메뉴 건너뛰기




Volumn 434, Issue 1, 2011, Pages 171-180

Myosin regulatory light chains are required to maintain the stability of myosin II and cellular integrity

Author keywords

Myosin essential light chain; Myosin heavy chain; Myosin regulatory light chain; Non muscle myosin; Short interfering RNA (siRNA) mediated knockdown

Indexed keywords

MYOSIN HEAVY CHAIN; MYOSIN HEAVY CHAIN 10; MYOSIN HEAVY CHAIN 9; MYOSIN II; MYOSIN LIGHT CHAIN; MYOSIN LIGHT CHAIN 10; MYOSIN LIGHT CHAIN 12A; MYOSIN LIGHT CHAIN 12B; MYOSIN LIGHT CHAIN 2; MYOSIN LIGHT CHAIN 7; MYOSIN LIGHT CHAIN 9; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 79251554351     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20101473     Document Type: Article
Times cited : (100)

References (42)
  • 2
    • 21544444439 scopus 로고    scopus 로고
    • Molecular mechanism of actomyosin-based motility
    • Geeves, M. A., Fedorov, R. and Manstein, D. J. (2005) Molecular mechanism of actomyosin-based motility. Cell. Mol. Life Sci. 62, 1462-1477
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 1462-1477
    • Geeves, M.A.1    Fedorov, R.2    Manstein, D.J.3
  • 4
    • 34347387093 scopus 로고    scopus 로고
    • Fast skeletal muscle regulatory light chain is required for fast and slow skeletal muscle development
    • Wang, Y., Szczesna-Cordary, D., Craig, R., Diaz-Perez, Z., Guzman, G., Miller, T. and Potter, J. D. (2007) Fast skeletal muscle regulatory light chain is required for fast and slow skeletal muscle development. FASEB J. 21, 2205-2214
    • (2007) FASEB J. , vol.21 , pp. 2205-2214
    • Wang, Y.1    Szczesna-Cordary, D.2    Craig, R.3    Diaz-Perez, Z.4    Guzman, G.5    Miller, T.6    Potter, J.D.7
  • 6
    • 0025076788 scopus 로고
    • Mammalian nonsarcomeric myosin regulatory light chains are encoded by two differentially regulated and linked genes
    • DOI 10.1083/jcb.111.3.1127
    • Grant, J. W., Taubman, M. B., Church, S. L., Johnson, R. L. and Nadal-Ginard, B. (1990) Mammalian nonsarcomeric myosin regulatory light chains are encoded by two differentially regulated and linked genes. J. Cell Biol. 111, 1127-1135 (Pubitemid 20263792)
    • (1990) Journal of Cell Biology , vol.111 , Issue.3 , pp. 1127-1135
    • Grant, J.W.1    Taubman, M.B.2    Church, S.L.3    Johnson, R.L.4    Nadal-Ginard, B.5
  • 7
    • 0025087362 scopus 로고
    • Human nonsarcomeric 20,000 Da myosin regulatory light chain cDNA
    • Grant, J. W., Zhong, R. Q., McEwen, P. M. and Church, S. L. (1990) Human nonsarcomeric 20,000 Da myosin regulatory light chain cDNA. Nucleic Acids Res. 18, 5892
    • (1990) Nucleic Acids Res. , vol.18 , pp. 5892
    • Grant, J.W.1    Zhong, R.Q.2    McEwen, P.M.3    Church, S.L.4
  • 9
    • 0035736484 scopus 로고    scopus 로고
    • Diphosphorylated MRLC is required for organization of stress fibers in interphase cells and the contractile ring in dividing cells
    • Iwasaki, T., Murata-Hori, M., Ishitobi, S. and Hosoya, H. (2001) Diphosphorylated MRLC is required for organization of stress fibers in interphase cells and the contractile ring in dividing cells. Cell Struct. Funct. 26, 677-683
    • (2001) Cell Struct. Funct. , vol.26 , pp. 677-683
    • Iwasaki, T.1    Murata-Hori, M.2    Ishitobi, S.3    Hosoya, H.4
  • 10
    • 17044377499 scopus 로고    scopus 로고
    • Identification of a multiprotein 'motor' complex binding to water channel aquaporin-2
    • Noda, Y., Horikawa, S., Katayama, Y. and Sasaki, S. (2005) Identification of a multiprotein 'motor' complex binding to water channel aquaporin-2. Biochem. Biophys. Res. Commun. 330, 1041-1047
    • (2005) Biochem. Biophys. Res. Commun. , vol.330 , pp. 1041-1047
    • Noda, Y.1    Horikawa, S.2    Katayama, Y.3    Sasaki, S.4
  • 11
    • 0025179721 scopus 로고
    • Cloning and characterization of a vertebrate cellular myosin regulatory light chain complementary DNA
    • Zavodny, P. J., Petro, M. E., Lonial, H. K., Dailey, S. H., Narula, S. K., Leibowitz, P. J. and Kumar, C. C. (1990) Cloning and characterization of a vertebrate cellular myosin regulatory light chain complementary DNA. Circ. Res. 67, 933-940
    • (1990) Circ. Res. , vol.67 , pp. 933-940
    • Zavodny, P.J.1    Petro, M.E.2    Lonial, H.K.3    Dailey, S.H.4    Narula, S.K.5    Leibowitz, P.J.6    Kumar, C.C.7
  • 12
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL-X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D., Gibson, T. J., Plewniak, F., Jeanmougin, F. and Higgins, D. G. (1997) The CLUSTAL-X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25, 4876-4882
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 13
    • 0021379023 scopus 로고
    • 45Ca autoradiography on nitrocellulose membrane after sodium dodecyl sulfate gel electrophoresis
    • 45Ca autoradiography on nitrocellulose membrane after sodium dodecyl sulfate gel electrophoresis. J. Biochem. 95, 511-519
    • (1984) J. Biochem. , vol.95 , pp. 511-519
    • Maruyama, K.1    Mikawa, T.2    Ebashi, S.3
  • 14
    • 0014829125 scopus 로고
    • An electrophoretic study of the low-molecular-weight components of myosin
    • Perrie, W. T. and Perry, S. V. (1970) An electrophoretic study of the low-molecular-weight components of myosin. Biochem. J. 119, 31-38
    • (1970) Biochem. J. , vol.119 , pp. 31-38
    • Perrie, W.T.1    Perry, S.V.2
  • 15
    • 0024478129 scopus 로고
    • Cytoplasmic Ca2+ is a primary determinant for myosin phosphorylation in smooth muscle cells
    • Taylor, D. A., Bowman, B. F. and Stull, J. T. (1989) Cytoplasmic Ca2+ is a primary determinant for myosin phosphorylation in smooth muscle cells. J. Biol. Chem. 264, 6207-6213
    • (1989) J. Biol. Chem. , vol.264 , pp. 6207-6213
    • Taylor, D.A.1    Bowman, B.F.2    Stull, J.T.3
  • 16
    • 0032553296 scopus 로고    scopus 로고
    • Myosin essential light chain isoforms modulate the velocity of shortening propelled by nonphosphorylated cross-bridges
    • Matthew, J. D., Khromov, A. S., Trybus, K. M., Somlyo, A. P. and Somlyo, A. V. (1998) Myosin essential light chain isoforms modulate the velocity of shortening propelled by nonphosphorylated cross-bridges. J. Biol. Chem. 273, 31289-31296
    • (1998) J. Biol. Chem. , vol.273 , pp. 31289-31296
    • Matthew, J.D.1    Khromov, A.S.2    Trybus, K.M.3    Somlyo, A.P.4    Somlyo, A.V.5
  • 17
  • 18
    • 0036393898 scopus 로고    scopus 로고
    • DTASelect and contrast: Tools for assembling and comparing protein identifications from shotgun proteomics
    • Tabb, D. L., McDonald, W. H. and Yates, III, J. R. (2002) DTASelect and contrast: tools for assembling and comparing protein identifications from shotgun proteomics. J. Proteome Res. 1, 21-26
    • (2002) J. Proteome Res. , vol.1 , pp. 21-26
    • Tabb, D.L.1    McDonald, W.H.2    Yates III, J.R.3
  • 19
    • 0033005168 scopus 로고    scopus 로고
    • Molecular mechanisms of nonmuscle myosin-II regulation
    • Bresnick, A. R. (1999) Molecular mechanisms of nonmuscle myosin-II regulation. Curr. Opin. Cell Biol. 11, 26-33
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 26-33
    • Bresnick, A.R.1
  • 20
    • 0021438535 scopus 로고
    • Actomyosin adenosine triphosphatase regulation by intramolecular myosin mechanisms. Myosin light chains functions and rod modification effects
    • Kofman, E. B. and Kalamkarova, M. B. (1984) Actomyosin adenosine triphosphatase regulation by intramolecular myosin mechanisms. Myosin light chains functions and rod modification effects. Gen. Physiol. Biophys. 3, 201-221
    • (1984) Gen. Physiol. Biophys. , vol.3 , pp. 201-221
    • Kofman, E.B.1    Kalamkarova, M.B.2
  • 21
    • 0034080528 scopus 로고    scopus 로고
    • Nonmuscle myosin II localizes to the Z-lines and intercalated discs of cardiac muscle and to the Z-lines of skeletal muscle
    • Takeda, K., Yu, Z. X., Qian, S., Chin, T. K., Adelstein, R. S. and Ferrans, V. J. (2000) Nonmuscle myosin II localizes to the Z-lines and intercalated discs of cardiac muscle and to the Z-lines of skeletal muscle. Cell Motil. Cytoskeleton 46, 59-68 (Pubitemid 30368505)
    • (2000) Cell Motility and the Cytoskeleton , vol.46 , Issue.1 , pp. 59-68
    • Takeda, K.1    Yu, Z.-X.2    Qian, S.3    Chin, T.K.4    Adelstein, R.S.5    Ferrans, V.J.6
  • 24
    • 13944265302 scopus 로고    scopus 로고
    • Basic mechanism of three-dimensional collagen fibre transport by fibroblasts
    • Meshel, A. S., Wei, Q., Adelstein, R. S. and Sheetz, M. P. (2005) Basic mechanism of three-dimensional collagen fibre transport by fibroblasts. Nat. Cell Biol. 7, 157-164
    • (2005) Nat. Cell Biol. , vol.7 , pp. 157-164
    • Meshel, A.S.1    Wei, Q.2    Adelstein, R.S.3    Sheetz, M.P.4
  • 25
    • 0037194590 scopus 로고    scopus 로고
    • Rho-kinase contributes to diphosphorylation of myosin II regulatory light chain in nonmuscle cells
    • DOI 10.1038/sj.onc.1205747
    • Ueda, K., Murata-Hori, M., Tatsuka, M. and Hosoya, H. (2002) Rho-kinase contributes to diphosphorylation of myosin II regulatory light chain in nonmuscle cells. Oncogene 21, 5852-5860 (Pubitemid 35007235)
    • (2002) Oncogene , vol.21 , Issue.38 , pp. 5852-5860
    • Ueda, K.1    Murata-Hori, M.2    Tatsuka, M.3    Hosoya, H.4
  • 26
    • 0034698841 scopus 로고    scopus 로고
    • Distinct roles of ROCK (Rho-kinase) and MLCK in spatial regulation of MLC phosphorylation for assembly of stress fibers and focal adhesions in 3T3 fibroblasts
    • DOI 10.1083/jcb.150.4.797
    • Totsukawa, G., Yamakita, Y., Yamashiro, S., Hartshorne, D. J., Sasaki, Y. and Matsumura, F. (2000) Distinct roles of ROCK (Rho-kinase) and MLCK in spatial regulation of MLC phosphorylation for assembly of stress fibers and focal adhesions in 3T3 fibroblasts. J. Cell Biol. 150, 797-806 (Pubitemid 30663416)
    • (2000) Journal of Cell Biology , vol.150 , Issue.4 , pp. 797-806
    • Totsukawa, G.1    Yamakita, Y.2    Yamashiro, S.3    Hartshorne, D.J.4    Sasaki, Y.5    Matsumura, F.6
  • 29
    • 0035857044 scopus 로고    scopus 로고
    • HeLa ZIP kinase induces diphosphorylation of myosin II regulatory light chain and reorganization of actin filaments in nonmuscle cells
    • DOI 10.1038/sj.onc.1205055
    • Murata-Hori, M., Fukuta, Y., Ueda, K., Iwasaki, T. and Hosoya, H. (2001) HeLa ZIP kinase induces diphosphorylation of myosin II regulatory light chain and reorganization of actin filaments in nonmuscle cells. Oncogene 20, 8175-8183 (Pubitemid 34038206)
    • (2001) Oncogene , vol.20 , Issue.57 , pp. 8175-8183
    • Murata-Hori, M.1    Fukuta, Y.2    Ueda, K.3    Iwasaki, T.4    Hosoya, H.5
  • 30
    • 21744445075 scopus 로고    scopus 로고
    • Regulation of myosin II during cytokinesis in higher eukaryotes
    • Matsumura, F. (2005) Regulation of myosin II during cytokinesis in higher eukaryotes. Trends Cell Biol. 15, 371-377
    • (2005) Trends Cell Biol. , vol.15 , pp. 371-377
    • Matsumura, F.1
  • 31
    • 0034104605 scopus 로고    scopus 로고
    • The interaction between the regulatory light chain domains on two heads is critical for regulation of smooth muscle myosin
    • DOI 10.1021/bi9924617
    • Li, X. D., Saito, J., Ikebe, R., Mabuchi, K. and Ikebe, M. (2000) The interaction between the regulatory light chain domains on two heads is critical for regulation of smooth muscle myosin. Biochemistry 39, 2254-2260 (Pubitemid 30130074)
    • (2000) Biochemistry , vol.39 , Issue.9 , pp. 2254-2260
    • Li, X.-D.1    Saito, J.2    Ikebe, R.3    Mabuchi, K.4    Ikebe, M.5
  • 32
    • 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. and Adelstein, R. S. (2004) Defects in cell adhesion and the visceral endoderm following ablation of nonmuscle myosin heavy chain II-A in mice. J. Biol. Chem. 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
  • 33
    • 39849103291 scopus 로고    scopus 로고
    • A unique role for nonmuscle myosin heavy chain IIA in regulation of epithelial apical junctions
    • Ivanov, A. I., Bachar, M., Babbin, B. A., Adelstein, R. S., Nusrat, A. and Parkos, C. A. (2007) A unique role for nonmuscle myosin heavy chain IIA in regulation of epithelial apical junctions. PLoS ONE 2, e658
    • (2007) PLoS ONE , vol.2
    • Ivanov, A.I.1    Bachar, M.2    Babbin, B.A.3    Adelstein, R.S.4    Nusrat, A.5    Parkos, C.A.6
  • 34
    • 0041356912 scopus 로고    scopus 로고
    • Ablation and mutation of nonmuscle myosin heavy chain II-B results in a defect in cardiac myocyte cytokinesis
    • Takeda, K., Kishi, H., Ma, X., Yu, Z. X. and Adelstein, R. S. (2003) Ablation and mutation of nonmuscle myosin heavy chain II-B results in a defect in cardiac myocyte cytokinesis. Circ. Res. 93, 330-337
    • (2003) Circ. Res. , vol.93 , pp. 330-337
    • Takeda, K.1    Kishi, H.2    Ma, X.3    Yu, Z.X.4    Adelstein, R.S.5
  • 35
    • 57449098002 scopus 로고    scopus 로고
    • Ablation of smooth muscle myosin heavy chain SM2 increases smooth muscle contraction and results in postnatal death in mice
    • Chi, M., Zhou, Y., Vedamoorthyrao, S., Babu, G. J. and Periasamy, M. (2008) Ablation of smooth muscle myosin heavy chain SM2 increases smooth muscle contraction and results in postnatal death in mice. Proc. Natl. Acad. Sci. U.S.A. 105, 18614-18618
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 18614-18618
    • Chi, M.1    Zhou, Y.2    Vedamoorthyrao, S.3    Babu, G.J.4    Periasamy, M.5
  • 36
    • 0019308534 scopus 로고
    • Regulation of non-muscle myosin assembly by calmodulin-dependent light chain kinase
    • DOI 10.1038/287233a0
    • Scholey, J. M., Taylor, K. A. and Kendrick-Jones, J. (1980) Regulation of non-muscle myosin assembly by calmodulin-dependent light chain kinase. Nature 287, 233-235 (Pubitemid 10019772)
    • (1980) Nature , vol.287 , Issue.5779 , pp. 233-235
    • Scholey, J.M.1    Taylor, K.A.2    Kendrick-Jones, J.3
  • 37
    • 33846815057 scopus 로고    scopus 로고
    • Regulation of myosin II dynamics by phosphorylation and dephosphorylation of its light chain in epithelial cells
    • Watanabe, T., Hosoya, H. and Yonemura, S. (2007) Regulation of myosin II dynamics by phosphorylation and dephosphorylation of its light chain in epithelial cells. Mol. Biol. Cell 18, 605-616
    • (2007) Mol. Biol. Cell , vol.18 , pp. 605-616
    • Watanabe, T.1    Hosoya, H.2    Yonemura, S.3
  • 38
    • 0141751697 scopus 로고    scopus 로고
    • Ca2+ sensitivity of smooth muscle and nonmuscle myosin II: Modulated by G proteins, kinases and myosin phosphatase
    • Somlyo, A. P. and Somlyo, A. V. (2003) Ca2+ sensitivity of smooth muscle and nonmuscle myosin II: modulated by G proteins, kinases and myosin phosphatase. Physiol. Rev. 83, 1325-1358
    • (2003) Physiol. Rev. , vol.83 , pp. 1325-1358
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 39
    • 77952787533 scopus 로고    scopus 로고
    • Common structural motifs for the regulation of divergent class II myosins
    • Lowey, S. and Trybus, K. M. (2010) Common structural motifs for the regulation of divergent class II myosins. J. Biol. Chem. 285, 16403-16407
    • (2010) J. Biol. Chem. , vol.285 , pp. 16403-16407
    • Lowey, S.1    Trybus, K.M.2
  • 40
    • 0022829574 scopus 로고
    • Myosin subunit interactions. Properties of the 19,000-dalton light chain-deficient myosin
    • Pastra-Landis, S. C. and Lowey, S. (1986) Myosin subunit interactions. Properties of the 19,000-dalton light chain-deficient myosin. J. Biol. Chem. 261, 14811-14816
    • (1986) J. Biol. Chem. , vol.261 , pp. 14811-14816
    • Pastra-Landis, S.C.1    Lowey, S.2
  • 41
    • 33746843968 scopus 로고    scopus 로고
    • Cardiac myosin light chain-2: A novel essential component of thick-myofilament assembly and contractility of the heart
    • Rottbauer, W., Wessels, G., Dahme, T., Just, S., Trano, N., Hassel, D., Burns, C. G., Katus, H. A. and Fishman, M. C. (2006) Cardiac myosin light chain-2: a novel essential component of thick-myofilament assembly and contractility of the heart. Circ. Res. 99, 323-331
    • (2006) Circ. Res. , vol.99 , pp. 323-331
    • Rottbauer, W.1    Wessels, G.2    Dahme, T.3    Just, S.4    Trano, N.5    Hassel, D.6    Burns, C.G.7    Katus, H.A.8    Fishman, M.C.9
  • 42
    • 33748997964 scopus 로고    scopus 로고
    • Native nonmuscle myosin II stability and light chain binding in Drosophila melanogaster
    • Franke, J. D., Boury, A. L., Gerald, N. J. and Kiehart, D. P. (2006) Native nonmuscle myosin II stability and light chain binding in Drosophila melanogaster. Cell Motil. Cytoskeleton 63, 604-622
    • (2006) Cell Motil. Cytoskeleton , vol.63 , pp. 604-622
    • Franke, J.D.1    Boury, A.L.2    Gerald, N.J.3    Kiehart, D.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.