메뉴 건너뛰기




Volumn 4, Issue 2, 1998, Pages 116-127

Capping and dynamic relation between domains 1 and 2 of gelsolin

Author keywords

Actin; Capping proteins; Gelsolin; Synthetic peptides

Indexed keywords

ACTIN; GELSOLIN; PEPTIDE FRAGMENT; TRYPTOPHAN;

EID: 0032037457     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1099-1387(199804)4:2<116::aid-psc135>3.0.co;2-r     Document Type: Article
Times cited : (8)

References (45)
  • 1
    • 0030023293 scopus 로고    scopus 로고
    • Cap Z, a calcium insensitive capping protein in resting and activated platelets
    • V. T. Nachmias, R. Golla, J. F. Casella and E. Barron- Casella (1996). Cap Z, a calcium insensitive capping protein in resting and activated platelets. FEBS Lett. 387, 258-262.
    • (1996) FEBS Lett. , vol.387 , pp. 258-262
    • Nachmias, V.T.1    Golla, R.2    Casella, J.F.3    Barron- Casella, E.4
  • 2
    • 0021984210 scopus 로고
    • Effect of capping protein on the kinetics of actin polymerization
    • J. A. Cooper and T. D. Pollard (1985). Effect of capping protein on the kinetics of actin polymerization. Biochemistry 24, 793-799.
    • (1985) Biochemistry , vol.24 , pp. 793-799
    • Cooper, J.A.1    Pollard, T.D.2
  • 3
    • 0026089715 scopus 로고
    • Two of the three actin-binding domains of gelsolin bind to the same subdomain of actin. Implications of capping and severing mechanisms
    • B. Pope, M. Way and A. G. Weeds (1991). Two of the three actin-binding domains of gelsolin bind to the same subdomain of actin. Implications of capping and severing mechanisms. FEBS Lett. 280, 70-74.
    • (1991) FEBS Lett. , vol.280 , pp. 70-74
    • Pope, B.1    Way, M.2    Weeds, A.G.3
  • 4
    • 0027299745 scopus 로고
    • On the crawling of animal cells
    • T. P. Stossel (1993). On the crawling of animal cells. Science 260, 1086-1094.
    • (1993) Science , vol.260 , pp. 1086-1094
    • Stossel, T.P.1
  • 5
    • 0025782925 scopus 로고
    • Enhanced motility in NIH 3T3 fibroblasts that overexpress gelsolin
    • C. C. Cunningham, T. P. Stossel and D. J. Kwiatkowski (1991). Enhanced motility in NIH 3T3 fibroblasts that overexpress gelsolin. Science 251, 1233-1236.
    • (1991) Science , vol.251 , pp. 1233-1236
    • Cunningham, C.C.1    Stossel, T.P.2    Kwiatkowski, D.J.3
  • 6
    • 0028897520 scopus 로고
    • Role of gelsolin in the formation and organization of triton soluble F-actin, during myeloïd differentiation of HL-60 cells
    • R. G. Watts (1995). Role of gelsolin in the formation and organization of triton soluble F-actin, during myeloïd differentiation of HL-60 cells. Blood 85, 2212-2221.
    • (1995) Blood , vol.85 , pp. 2212-2221
    • Watts, R.G.1
  • 7
    • 0023894120 scopus 로고
    • Gelsolin has three actin-binding sites
    • J. Bryan, (1988). Gelsolin has three actin-binding sites. J. Cell Biol. 106, 1553-1562.
    • (1988) J. Cell Biol. , vol.106 , pp. 1553-1562
    • Bryan, J.1
  • 8
    • 0026495427 scopus 로고
    • Evidence for functional homology in the F-actin binding domains of gelsolin and alpha-actinin: Implications for the requirements of severing and capping
    • M. Way, B. Pope and A. G. Weeds (1992). Evidence for functional homology in the F-actin binding domains of gelsolin and alpha-actinin: Implications for the requirements of severing and capping. J. Cell. Biol. 119, 835-842.
    • (1992) J. Cell. Biol. , vol.119 , pp. 835-842
    • Way, M.1    Pope, B.2    Weeds, A.G.3
  • 9
    • 0027258984 scopus 로고
    • The Ca(2+)-induced conformational change of gelsolin is located in the carboxyl-terminal of the molecule
    • T. Hellweg, H. Huissen and W. Eimer (1993). The Ca(2+)-induced conformational change of gelsolin is located in the carboxyl-terminal of the molecule. Biophys. J. 65, 799-805.
    • (1993) Biophys. J. , vol.65 , pp. 799-805
    • Hellweg, T.1    Huissen, H.2    Eimer, W.3
  • 10
    • 0024318706 scopus 로고
    • Expression of human plasma gelsolin in Escherichia coli and dissection of actin binding sites by segmental deletion mutagenesis
    • M. Way, 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
  • 11
    • 0026605823 scopus 로고
    • Are the conserved sequences in segment 1 of gelsolin important for binding actin?
    • M. Way, B. Pope and A. G. Weeds (1992). Are the conserved sequences in segment 1 of gelsolin important for binding actin? J. Cell. Biol. 116, 1135-1143.
    • (1992) J. Cell. Biol. , vol.116 , pp. 1135-1143
    • Way, M.1    Pope, B.2    Weeds, A.G.3
  • 12
    • 0028235759 scopus 로고
    • The actin side-binding domain of gelsolin also caps actin filaments. Implication for actin filament severing
    • H. Q. Sun, D. C. Wooten, P. A. Janmey and H. L. Yin (1994). The actin side-binding domain of gelsolin also caps actin filaments. Implication for actin filament severing. J. Biol. Chem. 269, 9473-9479.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9473-9479
    • Sun, H.Q.1    Wooten, D.C.2    Janmey, P.A.3    Yin, H.L.4
  • 13
    • 0027134766 scopus 로고
    • The secrets of severing?
    • M. Way and P. Matsudaira (1993). The secrets of severing? Current Biol 3, 887-890.
    • (1993) Current Biol , vol.3 , pp. 887-890
    • Way, M.1    Matsudaira, P.2
  • 14
    • 0028921170 scopus 로고
    • Definition of an interface implicated in gelsolin binding to the sides of actin filaments
    • J. Feinberg, Y. Benyamin and C. Roustan (1995). Definition of an interface implicated in gelsolin binding to the sides of actin filaments. Biochem. Biophys. Res. Commun 209, 426-432.
    • (1995) Biochem. Biophys. Res. Commun , vol.209 , pp. 426-432
    • Feinberg, J.1    Benyamin, Y.2    Roustan, C.3
  • 15
    • 0027251071 scopus 로고
    • Structure of gelsolin segment 1-actin complex and the mechanism of filament severing
    • P. J. McLaughlin, J. T. Gooch, H. G. Mannhertz 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    Mannhertz, H.G.3    Weeds, A.G.4
  • 16
    • 0028863184 scopus 로고
    • Molecular model of an actin filament capped by a severing protein
    • A. McGooch and M. Way (1995). Molecular model of an actin filament capped by a severing protein. J. Struct Biol. 115, 144-150.
    • (1995) J. Struct Biol. , vol.115 , pp. 144-150
    • McGooch, A.1    Way, M.2
  • 17
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • J. A. Spudich and S. Watt (1971). The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 249, 4866-4871.
    • (1971) J. Biol. Chem. , vol.249 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 18
    • 0018789686 scopus 로고
    • Fluorescence energy transfer between subfragment-1 and actin points in the rigor complex of actosubfragment-1
    • R. Takashi (1979). Fluorescence energy transfer between subfragment-1 and actin points in the rigor complex of actosubfragment-1. Biochemistry 18, 5164-5169.
    • (1979) Biochemistry , vol.18 , pp. 5164-5169
    • Takashi, R.1
  • 19
    • 0019427215 scopus 로고
    • Fluorometry study of N-(1-pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin
    • T. Kouyama and K. Mihashi (1981). Fluorometry study of N-(1-pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin. Eur. J. Biochem. 114, 33-38.
    • (1981) Eur. J. Biochem. , vol.114 , pp. 33-38
    • Kouyama, T.1    Mihashi, K.2
  • 20
    • 0022341502 scopus 로고
    • Bovin serum brevin. Purification by hydrophobic chromatography and properties
    • Z. Soua, F. Porte, M. C. Harricane, J. Feinberg and J. P. Capony (1985). Bovin serum brevin. Purification by hydrophobic chromatography and properties. Eur. J. Biochem. 153, 275-287.
    • (1985) Eur. J. Biochem. , vol.153 , pp. 275-287
    • Soua, Z.1    Porte, F.2    Harricane, M.C.3    Feinberg, J.4    Capony, J.P.5
  • 21
    • 0027312838 scopus 로고
    • Definition of the EGTA-independent interface involved in the serum gelsolin-actin complex
    • J. Felnberg, J. P. Capony, Y. Benyamin and C. Roustan (1993). Definition of the EGTA-independent interface involved in the serum gelsolin-actin complex. Biochem. J. 293, 813-817,
    • (1993) Biochem. J. , vol.293 , pp. 813-817
    • Felnberg, J.1    Capony, J.P.2    Benyamin, Y.3    Roustan, C.4
  • 23
    • 0030053370 scopus 로고    scopus 로고
    • Promod and Swiss-model: Internet-based tools for automated comparative protein modelling
    • M. C. Peitsch (1996). Promod and Swiss-model: Internet-based tools for automated comparative protein modelling. Biochem. Soc. Trans. 24, 274-279.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 274-279
    • Peitsch, M.C.1
  • 25
    • 0026604226 scopus 로고
    • Localization of a myosin subfragment 1 interaction site on the C-terminal part of actin
    • J.P. Labbé, M. Boyer, C. Roustan and Y. Benyamin (1992). Localization of a myosin subfragment 1 interaction site on the C-terminal part of actin. Biochem. J. 284, 75-79.
    • (1992) Biochem. J. , vol.284 , pp. 75-79
    • Labbé, J.P.1    Boyer, M.2    Roustan, C.3    Benyamin, Y.4
  • 26
    • 0026774746 scopus 로고
    • Localization and identification of actin structures involved in the fllamin-actin interaction
    • C. Mejean, M. C. Lebart, M. Boyer, C. Roustan and Y. Benyamin, (1992). Localization and identification of actin structures involved in the fllamin-actin interaction. Eur. J. Biochem. 209, 555-562.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 555-562
    • Mejean, C.1    Lebart, M.C.2    Boyer, M.3    Roustan, C.4    Benyamin, Y.5
  • 27
    • 0039552510 scopus 로고
    • 2+ induced proceed at pH 8 and 20°C
    • 2+ induced proceed at pH 8 and 20°C. Proc. Natl. Acad. Sci. USA 80, 6513-6517.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 6513-6517
    • Frieden, C.1
  • 28
    • 0028823009 scopus 로고
    • Spectroscopic studies of a phosphoinositide- Binding peptide from gelsolin: Behaviour in solutions of mixed solvent and anionic micelles
    • W. Xian, R. Vegners, P. A. Janmey and W. H. Braunlin (1995). Spectroscopic studies of a phosphoinositide- binding peptide from gelsolin: Behaviour in solutions of mixed solvent and anionic micelles. Biophys. J. 69, 2696-2702.
    • (1995) Biophys. J. , vol.69 , pp. 2696-2702
    • Xian, W.1    Vegners, R.2    Janmey, P.A.3    Braunlin, W.H.4
  • 29
    • 0023812318 scopus 로고
    • Sequence of human villin: A large duplicated domain homologous with other actin-severing proteins and a unique small carboxyl-terminal related to villin specificity
    • M. Arpin, E. Pringault, J. Finidori, A. Garcia, J. M. Jeltsch, J. Vandekerckhowe and D. Louvard (1988). Sequence of human villin: A large duplicated domain homologous with other actin-severing proteins and a unique small carboxyl-terminal related to villin specificity. J. Cell Biol. 107, 1759-1766.
    • (1988) J. Cell Biol. , vol.107 , pp. 1759-1766
    • Arpin, M.1    Pringault, E.2    Finidori, J.3    Garcia, A.4    Jeltsch, J.M.5    Vandekerckhowe, J.6    Louvard, D.7
  • 30
    • 0029889988 scopus 로고    scopus 로고
    • PHD: Predicting one-dimensional protein structure
    • B. Rost (1996). PHD: Predicting one-dimensional protein structure. Methods. Enzymol. 266, 525-539.
    • (1996) Methods. Enzymol. , vol.266 , pp. 525-539
    • Rost, B.1
  • 31
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • B. Rost and C. Sander (1993). Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol. 232, 584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 32
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • B. Rost and C. Sander (1994). Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 19, 55-72.
    • (1994) Proteins , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 33
    • 0025357111 scopus 로고
    • Protein secondary structures in water from second-derivative amide I infrared spectra
    • A. Dong, P. Huang and W. S. Caughey (1990). Protein secondary structures in water from second-derivative amide I infrared spectra. Biochemistry 29, 3303-3308.
    • (1990) Biochemistry , vol.29 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 34
    • 0019872602 scopus 로고
    • Conformations of (X-L-Pro-Y)2 cyclic hexapeptides. Preferred beta-turn conformers and implications for beta-turns in proteins
    • L. M. Gierasch, C. M. Deber, V. Madison, C. H. Niu and E. R Blout (1981). Conformations of (X-L-Pro-Y)2 cyclic hexapeptides. Preferred beta-turn conformers and implications for beta-turns in proteins. Biochemistry 20, 4730-4738.
    • (1981) Biochemistry , vol.20 , pp. 4730-4738
    • Gierasch, L.M.1    Deber, C.M.2    Madison, V.3    Niu, C.H.4    Blout, E.R.5
  • 35
    • 0018172307 scopus 로고
    • Does protamine dictate the direction of growth of the actin filaments?
    • E. Magri, M. Zaccarini and E. Grazi (1978). Does protamine dictate the direction of growth of the actin filaments? Biochem. Biophys. Res. Commun. 85, 35-41.
    • (1978) Biochem. Biophys. Res. Commun. , vol.85 , pp. 35-41
    • Magri, E.1    Zaccarini, M.2    Grazi, E.3
  • 36
    • 0026515991 scopus 로고
    • Identification and characterization of an actin-binding site of CapZ
    • C. Hug, T. M. Miller, M. A. Torres, J. F. Casella and J. A. Cooper (1992). Identification and characterization of an actin-binding site of CapZ. J. Cell Biol. 116, 923-931.
    • (1992) J. Cell Biol. , vol.116 , pp. 923-931
    • Hug, C.1    Miller, T.M.2    Torres, M.A.3    Casella, J.F.4    Cooper, J.A.5
  • 37
    • 0024421755 scopus 로고
    • Effect of CapZ, an actin capping protein of muscle, on the polymerization of actin
    • S. E. Caldwell, S. G. Heiss, V. Mermall and J. A. Cooper (1989). Effect of CapZ, an actin capping protein of muscle, on the polymerization of actin. Biochemistry 28, 8506-8514.
    • (1989) Biochemistry , vol.28 , pp. 8506-8514
    • Caldwell, S.E.1    Heiss, S.G.2    Mermall, V.3    Cooper, J.A.4
  • 38
    • 0025949804 scopus 로고
    • Role of the N- and C-terminal actin-binding domains of gelsolin in barbed filament end capping
    • A. Weber, M. Pring, S. L. Lin and J. Bryan (1991). Role of the N- and C-terminal actin-binding domains of gelsolin in barbed filament end capping. Biochemistry 30, 9327-9334.
    • (1991) Biochemistry , vol.30 , pp. 9327-9334
    • Weber, A.1    Pring, M.2    Lin, S.L.3    Bryan, J.4
  • 39
    • 0022487183 scopus 로고
    • Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain
    • D. J. Kwiatkowski, T. P. Stossel, S. H. Orkin, J. E. Mole, H. R. Colten and H. L. Yin (1986). Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain. Nature 323, 455-458.
    • (1986) Nature , vol.323 , pp. 455-458
    • Kwiatkowski, D.J.1    Stossel, T.P.2    Orkin, S.H.3    Mole, J.E.4    Colten, H.R.5    Yin, H.L.6
  • 40
    • 0030012195 scopus 로고    scopus 로고
    • Conformational changes in subdomain 1 of actin induced by proteolytic cleavage within the DNase I-binding loop: Energy transfer from tryptophan to AEDANS
    • I. Kuznetsova, O. Antropovax, K. Turoverov and S. Khaitlina (1996). Conformational changes in subdomain 1 of actin induced by proteolytic cleavage within the DNase I-binding loop: Energy transfer from tryptophan to AEDANS. FEBS Lett. 383, 105-108.
    • (1996) FEBS Lett. , vol.383 , pp. 105-108
    • Kuznetsova, I.1    Antropovax, O.2    Turoverov, K.3    Khaitlina, S.4
  • 41
    • 0030564835 scopus 로고    scopus 로고
    • Cooperativity in F-actin: Binding of gelsolin at the barbed end effects structure and dynamics of the whole filament
    • E. Prochniewicz, Q. Zhang, P. A. Janmey and D. D. Thomas (1996). Cooperativity in F-actin: Binding of gelsolin at the barbed end effects structure and dynamics of the whole filament. J. Mol. Biol. 260, 756-766.
    • (1996) J. Mol. Biol. , vol.260 , pp. 756-766
    • Prochniewicz, E.1    Zhang, Q.2    Janmey, P.A.3    Thomas, D.D.4
  • 42
    • 0018830967 scopus 로고
    • Cytochalasins inhibit nuclei-induced actin polymerization by blocking filament elongation
    • D. C. Lin, K. D. Tobin, M. Grumet and S. Lin (1980). Cytochalasins inhibit nuclei-induced actin polymerization by blocking filament elongation. J. Cell Biol. 84, 455-460.
    • (1980) J. Cell Biol. , vol.84 , pp. 455-460
    • Lin, D.C.1    Tobin, K.D.2    Grumet, M.3    Lin, S.4
  • 44
    • 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
  • 45
    • 0023008203 scopus 로고
    • The actin filament-severing domain of plasma gelsolin
    • C. Chaponnier, 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.