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Volumn 140, Issue 1, 1998, Pages 119-129

Specific localization of serine 19 phosphorylated myosin II during cell locomotion and mitosis of cultured cells

Author keywords

[No Author keywords available]

Indexed keywords

MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOSIN LIGHT CHAIN; SERINE;

EID: 0031917782     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.140.1.119     Document Type: Article
Times cited : (195)

References (35)
  • 2
    • 0027176798 scopus 로고
    • A novel cytoskeletal structure involved in purse string closure and cell polarity maintenance
    • Bement, W.M., P. Forscher, and M.S. Mooseker. 1993. A novel cytoskeletal structure involved in purse string closure and cell polarity maintenance. J. Cell Biol. 121:565-578.
    • (1993) J. Cell Biol. , vol.121 , pp. 565-578
    • Bement, W.M.1    Forscher, P.2    Mooseker, M.S.3
  • 3
    • 0024245742 scopus 로고
    • Spatial pattern of myosin phosphorylation in contracting smooth muscle cells: Evidence for contractile zones
    • Bennett, J.P., R.A. Cross, J. Kendrick-Jones, and A.G. Weeds. 1988. Spatial pattern of myosin phosphorylation in contracting smooth muscle cells: Evidence for contractile zones. J. Cell Biol. 107:2623-2629.
    • (1988) J. Cell Biol. , vol.107 , pp. 2623-2629
    • Bennett, J.P.1    Cross, R.A.2    Kendrick-Jones, J.3    Weeds, A.G.4
  • 4
    • 0029583423 scopus 로고
    • A localized elevation of cytosolic free calcium is associated with cytokinesis in the zebrafish embryo
    • Chang, D.C., and C. Meng. 1995. A localized elevation of cytosolic free calcium is associated with cytokinesis in the zebrafish embryo. J. Cell Biol. 131:1539-1545.
    • (1995) J. Cell Biol. , vol.131 , pp. 1539-1545
    • Chang, D.C.1    Meng, C.2
  • 6
    • 0029779538 scopus 로고    scopus 로고
    • Myosin II transport, organization, and phosphorylation: Evidence for cortical flow/solution-contraction coupling during cytokinesis and cell locomotion
    • DeBiasio, R.L., G.M. LaRocca, P.L. Post, and D.L. Taylor. 1996. Myosin II transport, organization, and phosphorylation: evidence for cortical flow/solution-contraction coupling during cytokinesis and cell locomotion. Mol. Biol. Cell. 7:1259-1282.
    • (1996) Mol. Biol. Cell. , vol.7 , pp. 1259-1282
    • DeBiasio, R.L.1    LaRocca, G.M.2    Post, P.L.3    Taylor, D.L.4
  • 7
    • 0027372314 scopus 로고
    • Dictyostelium myosin heavy chain phosphorylation sites regulate myosin filament assembly and localization in vivo
    • Egelhoff, T.T., R.J. Lee, and J.A. Spudich. 1993. Dictyostelium myosin heavy chain phosphorylation sites regulate myosin filament assembly and localization in vivo. Cell. 75:363-371.
    • (1993) Cell , vol.75 , pp. 363-371
    • Egelhoff, T.T.1    Lee, R.J.2    Spudich, J.A.3
  • 8
    • 0025790165 scopus 로고
    • Slow calcium waves accompany cytokinesis in medaka fish eggs
    • Fluck, R.A., A.L. Miller, and L.F. Jaffe. 1991. Slow calcium waves accompany cytokinesis in medaka fish eggs. J. Cell Biol. 115:1259-1265.
    • (1991) J. Cell Biol. , vol.115 , pp. 1259-1265
    • Fluck, R.A.1    Miller, A.L.2    Jaffe, L.F.3
  • 9
    • 0017109215 scopus 로고
    • Fluorescent antibody localization of myosin in the cytoplasm, cleavage furrow and mitotic spindle of human cells
    • Fujiwara, K., and T.D. Pollard. 1976. Fluorescent antibody localization of myosin in the cytoplasm, cleavage furrow and mitotic spindle of human cells. J. Cell Biol. 71:848-875.
    • (1976) J. Cell Biol. , vol.71 , pp. 848-875
    • Fujiwara, K.1    Pollard, T.D.2
  • 10
    • 0027057547 scopus 로고
    • Myosin II phosphorylation and the dynamics of stress fibers in serum-deprived and stimulated fibroblasts
    • Giuliano, K.A., J. Kolega, R.L. DeBiasio, and D.L. Taylor. 1992. Myosin II phosphorylation and the dynamics of stress fibers in serum-deprived and stimulated fibroblasts. Mol. Biol. Cell. 3:1037-1048.
    • (1992) Mol. Biol. Cell. , vol.3 , pp. 1037-1048
    • Giuliano, K.A.1    Kolega, J.2    DeBiasio, R.L.3    Taylor, D.L.4
  • 11
    • 0029119895 scopus 로고
    • Myosin light chain kinase-regulated endothelial cell contraction: The relationship between isometric tension, actin polymerization, and myosin phosphorylation
    • Goeckeleer, M.Z., and R.B. Wysolmerski. 1995. Myosin light chain kinase-regulated endothelial cell contraction: The relationship between isometric tension, actin polymerization, and myosin phosphorylation. J. Cell Biol. 130:613-627.
    • (1995) J. Cell Biol. , vol.130 , pp. 613-627
    • Goeckeleer, M.Z.1    Wysolmerski, R.B.2
  • 12
    • 0028597065 scopus 로고
    • Regulation of Dictyostelium myosin II by phosphorylation: What is essential and what is important?
    • Hammer, J.A. 1994. Regulation of Dictyostelium myosin II by phosphorylation: what is essential and what is important? J. Cell Biol. 127:1779-1782.
    • (1994) J. Cell Biol. , vol.127 , pp. 1779-1782
    • Hammer, J.A.1
  • 13
    • 0027322156 scopus 로고
    • Localization of caldesmon and its dephosphorylation during cell division
    • Hosoya, N., H. Hosoya, S. Yamashiro, H. Mohri, and F. Matsumura. 1993. Localization of caldesmon and its dephosphorylation during cell division. J. Cell Biol. 121:1075-1082.
    • (1993) J. Cell Biol. , vol.121 , pp. 1075-1082
    • Hosoya, N.1    Hosoya, H.2    Yamashiro, S.3    Mohri, H.4    Matsumura, F.5
  • 14
    • 0021894617 scopus 로고
    • The function of myosin and myosin light chain kinase phosphorylation in smooth muscle
    • Kamm, K.E., and J.T. Stull. 1985. The function of myosin and myosin light chain kinase phosphorylation in smooth muscle. Annu. Rev. Pharmacol. Toxicol. 25:593-620.
    • (1985) Annu. Rev. Pharmacol. Toxicol. , vol.25 , pp. 593-620
    • Kamm, K.E.1    Stull, J.T.2
  • 15
    • 0029782819 scopus 로고    scopus 로고
    • Xenopus nonmuscle myosin heavy chain isoforms have different subcellular localizations and enzymatic activities
    • Kelley, C.A., J.R. Sellers, D.L. Gard, D. Bui, R.S. Adelstein, and I.C. Baines. 1996. Xenopus nonmuscle myosin heavy chain isoforms have different subcellular localizations and enzymatic activities. J. Cell Biol. 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
  • 17
    • 0027509362 scopus 로고
    • Regulation of cytoplasmic division of Xenopus embryo by rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI)
    • Kishi, K., T. Sasaki, S. Kuroda, T. Itoh, and Y. Takai. 1993. Regulation of cytoplasmic division of Xenopus embryo by rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI). J. Cell Biol. 120:1187-1195.
    • (1993) J. Cell Biol. , vol.120 , pp. 1187-1195
    • Kishi, K.1    Sasaki, T.2    Kuroda, S.3    Itoh, T.4    Takai, Y.5
  • 18
    • 0022521095 scopus 로고
    • Myosin at the apical pole of ciliated epithelial cells as revealed by a monoclonal antibody
    • Klotz, C., N. Bordes, M.C. Laine, D. Sandoz, and M. Bornens. 1986. Myosin at the apical pole of ciliated epithelial cells as revealed by a monoclonal antibody. J. Cell Biol. 103:613-619.
    • (1986) J. Cell Biol. , vol.103 , pp. 613-619
    • Klotz, C.1    Bordes, N.2    Laine, M.C.3    Sandoz, D.4    Bornens, M.5
  • 19
    • 0027435246 scopus 로고
    • Correlation of myosin light chain phosphorylation with isometric contraction of fibroblasts
    • Kolodney, M.S., and E.L. Elson. 1993. Correlation of myosin light chain phosphorylation with isometric contraction of fibroblasts. J. Biol. Chem. 268:23850-23855.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23850-23855
    • Kolodney, M.S.1    Elson, E.L.2
  • 20
    • 0030977123 scopus 로고    scopus 로고
    • Rho-associated kinase directly induces smooth muscle contraction through myosin light chain phosphorylation
    • Kureishi, Y., S. Kobayashi, M. Amano, K. Kimura, H. Kanaide, T. Nakano, K. Kaibuchi, and M. Ito. 1997. Rho-associated kinase directly induces smooth muscle contraction through myosin light chain phosphorylation. J. Biol. Chem. 272:12257-12260.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12257-12260
    • Kureishi, Y.1    Kobayashi, S.2    Amano, M.3    Kimura, K.4    Kanaide, H.5    Nakano, T.6    Kaibuchi, K.7    Ito, M.8
  • 21
    • 0023352340 scopus 로고
    • Immunocytochemical localization of myosin during ciliogenesis of quail oviduct
    • Lemullois, M., C. Klotz, and D. Sandoz. 1987. Immunocytochemical localization of myosin during ciliogenesis of quail oviduct. Eur. J. Cell Biol. 43:429-437.
    • (1987) Eur. J. Cell Biol. , vol.43 , pp. 429-437
    • Lemullois, M.1    Klotz, C.2    Sandoz, D.3
  • 22
    • 0027691240 scopus 로고
    • A rho-like protein is involved in the organisation of the contractile ring in dividing sand dollar eggs
    • Mabuchi, I., Y. Hamaguchi, H. Fujimoto, N. Morii, M. Mishima, and S. Narumiya. 1993. A rho-like protein is involved in the organisation of the contractile ring in dividing sand dollar eggs. Zygote. 1:325-331.
    • (1993) Zygote , vol.1 , pp. 325-331
    • Mabuchi, I.1    Hamaguchi, Y.2    Fujimoto, H.3    Morii, N.4    Mishima, M.5    Narumiya, S.6
  • 23
    • 0028577135 scopus 로고
    • Expression of a myosin regulatory light chain phosphorylation site mutant complements the cytokinesis and developmental defects of Dictyostelium RMLC null cells
    • Ostrow, B.D., P. Chen, and R.L., Chisholm. 1994. Expression of a myosin regulatory light chain phosphorylation site mutant complements the cytokinesis and developmental defects of Dictyostelium RMLC null cells. J. Cell Biol. 127:1945-1955.
    • (1994) J. Cell Biol. , vol.127 , pp. 1945-1955
    • Ostrow, B.D.1    Chen, P.2    Chisholm, R.L.3
  • 24
    • 0014829125 scopus 로고
    • An electrophoretic study of the low-molecular-weight components of myosin
    • Perrie, W.T., and S.V. Perry. 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
  • 25
    • 0028864440 scopus 로고
    • A fluorescent protein biosensor of myosin II regulatory light chain phosphorylation reports a gradient of phosphorylated myosin II in migrating cells
    • Post, P.L., R.L. DeBiasio, and D.L. Taylor. 1995. A fluorescent protein biosensor of myosin II regulatory light chain phosphorylation reports a gradient of phosphorylated myosin II in migrating cells. Mol. Biol. Cell. 6:1755-1768.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1755-1768
    • Post, P.L.1    DeBiasio, R.L.2    Taylor, D.L.3
  • 26
    • 0028120774 scopus 로고
    • An antibody for phosphorylated myosin light chain of smooth muscle: Application to a biochemical study
    • Sakurada, K., T. Ikuhara, M. Seto, and Y. Sasaki. 1994. An antibody for phosphorylated myosin light chain of smooth muscle: application to a biochemical study. J. Biochem. (Tokyo). 115:18-21.
    • (1994) J. Biochem. (Tokyo) , vol.115 , pp. 18-21
    • Sakurada, K.1    Ikuhara, T.2    Seto, M.3    Sasaki, Y.4
  • 27
    • 0024433443 scopus 로고
    • Analysis of cell division using fluorescently labeled actin and myosin in living PtK2 cells
    • Sanger, J.M., B. Mittal, J.S. Dome, and J.W. Sanger. 1989. Analysis of cell division using fluorescently labeled actin and myosin in living PtK2 cells. Cell Motil. Cytoskeleton. 14:201-219.
    • (1989) Cell Motil. Cytoskeleton , vol.14 , pp. 201-219
    • Sanger, J.M.1    Mittal, B.2    Dome, J.S.3    Sanger, J.W.4
  • 28
    • 0025825087 scopus 로고
    • Regulation of cytoplasmic and smooth muscle myosin
    • Sellers, J.R. 1991. Regulation of cytoplasmic and smooth muscle myosin. Curr. Opin. Cell Biol. 3:98-104.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 98-104
    • Sellers, J.R.1
  • 29
    • 0024755672 scopus 로고
    • In pursuit of myosin function
    • Spudich, J.A. 1989. In pursuit of myosin function. Cell Regul. 1:1-11.
    • (1989) Cell Regul. , vol.1 , pp. 1-11
    • Spudich, J.A.1
  • 30
    • 0026026368 scopus 로고
    • Regulation of smooth muscle myosin
    • Trybus, K.M. 1991. Regulation of smooth muscle myosin. Cell Motil. Cytoskeleton. 18:81-85.
    • (1991) Cell Motil. Cytoskeleton , vol.18 , pp. 81-85
    • Trybus, K.M.1
  • 31
    • 0027767689 scopus 로고
    • A functional recombinant myosin II lacking a regulatory light chain-binding site
    • Uyeda, T.Q., and J.A. Spudich. 1993. A functional recombinant myosin II lacking a regulatory light chain-binding site. Science. 262:1867-1870.
    • (1993) Science , vol.262 , pp. 1867-1870
    • Uyeda, T.Q.1    Spudich, J.A.2
  • 33
    • 0028123676 scopus 로고
    • In vivo phosphorylation of regulatory light chain of myosin II during mitosis of cultured cells
    • Yamakita, Y., S. Yamashiro, and F. Matsumura. 1994. In vivo phosphorylation of regulatory light chain of myosin II during mitosis of cultured cells. J. Cell Biol. 124:129-137.
    • (1994) J. Cell Biol. , vol.124 , pp. 129-137
    • Yamakita, Y.1    Yamashiro, S.2    Matsumura, F.3
  • 34
    • 0022535995 scopus 로고
    • Intracellular localization of the 55-kD actin-bundling protein in cultured cells: Spatial relationships with actin, alpha-actinin, tropomyosin, and fimbrin
    • Yamashiro-Matsumura, S., and F. Matsumura. 1986. Intracellular localization of the 55-kD actin-bundling protein in cultured cells: spatial relationships with actin, alpha-actinin, tropomyosin, and fimbrin. J. Cell Biol. 103:631-640.
    • (1986) J. Cell Biol. , vol.103 , pp. 631-640
    • Yamashiro-Matsumura, S.1    Matsumura, F.2
  • 35
    • 0030989551 scopus 로고    scopus 로고
    • Myosin II can be localized to the cleavage furrow and to the posterior region of Dictyostelium amoebae without control by phosphorylation of myosin heavy and light chains
    • Yumura, S., and T.Q. Uyeda. 1997. Myosin II can be localized to the cleavage furrow and to the posterior region of Dictyostelium amoebae without control by phosphorylation of myosin heavy and light chains. Cell Motil. Cytoskeleton. 36:313-322.
    • (1997) Cell Motil. Cytoskeleton , vol.36 , pp. 313-322
    • Yumura, S.1    Uyeda, T.Q.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.