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Volumn 407, Issue 5, 2011, Pages 673-686

A proteomic study of myosin II motor proteins during tumor cell migration

Author keywords

cell migration; cytoskeleton; myosin II; phosphorylation

Indexed keywords

CASEIN KINASE II; FIBRONECTIN; INTEGRIN; MYOSIN HEAVY CHAIN; MYOSIN II; PROTEIN KINASE C; RNA;

EID: 79952739523     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.02.010     Document Type: Article
Times cited : (31)

References (30)
  • 1
    • 39449101285 scopus 로고    scopus 로고
    • Nonmuscle myosin II moves in new directions
    • Conti, M. A. & Adelstein, R. S. (2008). Nonmuscle myosin II moves in new directions. J. Cell Sci. 121, 11-18.
    • (2008) J. Cell Sci. , vol.121 , pp. 11-18
    • Conti, M.A.1    Adelstein, R.S.2
  • 3
    • 77952902430 scopus 로고    scopus 로고
    • Mechanisms of motility in metastasizing cells
    • Yilmaz, M. & Christofori, G. (2010). Mechanisms of motility in metastasizing cells. Mol. Cancer Res. 8, 629-642.
    • (2010) Mol. Cancer Res. , vol.8 , pp. 629-642
    • Yilmaz, M.1    Christofori, G.2
  • 6
    • 33745625368 scopus 로고    scopus 로고
    • PAK1 and aPKCzeta regulate myosin II-B phosphorylation: A novel signaling pathway regulating filament assembly
    • Even-Faitelson, L. & Ravid, S. (2006). PAK1 and aPKCzeta regulate myosin II-B phosphorylation: a novel signaling pathway regulating filament assembly. Mol. Biol. Cell, 17, 2869-2881.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2869-2881
    • Even-Faitelson, L.1    Ravid, S.2
  • 7
    • 0024362253 scopus 로고
    • Antigen-induced secretion of histamine and the phosphorylation of myosin by protein kinase C in rat basophilic leukemia cells
    • Ludowyke, R. I., Peleg, I., Beaven, M. A. & Adelstein, R. S. (1989). Antigen-induced secretion of histamine and the phosphorylation of myosin by protein kinase C in rat basophilic leukemia cells. J. Biol. Chem. 264, 12492-12501.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12492-12501
    • Ludowyke, R.I.1    Peleg, I.2    Beaven, M.A.3    Adelstein, R.S.4
  • 8
    • 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. (2007). Myosin-IIA heavy-chain phosphorylation regulates the motility of MDA-MB-231 carcinoma cells. Mol. Biol. Cell, 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
  • 9
    • 18244385740 scopus 로고    scopus 로고
    • Regulation of myosin-IIA assembly and Mts1 binding by heavy chain phosphorylation
    • DOI 10.1021/bi0500776
    • Dulyaninova, N. G., Malashkevich, V. N., Almo, S. C. & Bresnick, A. R. (2005). Regulation of myosin-IIA assembly and Mts1 binding by heavy chain phosphorylation. Biochemistry, 44, 6867-6876. (Pubitemid 40632405)
    • (2005) Biochemistry , vol.44 , Issue.18 , pp. 6867-6876
    • Dulyaninova, N.G.1    Malashkevich, V.N.2    Almo, S.C.3    Bresnick, A.R.4
  • 10
    • 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. (2009). Multiple regulatory steps control mammalian nonmuscle myosin II assembly in live cells. Mol. Biol. Cell, 20, 338-347.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 338-347
    • Breckenridge, M.T.1    Dulyaninova, N.G.2    Egelhoff, T.T.3
  • 11
    • 0025092579 scopus 로고
    • The 204-kDa smooth muscle myosin heavy chain is phosphorylated in intact cells by casein kinase II on a serine near the carboxyl terminus
    • Kelley, C. A. & Adelstein, R. S. (1990). The 204-kDa smooth muscle myosin heavy chain is phosphorylated in intact cells by casein kinase II on a serine near the carboxyl terminus. J. Biol. Chem. 265, 17876-17882.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17876-17882
    • Kelley, C.A.1    Adelstein, R.S.2
  • 12
    • 0032539586 scopus 로고    scopus 로고
    • Two nonmuscle myosin II heavy chain isoforms expressed in rabbit brains: Filament forming properties, the effects of phosphorylation by protein kinase C and casein kinase II, and location of the phosphorylation sites
    • DOI 10.1021/bi971959a
    • Murakami, N., Chauhan, V. P. & Elzinga, M. (1998). Two nonmuscle myosin II heavy chain isoforms expressed in rabbit brains: filament forming properties, the effects of phosphorylation by protein kinase C and casein kinase II, and location of the phosphorylation sites. Biochemistry, 37, 1989-2003. (Pubitemid 28099823)
    • (1998) Biochemistry , vol.37 , Issue.7 , pp. 1989-2003
    • Murakami, N.1    Chauhan, V.P.S.2    Elzinga, M.3
  • 13
    • 0025095403 scopus 로고
    • Amino acid sequence around the serine phosphorylated by casein kinase II in brain myosin heavy chain
    • Murakami, N., Healy-Louie, G. & Elzinga, M. (1990). Amino acid sequence around the serine phosphorylated by casein kinase II in brain myosin heavy chain. J. Biol. Chem. 265, 1041-1047.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1041-1047
    • Murakami, N.1    Healy-Louie, G.2    Elzinga, M.3
  • 14
    • 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
    • Betapudi, V., Licate, L. S. & Egelhoff, T. T. (2006). Distinct roles of nonmuscle myosin II isoforms in the regulation of MDA-MB-231 breast cancer cell spreading and migration. Cancer Res. 66, 4725-4733.
    • (2006) Cancer Res. , vol.66 , pp. 4725-4733
    • Betapudi, V.1    Licate, L.S.2    Egelhoff, T.T.3
  • 15
    • 77649103340 scopus 로고    scopus 로고
    • Myosin II motor proteins with different functions determine the fate of lamellipodia extension during cell spreading
    • Betapudi, V. (2010). Myosin II motor proteins with different functions determine the fate of lamellipodia extension during cell spreading. PLoS ONE, 5, e8560.
    • (2010) PLoS ONE , vol.5
    • Betapudi, V.1
  • 18
    • 0031917782 scopus 로고    scopus 로고
    • Specific localization of serine 19 phosphorylated myosin II during cell locomotion and mitosis of cultured cells
    • DOI 10.1083/jcb.140.1.119
    • Matsumura, F., Ono, S., Yamakita, Y., Totsukawa, G. & Yamashiro, S. (1998). Specific localization of serine 19 phosphorylated myosin II during cell locomotion and mitosis of cultured cells. J. Cell Biol. 140, 119-129. (Pubitemid 28070900)
    • (1998) Journal of Cell Biology , vol.140 , Issue.1 , pp. 119-129
    • Matsumura, F.1    Ono, S.2    Yamakita, Y.3    Totsukawa, G.4    Yamashiro, S.5
  • 19
    • 0035794231 scopus 로고    scopus 로고
    • WD repeat domains target Dictyostelium myosin heavy chain kinases by binding directly to myosin filaments
    • Steimle, P. A., Naismith, T., Licate, L. & Egelhoff, T. T. (2001). WD repeat domains target Dictyostelium myosin heavy chain kinases by binding directly to myosin filaments. J. Biol. Chem. 276, 6853-6860.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6853-6860
    • Steimle, P.A.1    Naismith, T.2    Licate, L.3    Egelhoff, T.T.4
  • 20
    • 0027769523 scopus 로고
    • Phosphorylation of vertebrate nonmuscle and smooth muscle myosin heavy chains and light chains
    • Moussavi, R. S., Kelley, C. A. & Adelstein, R. S. (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
  • 21
    • 69049113869 scopus 로고    scopus 로고
    • Protein kinase CK2 in health and disease: Protein kinase CK2: From structures to insights
    • Niefind, K., Raaf, J. & Issinger, O. G. (2009). Protein kinase CK2 in health and disease: protein kinase CK2: from structures to insights. Cell Mol. Life Sci. 66, 1800-1816.
    • (2009) Cell Mol. Life Sci. , vol.66 , pp. 1800-1816
    • Niefind, K.1    Raaf, J.2    Issinger, O.G.3
  • 22
    • 4043162055 scopus 로고    scopus 로고
    • Unbalanced activation of ERK1/2 and MEK1/2 in apigenin-induced HeLa cell death
    • Llorens, F., Miro, F. A., Casanas, A., Roher, N., Garcia, L., Plana, M. et al. (2004). Unbalanced activation of ERK1/2 and MEK1/2 in apigenin-induced HeLa cell death. Exp. Cell Res. 299, 15-26.
    • (2004) Exp. Cell Res. , vol.299 , pp. 15-26
    • Llorens, F.1    Miro, F.A.2    Casanas, A.3    Roher, N.4    Garcia, L.5    Plana, M.6
  • 24
    • 33746215280 scopus 로고    scopus 로고
    • 1917 is mediated by protein kinase CbetaII and coincides with the onset of stimulated degranulation of RBL-2H3 mast cells
    • Ludowyke, R. I., Elgundi, Z., Kranenburg, T., Stehn, J. R., Schmitz-Peiffer, C., Hughes, W. E. & Biden, T. J. (2006). Phosphorylation of nonmuscle myosin heavy chain IIA on Ser1917 is mediated by protein kinase C beta II and coincides with the onset of stimulated degranulation of RBL-2H3 mast cells. J. Immunol. 177, 1492-1499. (Pubitemid 44092482)
    • (2006) Journal of Immunology , vol.177 , Issue.3 , pp. 1492-1499
    • Ludowyke, R.I.1    Elgundi, Z.2    Kranenburg, T.3    Stehn, J.R.4    Schmitz-Peiffer, C.5    Hughes, W.E.6    Biden, T.J.7
  • 27
    • 70349320107 scopus 로고    scopus 로고
    • Protein kinase CK2 in health and disease: CK2: A key player in cancer biology
    • Trembley, J. H., Wang, G., Unger, G., Slaton, J. & Ahmed, K. (2009). Protein kinase CK2 in health and disease: CK2: a key player in cancer biology. Cell Mol. Life Sci. 66, 1858-1867.
    • (2009) Cell Mol. Life Sci. , vol.66 , pp. 1858-1867
    • Trembley, J.H.1    Wang, G.2    Unger, G.3    Slaton, J.4    Ahmed, K.5
  • 28
    • 0034687146 scopus 로고    scopus 로고
    • Two distinct mechanisms for regulation of nonmuscle myosin assembly via the heavy chain: Phosphorylation for MIIB and mts 1 binding for MIIA
    • Murakami, N., Kotula, L. & Hwang, Y. W. (2000). Two distinct mechanisms for regulation of nonmuscle myosin assembly via the heavy chain: phosphorylation for MIIB and mts 1 binding for MIIA. Biochemistry, 39, 11441-11451.
    • (2000) Biochemistry , vol.39 , pp. 11441-11451
    • Murakami, N.1    Kotula, L.2    Hwang, Y.W.3
  • 29
    • 77952891041 scopus 로고    scopus 로고
    • A microfluidic imaging chamber for the direct observation of chemotactic transmigration
    • Breckenridge, M. T., Egelhoff, T. T. & Baskaran, H. (2010). A microfluidic imaging chamber for the direct observation of chemotactic transmigration. Biomed. Microdevices, 12, 543-553.
    • (2010) Biomed. Microdevices , vol.12 , pp. 543-553
    • Breckenridge, M.T.1    Egelhoff, T.T.2    Baskaran, H.3
  • 30
    • 18244371902 scopus 로고    scopus 로고
    • Identification and characterization of a novel α-kinase with a von Willebrand factor α-like motif localized to the contractile vacuole and Golgi complex in Dictyostelium discoideum
    • Betapudi, V., Mason, C., Licate, L. & Egelhoff, T. T. (2005). Identification and characterization of a novel α-kinase with a von Willebrand factor α-like motif localized to the contractile vacuole and Golgi complex in Dictyostelium discoideum. Mol. Biol. Cell, 16, 2248-2262.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2248-2262
    • Betapudi, V.1    Mason, C.2    Licate, L.3    Egelhoff, T.T.4


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