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Volumn 75, Issue 6, 1998, Pages 3092-3100

Severing of F-actin by the amino-terminal half of gelsolin suggests internal cooperativity in gelsolin

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN BINDING PROTEIN; CALCIUM ION; F ACTIN; GELSOLIN; MAGNESIUM ION; PHALLOIDIN;

EID: 0031738101     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77750-1     Document Type: Article
Times cited : (53)

References (28)
  • 1
    • 0028603483 scopus 로고
    • 2+ affect the rate at which gelsolin severs F-actin
    • 2+ affect the rate at which gelsolin severs F-actin. J. Biol. Chem. 269:32916-32923.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32916-32923
    • Allen, P.G.1    Janmey, P.A.2
  • 3
    • 0022551969 scopus 로고
    • 2+ regulatory domain in human brevin
    • 2+ regulatory domain in human brevin. J. Cell Biol. 102:1439-1446.
    • (1986) J. Cell Biol. , vol.102 , pp. 1439-1446
    • Bryan, J.1    Hwo, S.2
  • 4
    • 0030829385 scopus 로고    scopus 로고
    • The crystal structure of plasma gelsolin: Implications for actin severing, capping and nucleation
    • Burtnick, L. D., E. K. Koepf, J. Grimes, E. Y. Jones, D. I. Stuart, P. J. McGlaughlin, and R. C. Robinson. 1997. The crystal structure of plasma gelsolin: implications for actin severing, capping and nucleation. Cell. 90:661-670.
    • (1997) Cell , vol.90 , pp. 661-670
    • Burtnick, L.D.1    Koepf, E.K.2    Grimes, J.3    Jones, E.Y.4    Stuart, D.I.5    McGlaughlin, P.J.6    Robinson, R.C.7
  • 5
    • 0023008203 scopus 로고
    • The actin filament severing domain of plasma gelsolin
    • Chaponnier, C., P. A. Janmey, and H. L. Yin. 1986. The actin filament severing domain of plasma gelsolin. J Cell Biol. 103:1473-1481.
    • (1986) J Cell Biol. , vol.103 , pp. 1473-1481
    • Chaponnier, C.1    Janmey, P.A.2    Yin, H.L.3
  • 6
    • 0028902614 scopus 로고
    • 2+ binding sites of gelsolin that regulate association with actin
    • 2+ binding sites of gelsolin that regulate association with actin. Eur. J. Biochem. 229: 512-516.
    • (1995) Eur. J. Biochem. , vol.229 , pp. 512-516
    • Ditsch, A.1    Wegner, A.2
  • 8
    • 0027258984 scopus 로고
    • 2+-induced conformational change of gelsolin is located in the carboxyl-terminal half of the molecule
    • 2+-induced conformational change of gelsolin is located in the carboxyl-terminal half of the molecule. Biophys. J. 65:799-805.
    • (1993) Biophys. J. , vol.65 , pp. 799-805
    • Hellweg, T.1    Hinssen, H.2    Elmer, W.3
  • 11
    • 0027378260 scopus 로고
    • Actin filament annealing in the presence of ATP and phalloidin
    • Kinosian H. J., L. A. Selden, J. E. Estes, and L. C. Gershman. 1993. Actin filament annealing in the presence of ATP and phalloidin. Biochemistry. 32:12353-12357.
    • (1993) Biochemistry , vol.32 , pp. 12353-12357
    • Kinosian, H.J.1    Selden, L.A.2    Estes, J.E.3    Gershman, L.C.4
  • 12
    • 0030467026 scopus 로고    scopus 로고
    • Kinetics of gelsolin interaction with phalloidin-stabilized F-actin: Rate constants for binding and severing
    • Kinosian, H. J., L. A. Selden, J. E. Estes, and L. C. Gershman. 1996. Kinetics of gelsolin interaction with phalloidin-stabilized F-actin: rate constants for binding and severing. Biochemistry. 35:16550-16556.
    • (1996) Biochemistry , vol.35 , pp. 16550-16556
    • Kinosian, H.J.1    Selden, L.A.2    Estes, J.E.3    Gershman, L.C.4
  • 14
    • 0020551499 scopus 로고
    • Purification and characterization of a gelsolin-actin complex from human platelets
    • Kurth, M. C., L.-L. Wang, J. Dingus, and J. Bryan. 1983. Purification and characterization of a gelsolin-actin complex from human platelets. J. Biol. Chem. 258:10895-10903.
    • (1983) J. Biol. Chem. , vol.258 , pp. 10895-10903
    • Kurth, M.C.1    Wang, L.-L.2    Dingus, J.3    Bryan, J.4
  • 15
    • 0024566030 scopus 로고
    • Identification of critical functional and regulatory domains in gelsolin
    • Kwiatkowski, D. J., P. A. Janmey, and H. L. Yin. 1989. Identification of critical functional and regulatory domains in gelsolin. J. Cell Biol. 108:1717-1726.
    • (1989) J. Cell Biol. , vol.108 , pp. 1717-1726
    • Kwiatkowski, D.J.1    Janmey, P.A.2    Yin, H.L.3
  • 18
    • 0031879577 scopus 로고    scopus 로고
    • Determination of the gelsolin binding site on F-actin: Implications for severing and capping
    • McGough, A., W. Chiu, and M. Way. 1998. Determination of the gelsolin binding site on F-actin: implications for severing and capping. Biophys. J. 74:764-772.
    • (1998) Biophys. J. , vol.74 , pp. 764-772
    • McGough, A.1    Chiu, W.2    Way, M.3
  • 19
    • 0027251071 scopus 로고
    • Structure of gelsolin segment 1-actin complex and the mechanism of filament severing
    • McLaughlin, P. J., J. T. Gooch, H. G. Mannherz, and A. G. Weeds. 1993. Structure of gelsolin segment 1-actin complex and the mechanism of filament severing. Nature. 364:685-692.
    • (1993) Nature , vol.364 , pp. 685-692
    • McLaughlin, P.J.1    Gooch, J.T.2    Mannherz, H.G.3    Weeds, A.G.4
  • 20
    • 0000477435 scopus 로고
    • Computer calculation of equilibrium concentrations in mixtures of metal ions and complexing species
    • Perrin, D. D., and I. G. Sayce. 1967. Computer calculation of equilibrium concentrations in mixtures of metal ions and complexing species. Talanta. 14:833-842.
    • (1967) Talanta , vol.14 , pp. 833-842
    • Perrin, D.D.1    Sayce, I.G.2
  • 21
    • 0031443215 scopus 로고    scopus 로고
    • Probing the effects of calcium on gelsolin
    • Pope, B. J., J. T. Gooch, and A. G. Weeds. 1997. Probing the effects of calcium on gelsolin. Biochemistry. 36:15848-15855.
    • (1997) Biochemistry , vol.36 , pp. 15848-15855
    • Pope, B.J.1    Gooch, J.T.2    Weeds, A.G.3
  • 22
    • 0025363196 scopus 로고
    • Comparative two-dimensional gel analysis and microsequencing identifies gelsolin as one of the most prominent downregulated markers of transformed human fibroblast and epithelial cells
    • Vandekerckhove, J., G. Hauw, K. Vancompernolle, B. Honore, and J. Celis. 1990. Comparative two-dimensional gel analysis and microsequencing identifies gelsolin as one of the most prominent downregulated markers of transformed human fibroblast and epithelial cells. J. Cell Biol. 111:95-102.
    • (1990) J. Cell Biol. , vol.111 , pp. 95-102
    • Vandekerckhove, J.1    Hauw, G.2    Vancompernolle, K.3    Honore, B.4    Celis, J.5
  • 23
    • 0027145126 scopus 로고
    • Coordinated inhibition of actin-induced platelet aggregation by plasma gelsolin and vitamin D-binding protein
    • Vasconcellos, C. A., and S. E. Lind. 1993. Coordinated inhibition of actin-induced platelet aggregation by plasma gelsolin and vitamin D-binding protein. Blood. 82:3648-3657.
    • (1993) Blood , vol.82 , pp. 3648-3657
    • Vasconcellos, C.A.1    Lind, S.E.2
  • 24
    • 0024318706 scopus 로고
    • Expression of human plasma gelsolin in Escherichia coli and dissection of actin binding sites by segmental deletion mutagenesis
    • Way, M., J. Gooch, B. Pope, and A. G. Weeds. 1989. Expression of human plasma gelsolin in Escherichia coli and dissection of actin binding sites by segmental deletion mutagenesis. J. Cell Biol. 109:593-605.
    • (1989) J. Cell Biol. , vol.109 , pp. 593-605
    • Way, M.1    Gooch, J.2    Pope, B.3    Weeds, A.G.4
  • 25
    • 0028898094 scopus 로고
    • Identification of the trapped calcium in the gelsolin segment 1-actin complex: Implications for the role of calcium in the control of gelsolin activity
    • Weeds, A. G., J. Gooch, P. McLaughlin, B. Pope, M. Bengtsdotter, R. Karlsson. 1995. Identification of the trapped calcium in the gelsolin segment 1-actin complex: implications for the role of calcium in the control of gelsolin activity. FEBS Lett. 360:227-230.
    • (1995) FEBS Lett. , vol.360 , pp. 227-230
    • Weeds, A.G.1    Gooch, J.2    McLaughlin, P.3    Pope, B.4    Bengtsdotter, M.5    Karlsson, R.6
  • 26
    • 0018667209 scopus 로고
    • Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium-dependent regulatory protein
    • Yin, H., and T. P. Stossel. 1979. Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium-dependent regulatory protein. Nature. 281:583-586.
    • (1979) Nature , vol.281 , pp. 583-586
    • Yin, H.1    Stossel, T.P.2
  • 27
    • 0019729339 scopus 로고
    • 2+ control of actin filament length by gelsolin: Effects of macrophage gelsolin on actin polymerization
    • 2+ control of actin filament length by gelsolin: effects of macrophage gelsolin on actin polymerization. J. Biol. Chem. 256:9693-9697.
    • (1981) J. Biol. Chem. , vol.256 , pp. 9693-9697
    • Yin, H.1    Hartwig, J.H.2    Maruyama, K.3    Stossel, T.P.4
  • 28
    • 0025933678 scopus 로고
    • Chimeric and truncated gCap39 elucidate the requirements for actin filament severing and end capping by the gelsolin family of proteins
    • Yu, F-X, D. Zhou, and H. L. Yin. 1991. Chimeric and truncated gCap39 elucidate the requirements for actin filament severing and end capping by the gelsolin family of proteins. J. Biol. Chem. 267: 14616-14621.
    • (1991) J. Biol. Chem. , vol.267 , pp. 14616-14621
    • Yu, F.-X.1    Zhou, D.2    Yin, H.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.