메뉴 건너뛰기




Volumn 144, Issue 4, 1999, Pages 735-744

Activation of myosin phosphatase targeting subunit by mitosis-specific phosphorylation

Author keywords

Mitosis; Myosin; Myosin binding; Phosphatase; Phosphorylation

Indexed keywords

PHOSPHATASE;

EID: 0033593792     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.144.4.735     Document Type: Article
Times cited : (56)

References (55)
  • 1
    • 0027049145 scopus 로고
    • The control of protein phosphatase-1 by targetting subunits. The major myosin phosphatase in avian smooth muscle is a novel form of protein phosphatase-1
    • Alessi, D., L.K. MacDougall, M.M. Sola, M. Ikebe, and P. Cohen. 1992. The control of protein phosphatase-1 by targetting subunits. The major myosin phosphatase in avian smooth muscle is a novel form of protein phosphatase-1. Eur. J. Biochem. 210:1023-1035.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 1023-1035
    • Alessi, D.1    MacDougall, L.K.2    Sola, M.M.3    Ikebe, M.4    Cohen, P.5
  • 3
    • 0023645037 scopus 로고
    • Sequence of the sites phosphorylated by protein kinase C in the smooth muscle myosin light chain
    • Bengur, A.R., E.A. Robinson, E. Appella, and J.R. Sellers. 1987. Sequence of the sites phosphorylated by protein kinase C in the smooth muscle myosin light chain. J. Biol. Chem. 262:7613-7617.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7613-7617
    • Bengur, A.R.1    Robinson, E.A.2    Appella, E.3    Sellers, J.R.4
  • 4
    • 0000290454 scopus 로고
    • Quantitative electrophoresis in polyacrylamide gels of 2-40%
    • Blatter, D.P., F. Garner, K. Van Slyke, and A. Bradley. 1972. Quantitative electrophoresis in polyacrylamide gels of 2-40%. J. Chromatogr. 64:147-155.
    • (1972) J. Chromatogr. , vol.64 , pp. 147-155
    • Blatter, D.P.1    Garner, F.2    Van Slyke, K.3    Bradley, A.4
  • 5
    • 0025998840 scopus 로고
    • Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thinlayer cellulose plates
    • Boyle, W.J., P. van der Geer, and T. Hunter. 1991. Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thinlayer cellulose plates. Method Enzymol. 201:110-149.
    • (1991) Method Enzymol. , vol.201 , pp. 110-149
    • Boyle, W.J.1    Van Der Geer, P.2    Hunter, T.3
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 7
    • 0028114606 scopus 로고
    • Molecular cloning of cDNA encoding the 110 kDa and 21 kDa regulatory subunits of smooth muscle protein phosphatase 1M
    • Chen, Y.H., M.X. Chen, D.R. Alessi, D.G. Campbell, C. Shanahan, P. Cohen, and P.T. Cohen. 1994. Molecular cloning of cDNA encoding the 110 kDa and 21 kDa regulatory subunits of smooth muscle protein phosphatase 1M. FEBS Lett. 356:51-55.
    • (1994) FEBS Lett. , vol.356 , pp. 51-55
    • Chen, Y.H.1    Chen, M.X.2    Alessi, D.R.3    Campbell, D.G.4    Shanahan, C.5    Cohen, P.6    Cohen, P.T.7
  • 8
    • 0029995797 scopus 로고    scopus 로고
    • Rho-stimulated contractility drives the formation of stress fibers and focal adhesions
    • Chrzanowska-Wodnicka, M., and K. Burridge. 1996. Rho-stimulated contractility drives the formation of stress fibers and focal adhesions. J. Cell Biol. 133: 1403-1415.
    • (1996) J. Cell Biol. , vol.133 , pp. 1403-1415
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 9
    • 0029779538 scopus 로고    scopus 로고
    • Myosin II transport, organization, and phosphorylation: Evidence for cortical flow/solation-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/solation-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
  • 11
    • 0025837663 scopus 로고
    • Microinjection of the catalytic fragment of myosin light chain kinase into dividing cells: Effects on mitosis and cytokinesis
    • Fishkind, D.J., L.G. Cao, and Y.L. Wang. 1991. Microinjection of the catalytic fragment of myosin light chain kinase into dividing cells: effects on mitosis and cytokinesis. J. Cell Biol. 114:967-975.
    • (1991) J. Cell Biol. , vol.114 , pp. 967-975
    • Fishkind, D.J.1    Cao, L.G.2    Wang, Y.L.3
  • 12
    • 0032054799 scopus 로고    scopus 로고
    • A new isoform of human myosin phosphatase targeting/regulatory subunit (MYPT2): cDNA cloning, tissue expression, and chromosomal mapping
    • Fujioka, M., N. Takahashi, H. Odai, S. Araki, K. Ichikawa, J. Feng, M. Nakamura, K. Kaibuchi, D.J. Hartshorne, T. Nakano. et al. 1998. A new isoform of human myosin phosphatase targeting/regulatory subunit (MYPT2): cDNA cloning, tissue expression, and chromosomal mapping. Genomics. 49: 59-68.
    • (1998) Genomics , vol.49 , pp. 59-68
    • Fujioka, M.1    Takahashi, N.2    Odai, H.3    Araki, S.4    Ichikawa, K.5    Feng, J.6    Nakamura, M.7    Kaibuchi, K.8    Hartshorne, D.J.9    Nakano, T.10
  • 13
    • 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
  • 14
    • 0029119895 scopus 로고
    • Myosin light chain kinase-regulated endothelial cell contraction: The relationship between isometric tension, acin polymerization, and myosin phosphorylation
    • Goeckeler, M.Z., and R.B. Wysolmerski. 1995. Myosin light chain kinase-regulated endothelial cell contraction: the relationship between isometric tension, acin polymerization, and myosin phosphorylation. J. Cell Biol. 130: 613-627.
    • (1995) J. Cell Biol. , vol.130 , pp. 613-627
    • Goeckeler, M.Z.1    Wysolmerski, R.B.2
  • 15
    • 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
  • 16
    • 0031798554 scopus 로고    scopus 로고
    • Myosin light chain phosphatase: Subunit composition, interactions and regulation
    • Hartshorne, D.J., M. Ito, and F. Erdodi. 1998. Myosin light chain phosphatase: subunit composition, interactions and regulation. J. Muscle Res. Cell Motil. 19:325-341.
    • (1998) J. Muscle Res. Cell Motil. , vol.19 , pp. 325-341
    • Hartshorne, D.J.1    Ito, M.2    Erdodi, F.3
  • 17
    • 0031034680 scopus 로고    scopus 로고
    • Interactions of the subunits of smooth muscle myosin phosphatase
    • Hirano, K., B.C. Phan, and D.J. Hartshorne. 1997. Interactions of the subunits of smooth muscle myosin phosphatase. J. Biol Chem. 272:3683-3688.
    • (1997) J. Biol Chem. , vol.272 , pp. 3683-3688
    • Hirano, K.1    Phan, B.C.2    Hartshorne, D.J.3
  • 18
    • 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
  • 19
    • 0029976102 scopus 로고    scopus 로고
    • Phosphorylation of the large subunit of myosin phosphatase and inhibition of phosphatase activity
    • Ichikawa, K., M. Ito, and D.J. Hartshorne. 1996. Phosphorylation of the large subunit of myosin phosphatase and inhibition of phosphatase activity. J. Biol. Chem. 271:4733-4740.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4733-4740
    • Ichikawa, K.1    Ito, M.2    Hartshorne, D.J.3
  • 20
    • 0025306169 scopus 로고
    • Phosphorylation of bovine platelet myosin by protein kinase C
    • Ikebe, M., and S. Reardon. 1990. Phosphorylation of bovine platelet myosin by protein kinase C. Biochemistry. 29:2713-2720.
    • (1990) Biochemistry , vol.29 , pp. 2713-2720
    • Ikebe, M.1    Reardon, S.2
  • 23
    • 0030615319 scopus 로고    scopus 로고
    • Identification of the regions on the M110 subunit of protein phosphatase 1M that interact with the M21 subunit and with myosin
    • Johnson, D., P. Cohen, M.X. Chen, Y.H. Chen, and P.T. Cohen. 1997. Identification of the regions on the M110 subunit of protein phosphatase 1M that interact with the M21 subunit and with myosin. Eur. J. Biochem. 244:931-939.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 931-939
    • Johnson, D.1    Cohen, P.2    Chen, M.X.3    Chen, Y.H.4    Cohen, P.T.5
  • 24
    • 0030036564 scopus 로고    scopus 로고
    • Identification of protein-phosphatase-1-binding domains on the glycogen and myofibrillar targetting subunits
    • Johnson, D.F., G. Moorhead, F.B. Caudwell, P. Cohen, Y.H. Chen, M.X. Chen, and P.T. Cohen. 1996. Identification of protein-phosphatase-1-binding domains on the glycogen and myofibrillar targetting subunits. Eur. J. Biochem. 239:317-325.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 317-325
    • Johnson, D.F.1    Moorhead, G.2    Caudwell, F.B.3    Cohen, P.4    Chen, Y.H.5    Chen, M.X.6    Cohen, P.T.7
  • 25
    • 0031416614 scopus 로고    scopus 로고
    • Myosin light chain-activating phosphorylation sites are required for oogenesis in Drosophila
    • Jordan, P., and R. Karess. 1997. Myosin light chain-activating phosphorylation sites are required for oogenesis in Drosophila. J. Cell Biol. 139:1805-1819.
    • (1997) J. Cell Biol. , vol.139 , pp. 1805-1819
    • Jordan, P.1    Karess, R.2
  • 26
    • 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
  • 28
    • 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
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0031057516 scopus 로고    scopus 로고
    • 2+ desensitization in vascular smooth muscle by activating the myosin light chain phosphatase
    • 2+ desensitization in vascular smooth muscle by activating the myosin light chain phosphatase. J. Biol. Chem. 272:5063-5068.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5063-5068
    • Lee, M.R.1    Li, L.2    Kitazawa, T.3
  • 31
    • 0031917782 scopus 로고    scopus 로고
    • Specific localization of serine 19 phosphorylated myosin II during cell locomotion and mitosis of cultured cells
    • Matsumura, F., S. Ono, Y. Yamakita, G. Totsukawa, and S. Yamashiro. 1998. Specific localization of serine 19 phosphorylated myosin II during cell locomotion and mitosis of cultured cells. J. Cell Biol. 140:119-129.
    • (1998) J. Cell Biol. , vol.140 , pp. 119-129
    • Matsumura, F.1    Ono, S.2    Yamakita, Y.3    Totsukawa, G.4    Yamashiro, S.5
  • 32
    • 0027769523 scopus 로고
    • Phosphorylation of vertebrate nonmuscle and smooth muscle myosin heavy chains and light chains
    • Moussavi, R.S., C.A. Kelley, and R.S. Adelstein. 1993. Phosphorylation of vertebrate nonmuscle and smooth muscle myosin heavy chains and light chains. Mol. Cell. Biochem. 127-128:219-227.
    • (1993) Mol. Cell. Biochem. , vol.127-128 , pp. 219-227
    • Moussavi, R.S.1    Kelley, C.A.2    Adelstein, R.S.3
  • 33
    • 0032519506 scopus 로고    scopus 로고
    • Identification and localization of myosin phosphatase in human platelets
    • Muranyi, A., F. Erdodi, M. Ito, P. Gergely, and D.J. Hartshorne. 1998. Identification and localization of myosin phosphatase in human platelets. Biochem. J. 330:225-231.
    • (1998) Biochem. J. , vol.330 , pp. 225-231
    • Muranyi, A.1    Erdodi, F.2    Ito, M.3    Gergely, P.4    Hartshorne, D.J.5
  • 34
    • 0031004803 scopus 로고    scopus 로고
    • Differential localization of myosin and myosin phosphatase subunits in smooth muscle cells and migrating fibroblasts
    • Murata, K., K. Hirano, E. Villa-Moruzzi, D.J. Hartshorne, and D.L. Brautigan. 1997. Differential localization of myosin and myosin phosphatase subunits in smooth muscle cells and migrating fibroblasts. Mol. Biol. Cell. 8:663-673.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 663-673
    • Murata, K.1    Hirano, K.2    Villa-Moruzzi, E.3    Hartshorne, D.J.4    Brautigan, D.L.5
  • 35
    • 0031976355 scopus 로고    scopus 로고
    • Concentration of singly phosphorylated myosin II regulatory light chain along the cleavage furrow of dividing HeLa cells
    • Murata-Hori, M., N. Murai, S. Komatsu, Y. Uji, and H. Hosoya. 1998. Concentration of singly phosphorylated myosin II regulatory light chain along the cleavage furrow of dividing HeLa cells. Biomed. Res. 19:111-115.
    • (1998) Biomed. Res. , vol.19 , pp. 111-115
    • Murata-Hori, M.1    Murai, N.2    Komatsu, S.3    Uji, Y.4    Hosoya, H.5
  • 36
    • 0026266161 scopus 로고
    • Cell cycle extracts
    • Murray, A.W. 1991. Cell cycle extracts. Methods Cell Biol. 36:581-605.
    • (1991) Methods Cell Biol. , vol.36 , pp. 581-605
    • Murray, A.W.1
  • 38
    • 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
  • 39
    • 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
  • 40
    • 0029052804 scopus 로고
    • Isolation of a functional homolog of the cell cycle-specific NIMA protein kinase of Aspergillus nidulans and functional analysis of conserved residues
    • Pu, R.T., G. Xu, L. Wu. J. Vierula, K. O'Donnell, X.S. Ye, and S.A. Osmani. 1995. Isolation of a functional homolog of the cell cycle-specific NIMA protein kinase of Aspergillus nidulans and functional analysis of conserved residues. J. Biol. Chem. 270:18110-18116.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18110-18116
    • Pu, R.T.1    Xu, G.2    Wu, L.3    Vierula, J.4    O'Donnell, K.5    Ye, X.S.6    Osmani, S.A.7
  • 41
  • 42
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H., and G. von Jagow. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 43
    • 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
  • 45
    • 0028152923 scopus 로고
    • Purification and characterization of the mammalian myosin light chain phosphatase holoenzyme. The differential effects of the holoenzyme and its subunits on smooth muscle
    • Shirazi, A., K. Iizuka, P. Fadden, C. Mosse, A.P. Somlyo, A.V. Somlyo, and T.A. Haystead. 1994. Purification and characterization of the mammalian myosin light chain phosphatase holoenzyme. The differential effects of the holoenzyme and its subunits on smooth muscle. J. Biol. Chem. 269:31598-31606.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31598-31606
    • Shirazi, A.1    Iizuka, K.2    Fadden, P.3    Mosse, C.4    Somlyo, A.P.5    Somlyo, A.V.6    Haystead, T.A.7
  • 46
    • 0028043535 scopus 로고
    • Signal transduction and regulation in smooth muscle
    • published erratum appears in Nature. 1994, 372:812
    • Somlyo, A.P., and A.V. Somlyo. 1994. Signal transduction and regulation in smooth muscle [published erratum appears in Nature. 1994, 372:812]. Nature. 372:231-236.
    • (1994) Nature , vol.372 , pp. 231-236
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 47
    • 0031571683 scopus 로고    scopus 로고
    • Localization of the gene coding for myosin phosphatase, target subunit 1 (MYPT1) to human chromosome 12q15-q21
    • Takahashi, N., M. Ito, J. Tanaka, T. Nakano, K. Kaibuchi, H. Odai, and K. Takemura. 1997. Localization of the gene coding for myosin phosphatase, target subunit 1 (MYPT1) to human chromosome 12q15-q21. Genomics. 44: 150-152.
    • (1997) Genomics , vol.44 , pp. 150-152
    • Takahashi, N.1    Ito, M.2    Tanaka, J.3    Nakano, T.4    Kaibuchi, K.5    Odai, H.6    Takemura, K.7
  • 48
    • 0030441292 scopus 로고    scopus 로고
    • Mitosis-specific phosphorylation of smooth muscle regulatory light chain of myosin 11 at Ser-1 and/or -2 and Thr-9 in sea urchin egg extract
    • Totsukawa, G., E. Himi-Nakamura, S. Komatsu, K. Iwata, A. Tezuka, H. Sakai, K. Yazaki, and H. Hosoya. 1996. Mitosis-specific phosphorylation of smooth muscle regulatory light chain of myosin 11 at Ser-1 and/or -2 and Thr-9 in sea urchin egg extract. Cell Struct. Funct. 21:475-482.
    • (1996) Cell Struct. Funct. , vol.21 , pp. 475-482
    • Totsukawa, G.1    Himi-Nakamura, E.2    Komatsu, S.3    Iwata, K.4    Tezuka, A.5    Sakai, H.6    Yazaki, K.7    Hosoya, H.8
  • 49
    • 0029132694 scopus 로고
    • Thiophosphorylation of the 130-kDa subunit is associated with a decreased activity of myosin light chain phosphatase in alpha-toxin-permeabilized smooth muscle
    • Trinkle-Mulcahy, L., K. Ichikawa, D.J. Hartshorne, M.J. Siegman, and T.M. Butler. 1995. Thiophosphorylation of the 130-kDa subunit is associated with a decreased activity of myosin light chain phosphatase in alpha-toxin-permeabilized smooth muscle. J. Biol. Chem. 270:18191-18194.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18191-18194
    • Trinkle-Mulcahy, L.1    Ichikawa, K.2    Hartshorne, D.J.3    Siegman, M.J.4    Butler, T.M.5
  • 50
    • 0026026368 scopus 로고
    • Regulation of smooth muscle myosin
    • Trybus, K.M. 1991. Regulation of smooth muscle myosin. Cell Motil. Cytoskelet. 18:81-85.
    • (1991) Cell Motil. Cytoskelet. , vol.18 , pp. 81-85
    • Trybus, K.M.1
  • 52
    • 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
  • 53
    • 0029892621 scopus 로고    scopus 로고
    • Cyclic GMP-dependent stimulation reverses G-protein-coupled inhibition of smooth muscle myosin light chain phosphate
    • Wu, X., A.V. Somlyo, and A.P. Somlyo. 1996. Cyclic GMP-dependent stimulation reverses G-protein-coupled inhibition of smooth muscle myosin light chain phosphate. Biochem. Biophys. Res. Commun. 220:658-663.
    • (1996) Biochem. Biophys. Res. Commun. , vol.220 , pp. 658-663
    • Wu, X.1    Somlyo, A.V.2    Somlyo, A.P.3
  • 54
    • 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
  • 55
    • 0025272184 scopus 로고
    • Mitosis-specific phosphorylation causes 83K non-muscle caldesmon to dissociate from microfilaments
    • Yamashiro, S., Y. Yamakita, R. Ishikawa, and F. Matsumura. 1990. Mitosis-specific phosphorylation causes 83K non-muscle caldesmon to dissociate from microfilaments. Nature. 344:675-678.
    • (1990) Nature , vol.344 , pp. 675-678
    • Yamashiro, S.1    Yamakita, Y.2    Ishikawa, R.3    Matsumura, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.