.D.1
  • 61
    • 78650486924 scopus 로고    scopus 로고
    • Multiple tail domain interactions stabilize nonmuscle myosin II bipolar filaments
    • Ricketson D., Johnston C.A., Prehoda K.E. Multiple tail domain interactions stabilize nonmuscle myosin II bipolar filaments. Proc. Natl. Acad. Sci. USA 2010, 107:20964-20969.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 20964-20969
    • Ricketson, D.1    Johnston, C.A.2    Prehoda, K.E.3
  • 62
    • 41949095658 scopus 로고    scopus 로고
    • MHC-IIB filament assembly and cellular localization are governed by the rod net charge
    • Rosenberg M., Straussman R., Ben-Ya[U+05F3]acov A., Ronen D., Ravid S. MHC-IIB filament assembly and cellular localization are governed by the rod net charge. PLoS One 2008, 3:e1496.
    • (2008) PLoS One , vol.3 , pp. e1496
    • Rosenberg, M.1    Straussman, R.2    Ben-Ya'acov, A.3    Ronen, D.4    Ravid, S.5
  • 63
    • 58049220355 scopus 로고    scopus 로고
    • The C-terminal tail region of nonmuscle myosin II directs isoform-specific distribution in migrating cells
    • Sandquist J.C., Means A.R. The C-terminal tail region of nonmuscle myosin II directs isoform-specific distribution in migrating cells. Mol. Biol. Cell 2008, 19:5156-5167.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 5156-5167
    • Sandquist, J.C.1    Means, A.R.2
  • 64
    • 33845993635 scopus 로고    scopus 로고
    • Rho kinase differentially regulates phosphorylation of nonmuscle myosin II isoforms A and B during cell rounding and migration
    • Sandquist J.C., Swenson K.I., Demali K.A., Burridge K., Means A.R. Rho kinase differentially regulates phosphorylation of nonmuscle myosin II isoforms A and B during cell rounding and migration. J. Biol. Chem. 2006, 281:35873-35883.
    • (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
  • 65
    • 33947135876 scopus 로고    scopus 로고
    • Two regions of the tail are necessary for the isoform-specific functions of nonmuscle myosin IIB
    • Sato M.K., Takahashi M., Yazawa M. Two regions of the tail are necessary for the isoform-specific functions of nonmuscle myosin IIB. Mol. Biol. Cell 2007, 18:1009-1017.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 1009-1017
    • Sato, M.K.1    Takahashi, M.2    Yazawa, M.3
  • 66
  • 67
    • 0030071619 scopus 로고    scopus 로고
    • Sequences in the myosin II tail required for self-association
    • Shoffner J.D., De L.A. Sequences in the myosin II tail required for self-association. Biochem. Res. Commun. 1996, 218:860-864.
    • (1996) Biochem. Res. Commun. , vol.218 , pp. 860-864
    • Shoffner, J.D.1    De, L.A.2
  • 68
    • 84908053868 scopus 로고    scopus 로고
    • Endogenous species of mammalian nonmuscle myosin IIA and IIB include activated monomers and heteropolymers
    • Shutova M.S., Spessott W.A., Giraudo C.G., Svitkina T. Endogenous species of mammalian nonmuscle myosin IIA and IIB include activated monomers and heteropolymers. Curr. Biol. 2014, 24:1958-1968.
    • (2014) Curr. Biol. , vol.24 , pp. 1958-1968
    • Shutova, M.S.1    Spessott, W.A.2    Giraudo, C.G.3    Svitkina, T.4
  • 71
    • 11144333618 scopus 로고    scopus 로고
    • Anillin binds nonmuscle myosin II and regulates the contractile ring
    • Straight A.F., Field C.M., Mitchison T.J. Anillin binds nonmuscle myosin II and regulates the contractile ring. Mol. Biol. Cell 2005, 16:193-201.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 193-201
    • Straight, A.F.1    Field, C.M.2    Mitchison, T.J.3
  • 72
    • 26244466046 scopus 로고    scopus 로고
    • Skip residues and charge interactions in myosin II coiled-coils: implications for molecular packing
    • Straussman R., Squire J.M., Ben-Ya[U+05F3]acov A., Ravid S. Skip residues and charge interactions in myosin II coiled-coils: implications for molecular packing. J. Mol. Biol. 2005, 353:613-628.
    • (2005) J. Mol. Biol. , vol.353 , pp. 613-628
    • Straussman, R.1    Squire, J.M.2    Ben-Ya'acov, A.3    Ravid, S.4
  • 73
    • 0022294386 scopus 로고
    • Myosin light chain kinases and myosin phosphorylation in skeletal muscle
    • Stull J.T., Nunnally M.H., Moore R.L., Blumenthal D.K. Myosin light chain kinases and myosin phosphorylation in skeletal muscle. Adv. Enzyme Regul. 1985, 23:123-140.
    • (1985) Adv. Enzyme Regul. , vol.23 , pp. 123-140
    • Stull, J.T.1    Nunnally, M.H.2    Moore, R.L.3    Blumenthal, D.K.4
  • 74
    • 0028070116 scopus 로고
    • Involvement of S100-related calcium-binding protein pEL98 (or mts1) in cell motility and tumor cell invasion
    • Takenaga K., Nakamura Y., Endo H., Sakiyama S. Involvement of S100-related calcium-binding protein pEL98 (or mts1) in cell motility and tumor cell invasion. Jpn. J. Cancer Res. 1994, 85:831-839.
    • (1994) Jpn. J. Cancer Res. , vol.85 , pp. 831-839
    • Takenaga, K.1    Nakamura, Y.2    Endo, H.3    Sakiyama, S.4
  • 75
    • 84863113109 scopus 로고    scopus 로고
    • Actin stress fibers - assembly, dynamics and biological roles
    • Tojkander S., Gateva G., Lappalainen P. Actin stress fibers - assembly, dynamics and biological roles. J. Cell Sci. 2012, 125:1855-1864.
    • (2012) J. Cell Sci. , vol.125 , pp. 1855-1864
    • Tojkander, S.1    Gateva, G.2    Lappalainen, P.3
  • 76
    • 0024297036 scopus 로고
    • Identification of two phosphorylated threonines in the tail region of Dictyostelium myosin II
    • Vaillancourt J.P., Lyons C., Cote G.P. Identification of two phosphorylated threonines in the tail region of Dictyostelium myosin II. J. Biol. Chem. 1988, 263:10082-10087.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10082-10087
    • Vaillancourt, J.P.1    Lyons, C.2    Cote, G.P.3
  • 77
    • 79955516270 scopus 로고    scopus 로고
    • Myosin IIA/IIB restrict adhesive and protrusive signaling to generate front-back polarity in migrating cells
    • Vicente-Manzanares M., Newell-Litwa K., Bachir A.I., Whitmore L.A., Horwitz A.R. Myosin IIA/IIB restrict adhesive and protrusive signaling to generate front-back polarity in migrating cells. J. Cell Biol. 2011, 193:381-396.
    • (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
  • 78
    • 80053367989 scopus 로고    scopus 로고
    • Distinct and redundant roles of the non-muscle myosin II isoforms and functional domains
    • Wang A., Ma X., Conti M.A., Adelstein R.S. Distinct and redundant roles of the non-muscle myosin II isoforms and functional domains. Biochem. Trans. 2011, 39:1131-1135.
    • (2011) Biochem. Trans. , vol.39 , pp. 1131-1135
    • Wang, A.1    Ma, X.2    Conti, M.A.3    Adelstein, R.S.4
  • 80
    • 0042347443 scopus 로고    scopus 로고
    • Kinetic mechanism of non-muscle myosin IIB: functional adaptations for tension generation and maintenance
    • Wang F., Kovacs M., Hu A., Limouze J., Harvey E.V., Sellers J.R. Kinetic mechanism of non-muscle myosin IIB: functional adaptations for tension generation and maintenance. J. Biol. Chem. 2003, 278:27439-27448.
    • (2003) J. Biol. Chem. , vol.278 , pp. 27439-27448
    • Wang, F.1    Kovacs, M.2    Hu, A.3    Limouze, J.4    Harvey, E.V.5    Sellers, J.R.6
  • 81
    • 16344390935 scopus 로고    scopus 로고
    • A GIT1/PIX/Rac/PAK signaling module regulates spine morphogenesis and synapse formation through MLC
    • Zhang H., Webb D.J., Asmussen H., Niu S., Horwitz A.F. A GIT1/PIX/Rac/PAK signaling module regulates spine morphogenesis and synapse formation through MLC. J. Neurosci. 2005, 25:3379-3388.
    • (2005) J. Neurosci. , vol.25 , pp. 3379-3388
    • Zhang, H.1    Webb, D.J.2    Asmussen, H.3    Niu, S.4    Horwitz, A.F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.