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Volumn 369, Issue 2, 2008, Pages 654-659

Calmodulin-like protein enhances myosin-10 translation

Author keywords

Calmodulin like protein; Chaperone; In vitro translation; IQ motif; Myosin light chain; Myosin 10

Indexed keywords

CALMODULIN; CALMODULIN LIKE PROTEIN; MESSENGER RNA; MYOSIN; MYOSIN 10; MYOSIN HEAVY CHAIN; UNCLASSIFIED DRUG;

EID: 40849097482     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.02.056     Document Type: Article
Times cited : (7)

References (22)
  • 3
    • 0038670331 scopus 로고    scopus 로고
    • Possible involvement of myosin-X in intercellular adhesion: importance of serial pleckstrin homology regions for intracellular localization
    • Yonezawa S., Yoshizaki N., Sano M., Hanai A., Masaki S., Takizawa T., Kageyama T., and Moriyama A. Possible involvement of myosin-X in intercellular adhesion: importance of serial pleckstrin homology regions for intracellular localization. Dev. Growth Differ. 45 (2003) 175-185
    • (2003) Dev. Growth Differ. , vol.45 , pp. 175-185
    • Yonezawa, S.1    Yoshizaki, N.2    Sano, M.3    Hanai, A.4    Masaki, S.5    Takizawa, T.6    Kageyama, T.7    Moriyama, A.8
  • 5
    • 33747622327 scopus 로고    scopus 로고
    • Myosin-X is a molecular motor that functions in filopodia formation
    • Bohil A.B., Robertson B.W., and Cheney R.E. Myosin-X is a molecular motor that functions in filopodia formation. Proc. Natl. Acad. Sci. USA 103 (2006) 12411-12416
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 12411-12416
    • Bohil, A.B.1    Robertson, B.W.2    Cheney, R.E.3
  • 7
    • 4644326930 scopus 로고    scopus 로고
    • A microtubule-binding myosin required for nuclear anchoring and spindle assembly
    • Weber K.L., Sokac A.M., Berg J.S., Cheney R.E., and Bement W.M. A microtubule-binding myosin required for nuclear anchoring and spindle assembly. Nature 431 (2004) 325-329
    • (2004) Nature , vol.431 , pp. 325-329
    • Weber, K.L.1    Sokac, A.M.2    Berg, J.S.3    Cheney, R.E.4    Bement, W.M.5
  • 8
    • 33947596005 scopus 로고    scopus 로고
    • Integrin-mediated adhesion orients the spindle parallel to the substratum in an EB1- and myosin X-dependent manner
    • Toyoshima F., and Nishida E. Integrin-mediated adhesion orients the spindle parallel to the substratum in an EB1- and myosin X-dependent manner. EMBO J. 26 (2007) 1487-1498
    • (2007) EMBO J. , vol.26 , pp. 1487-1498
    • Toyoshima, F.1    Nishida, E.2
  • 9
    • 0033766768 scopus 로고    scopus 로고
    • Myosin-X, a novel myosin with pleckstrin homology domains, associates with regions of dynamic actin
    • Berg J.S., Derfler B.H., Pennisi C.M., Corey D.P., and Cheney R.E. Myosin-X, a novel myosin with pleckstrin homology domains, associates with regions of dynamic actin. J. Cell Sci. 113 (2000) 3439-3451
    • (2000) J. Cell Sci. , vol.113 , pp. 3439-3451
    • Berg, J.S.1    Derfler, B.H.2    Pennisi, C.M.3    Corey, D.P.4    Cheney, R.E.5
  • 11
    • 0029025172 scopus 로고
    • Regulation of calmodulin-binding myosins
    • Wolenski J.S. Regulation of calmodulin-binding myosins. Trends Cell Biol. 5 (1995) 310-316
    • (1995) Trends Cell Biol. , vol.5 , pp. 310-316
    • Wolenski, J.S.1
  • 12
    • 0035853701 scopus 로고    scopus 로고
    • The tumor-sensitive calmodulin-like protein is a specific light chain of human unconventional myosin X
    • Rogers M.S., and Strehler E.E. The tumor-sensitive calmodulin-like protein is a specific light chain of human unconventional myosin X. J. Biol. Chem. 276 (2001) 12182-12189
    • (2001) J. Biol. Chem. , vol.276 , pp. 12182-12189
    • Rogers, M.S.1    Strehler, E.E.2
  • 13
    • 0026883687 scopus 로고
    • Protein product of a human intronless calmodulin-like gene shows tissue-specific expression and reduced abundance in transformed cells
    • Yaswen P., Smoll A., Hosoda J., Parry G., and Stampfer M.R. Protein product of a human intronless calmodulin-like gene shows tissue-specific expression and reduced abundance in transformed cells. Cell Growth Differ. 3 (1992) 335-345
    • (1992) Cell Growth Differ. , vol.3 , pp. 335-345
    • Yaswen, P.1    Smoll, A.2    Hosoda, J.3    Parry, G.4    Stampfer, M.R.5
  • 14
    • 0035879284 scopus 로고    scopus 로고
    • Human calmodulin-like protein is an epithelial-specific protein regulated during keratinocyte differentiation
    • Rogers M.S., Kobayashi T., Pittelkow M.R., and Strehler E.E. Human calmodulin-like protein is an epithelial-specific protein regulated during keratinocyte differentiation. Exp. Cell Res. 267 (2001) 216-224
    • (2001) Exp. Cell Res. , vol.267 , pp. 216-224
    • Rogers, M.S.1    Kobayashi, T.2    Pittelkow, M.R.3    Strehler, E.E.4
  • 15
    • 34047250470 scopus 로고    scopus 로고
    • Calmodulin-like protein increases filopodia-dependent cell motility via up-regulation of myosin-10
    • Bennett R.D., Mauer A.S., and Strehler E.E. Calmodulin-like protein increases filopodia-dependent cell motility via up-regulation of myosin-10. J. Biol. Chem. 282 (2007) 3205-3212
    • (2007) J. Biol. Chem. , vol.282 , pp. 3205-3212
    • Bennett, R.D.1    Mauer, A.S.2    Strehler, E.E.3
  • 16
    • 0027085882 scopus 로고
    • Characterization of the human calmodulin-like protein expressed in Escherichia coli
    • Rhyner J.A., Koller M., Durussel-Gerber I., Cox J.A., and Strehler E.E. Characterization of the human calmodulin-like protein expressed in Escherichia coli. Biochemistry 31 (1992) 12826-12832
    • (1992) Biochemistry , vol.31 , pp. 12826-12832
    • Rhyner, J.A.1    Koller, M.2    Durussel-Gerber, I.3    Cox, J.A.4    Strehler, E.E.5
  • 17
    • 0033170851 scopus 로고    scopus 로고
    • Loss of immunoreactivity for human calmodulin-like protein is an early event in breast cancer development
    • Rogers M.S., Foley M.A., Crotty T.B., Hartmann L.C., Ingle J.N., Roche P.C., and Strehler E.E. Loss of immunoreactivity for human calmodulin-like protein is an early event in breast cancer development. Neoplasia 1 (1999) 220-225
    • (1999) Neoplasia , vol.1 , pp. 220-225
    • Rogers, M.S.1    Foley, M.A.2    Crotty, T.B.3    Hartmann, L.C.4    Ingle, J.N.5    Roche, P.C.6    Strehler, E.E.7
  • 18
    • 0029024163 scopus 로고
    • The translocation, folding, assembly and redox-dependent degradation of secretory and membrane proteins in semi-permeabilized mammalian cells
    • Wilson R., Allen A.J., Oliver J., Brookman J.L., High S., and Bulleid N.J. The translocation, folding, assembly and redox-dependent degradation of secretory and membrane proteins in semi-permeabilized mammalian cells. Biochem. J. 307 (1995) 679-687
    • (1995) Biochem. J. , vol.307 , pp. 679-687
    • Wilson, R.1    Allen, A.J.2    Oliver, J.3    Brookman, J.L.4    High, S.5    Bulleid, N.J.6
  • 19
    • 0035823492 scopus 로고    scopus 로고
    • Motor function and regulation of myosin X
    • Homma K., Saito J., Ikebe R., and Ikebe M. Motor function and regulation of myosin X. J. Biol. Chem. 276 (2001) 34348-34354
    • (2001) J. Biol. Chem. , vol.276 , pp. 34348-34354
    • Homma, K.1    Saito, J.2    Ikebe, R.3    Ikebe, M.4
  • 20
    • 38049037417 scopus 로고    scopus 로고
    • Sequential roles for myosin-X in BMP6-dependent filopodial extension, migration, and activation of BMP receptors
    • Pi X., Ren R., Kelley R., Zhang C., Moser M., Bohil A.B., DiVito M., Cheney R.E., and Patterson C. Sequential roles for myosin-X in BMP6-dependent filopodial extension, migration, and activation of BMP receptors. J. Cell Biol. 179 (2007) 1568-1582
    • (2007) J. Cell Biol. , vol.179 , pp. 1568-1582
    • Pi, X.1    Ren, R.2    Kelley, R.3    Zhang, C.4    Moser, M.5    Bohil, A.B.6    DiVito, M.7    Cheney, R.E.8    Patterson, C.9
  • 21
    • 0036438894 scopus 로고    scopus 로고
    • Regulation of peptide-chain elongation in mammalian cells
    • Browne G.J., and Proud C.G. Regulation of peptide-chain elongation in mammalian cells. Eur. J. Biochem. 269 (2002) 5360-5368
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5360-5368
    • Browne, G.J.1    Proud, C.G.2
  • 22


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.