메뉴 건너뛰기




Volumn 183, Issue 5, 2008, Pages 865-879

Cofilin is a pH sensor for actin free barbed end formation: role of phosphoinositide binding

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; COFILIN; GROWTH FACTOR; HISTIDINE; MUTANT PROTEIN; PHOSPHATIDYLINOSITIDE; SODIUM PROTON EXCHANGE PROTEIN 1; ACTIN BINDING PROTEIN; ACTIN DEPOLYMERIZING FACTOR; ACTOPHORIN PROTEIN, ACANTHAMOEBA; PHOSPHATIDYLINOSITOL; PLATELET DERIVED GROWTH FACTOR; PROTOZOAL PROTEIN; SODIUM PROTON EXCHANGE PROTEIN; UNCLASSIFIED DRUG;

EID: 58149293622     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.200804161     Document Type: Article
Times cited : (158)

References (86)
  • 1
    • 0037452660 scopus 로고    scopus 로고
    • Polarised migration: Cofilin holds the front
    • Bailly, M., and G.E. Jones. 2003. Polarised migration: cofilin holds the front. Curr. Biol. 13:R128-R130.
    • (2003) Curr. Biol , vol.13
    • Bailly, M.1    Jones, G.E.2
  • 2
    • 0036900955 scopus 로고    scopus 로고
    • ADF/cofilin and actin dynamics in disease
    • Bamburg, J.R., and O.P. Wiggan. 2002. ADF/cofilin and actin dynamics in disease. Trends Cell Biol. 12:598-605.
    • (2002) Trends Cell Biol , vol.12 , pp. 598-605
    • Bamburg, J.R.1    Wiggan, O.P.2
  • 3
    • 0018600258 scopus 로고
    • pH regulates the polymerization of actin in the sea urchin egg cortex
    • Begg, D.A., and L.I. Rebhun. 1979. pH regulates the polymerization of actin in the sea urchin egg cortex. J. Cell Biol. 83:241-248.
    • (1979) J. Cell Biol , vol.83 , pp. 241-248
    • Begg, D.A.1    Rebhun, L.I.2
  • 4
    • 2542611603 scopus 로고    scopus 로고
    • A proposed mechanism for cell polarization with no external cues
    • Bernstein, B.W., and J.R. Bamburg. 2004. A proposed mechanism for cell polarization with no external cues. CellMotil. Cytoskeleton. 58:96-103.
    • (2004) CellMotil. Cytoskeleton , vol.58 , pp. 96-103
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 6
    • 0034687235 scopus 로고    scopus 로고
    • Interactions of ADF/cofilin, Arp2/3 complex, capping protein and profilin in remodeling of branched actin filament networks
    • Blanchoin, L., T.D. Pollard, and R.D. Mullins. 2000. Interactions of ADF/cofilin, Arp2/3 complex, capping protein and profilin in remodeling of branched actin filament networks. Curr. Biol. 10:1273-1282.
    • (2000) Curr. Biol , vol.10 , pp. 1273-1282
    • Blanchoin, L.1    Pollard, T.D.2    Mullins, R.D.3
  • 7
    • 33646167587 scopus 로고    scopus 로고
    • Stimulation of actin polymerization by filament severing
    • Carlsson, A.E. 2006. Stimulation of actin polymerization by filament severing. Biophys. J. 90:413-422.
    • (2006) Biophys. J , vol.90 , pp. 413-422
    • Carlsson, A.E.1
  • 8
    • 23444454552 scopus 로고    scopus 로고
    • Case, D.A., T.E. Cheatham III, T. Darden, H. Gohlke, R. Luo, K.M. Merz Jr., A. Onufriev, C. Simmerling, B. Wang, and R.J. Woods. 2005. The Amber biomolecular simulation programs. J. Comput. Chem. 26:1668-1688.
    • Case, D.A., T.E. Cheatham III, T. Darden, H. Gohlke, R. Luo, K.M. Merz Jr., A. Onufriev, C. Simmerling, B. Wang, and R.J. Woods. 2005. The Amber biomolecular simulation programs. J. Comput. Chem. 26:1668-1688.
  • 9
    • 0031908252 scopus 로고    scopus 로고
    • EGF stimulates an increase in actin nucleation and filament number at the leading edge of the lamellipod in mammary adenocarcinoma cells
    • Chan, A.Y., S. Raft, M. Bailly, J.B. Wyckoff, J.E. Segall, and J.S. Condeelis. 1998. EGF stimulates an increase in actin nucleation and filament number at the leading edge of the lamellipod in mammary adenocarcinoma cells. J. Cell Sci. 111:199-211.
    • (1998) J. Cell Sci , vol.111 , pp. 199-211
    • Chan, A.Y.1    Raft, S.2    Bailly, M.3    Wyckoff, J.B.4    Segall, J.E.5    Condeelis, J.S.6
  • 10
    • 0034614942 scopus 로고    scopus 로고
    • Role of cofilin in epidermal growth factor-stimulated actin polymerization and lamellipod protrusion
    • Chan, A.Y., M. Bailly, N. Zebda, J.E. Segall, and J.S. Condeelis. 2000. Role of cofilin in epidermal growth factor-stimulated actin polymerization and lamellipod protrusion. J. Cell Biol. 148:531-542.
    • (2000) J. Cell Biol , vol.148 , pp. 531-542
    • Chan, A.Y.1    Bailly, M.2    Zebda, N.3    Segall, J.E.4    Condeelis, J.S.5
  • 11
    • 0033598956 scopus 로고    scopus 로고
    • Chaudhry, F.A., R.J. Reimer, D. Krizaj, D. Barber, J. Storm-Mathisen, D.R. Copenhagen, and R.H. Edwards. 1999. Molecular analysis of system N suggests novel physiological roles in nitrogen metabolism and synaptic transmission. Cell. 99:769-780.
    • Chaudhry, F.A., R.J. Reimer, D. Krizaj, D. Barber, J. Storm-Mathisen, D.R. Copenhagen, and R.H. Edwards. 1999. Molecular analysis of system N suggests novel physiological roles in nitrogen metabolism and synaptic transmission. Cell. 99:769-780.
  • 12
    • 0344796392 scopus 로고    scopus 로고
    • Two phases of actin polymerization display different dependencies on PI(3,4,5)P3 accumulation and have unique roles during chemotaxis
    • Chen, L., C. Janetopoulos, Y.E. Huang, M. Iijima, J. Borleis, and P.N. Devreotes. 2003. Two phases of actin polymerization display different dependencies on PI(3,4,5)P3 accumulation and have unique roles during chemotaxis. Mol. Biol. Cell. 14:5028-5037.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 5028-5037
    • Chen, L.1    Janetopoulos, C.2    Huang, Y.E.3    Iijima, M.4    Borleis, J.5    Devreotes, P.N.6
  • 13
    • 2642580847 scopus 로고    scopus 로고
    • In vitro activity differences between proteins of the ADF/cofilin family define two distinct subgroups
    • Chen, H., B.W. Bernstein, J.M. Sneider, J.A. Boyle, L.S. Minamide, and J.R. Bamburg. 2004. In vitro activity differences between proteins of the ADF/cofilin family define two distinct subgroups. Biochemistry. 43:7127-7142.
    • (2004) Biochemistry , vol.43 , pp. 7127-7142
    • Chen, H.1    Bernstein, B.W.2    Sneider, J.M.3    Boyle, J.A.4    Minamide, L.S.5    Bamburg, J.R.6
  • 15
    • 0035399959 scopus 로고    scopus 로고
    • How is actin polymerization nucleated in vivo?
    • Condeelis, J. 2001. How is actin polymerization nucleated in vivo? Trends Cell Biol. 11:288-293.
    • (2001) Trends Cell Biol , vol.11 , pp. 288-293
    • Condeelis, J.1
  • 16
    • 0030014646 scopus 로고    scopus 로고
    • Syk tyrosine kinase is required for immunoreceptor tyrosine activation motif-dependent actin assembly
    • Cox, D., P. Chang, T. Kurosaki, and S. Greenberg. 1996. Syk tyrosine kinase is required for immunoreceptor tyrosine activation motif-dependent actin assembly. J. Biol. Chem. 271:16597-16602.
    • (1996) J. Biol. Chem , vol.271 , pp. 16597-16602
    • Cox, D.1    Chang, P.2    Kurosaki, T.3    Greenberg, S.4
  • 17
    • 12244303674 scopus 로고    scopus 로고
    • ADF/cofilin controls cell polarity during fibroblast migration
    • Dawe, H.R., L.S. Minamide, J.R. Bamburg, and L.P. Cramer. 2003. ADF/cofilin controls cell polarity during fibroblast migration. Curr. Biol. 13:252-257.
    • (2003) Curr. Biol , vol.13 , pp. 252-257
    • Dawe, H.R.1    Minamide, L.S.2    Bamburg, J.R.3    Cramer, L.P.4
  • 18
    • 0037164808 scopus 로고    scopus 로고
    • Cell migration requires both ion transloca-tion and cytoskeletal anchoring by the Na-H exchanger NHE1
    • Denker, S.P., and D.L. Barber. 2002. Cell migration requires both ion transloca-tion and cytoskeletal anchoring by the Na-H exchanger NHE1. J. Cell Biol. 159:1087-1096.
    • (2002) J. Cell Biol , vol.159 , pp. 1087-1096
    • Denker, S.P.1    Barber, D.L.2
  • 19
    • 0034503095 scopus 로고    scopus 로고
    • Direct binding of the Na-H exchanger NHE1 to ERM proteins regulates the cortical cytoskeleton and cell shape independently of H(+) translocation
    • Denker, S.P., D.C. Huang, J. Orlowski, H. Furthmayr, and D.L. Barber. 2000. Direct binding of the Na-H exchanger NHE1 to ERM proteins regulates the cortical cytoskeleton and cell shape independently of H(+) translocation. Mol. Cell. 6:1425-1436.
    • (2000) Mol. Cell , vol.6 , pp. 1425-1436
    • Denker, S.P.1    Huang, D.C.2    Orlowski, J.3    Furthmayr, H.4    Barber, D.L.5
  • 20
    • 0036912348 scopus 로고    scopus 로고
    • Spatial regulation of actin dynamics: A tropomyosin-free, actin-rich compartment at the leading edge
    • DesMarais, V., I. Ichetovkin, J. Condeelis, and S.E. Hitchcock-DeGregori. 2002. Spatial regulation of actin dynamics: a tropomyosin-free, actin-rich compartment at the leading edge. J. CellSci. 115:4649-4660.
    • (2002) J. CellSci , vol.115 , pp. 4649-4660
    • DesMarais, V.1    Ichetovkin, I.2    Condeelis, J.3    Hitchcock-DeGregori, S.E.4
  • 25
    • 0035858886 scopus 로고    scopus 로고
    • Role of phosphatidylinositol 3' kinase and a downstream pleckstrin homology domain-containing protein in controlling chemotaxis in Dictyostelium
    • Funamoto, S., K. Milan, R. Meili, and R.A. Firtel. 2001. Role of phosphatidylinositol 3' kinase and a downstream pleckstrin homology domain-containing protein in controlling chemotaxis in Dictyostelium. J. Cell Biol. 153:795-810.
    • (2001) J. Cell Biol , vol.153 , pp. 795-810
    • Funamoto, S.1    Milan, K.2    Meili, R.3    Firtel, R.A.4
  • 26
    • 2342436150 scopus 로고    scopus 로고
    • Cofilin promotes actin polymerization and defines the direction of cell motility
    • Ghosh, M., X. Song, G. Mouneimne, M. Sidani, D.S. Lawrence, and J.S. Condeelis. 2004. Cofilin promotes actin polymerization and defines the direction of cell motility. Science. 304:743-746.
    • (2004) Science , vol.304 , pp. 743-746
    • Ghosh, M.1    Song, X.2    Mouneimne, G.3    Sidani, M.4    Lawrence, D.S.5    Condeelis, J.S.6
  • 27
    • 12344250639 scopus 로고    scopus 로고
    • Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics
    • Gohla, A., J. Birkenfeld, and G.M. Bokoch. 2005. Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics. Nat. Cell Biol. 7:21-29.
    • (2005) Nat. Cell Biol , vol.7 , pp. 21-29
    • Gohla, A.1    Birkenfeld, J.2    Bokoch, G.M.3
  • 28
    • 33749037156 scopus 로고    scopus 로고
    • The ARP2/3 complex: An actin nucleator comes of age
    • Goley, E.D., and M.D. Welch. 2006. The ARP2/3 complex: an actin nucleator comes of age. Nat. Rev. Mol. Cell Biol. 7:713-726.
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 713-726
    • Goley, E.D.1    Welch, M.D.2
  • 30
    • 1642310340 scopus 로고    scopus 로고
    • Glide: A new approach for rapid, accurate docking and scoring. 2. Enrichment factors in database screening
    • Halgren, T.A., R.B. Murphy, R.A. Friesner, H.S. Beard, L.L. Frye, W.T. Pollard, and J.L. Banks. 2004. Glide: a new approach for rapid, accurate docking and scoring. 2. Enrichment factors in database screening. J. Med. Chem. 47:1750-1759.
    • (2004) J. Med. Chem , vol.47 , pp. 1750-1759
    • Halgren, T.A.1    Murphy, R.B.2    Friesner, R.A.3    Beard, H.S.4    Frye, L.L.5    Pollard, W.T.6    Banks, J.L.7
  • 31
    • 0024453412 scopus 로고
    • Identification of actin nucleation activity and polymerization inhibitor in ameboid cells: Their regulation by chemotactic stimulation
    • Hall, A.L., V. Warren, S. Dharmawardhane, and J. Condeelis. 1989. Identification of actin nucleation activity and polymerization inhibitor in ameboid cells: their regulation by chemotactic stimulation. J. Cell Biol. 109:2207-2213.
    • (1989) J. Cell Biol , vol.109 , pp. 2207-2213
    • Hall, A.L.1    Warren, V.2    Dharmawardhane, S.3    Condeelis, J.4
  • 32
    • 0027439319 scopus 로고
    • Human actin depoly-merizing factor mediates a pH-sensitive destruction of actin filaments
    • Hawkins, M., B. Pope, S.K. Maciver, and A.G. Weeds. 1993. Human actin depoly-merizing factor mediates a pH-sensitive destruction of actin filaments. Biochemistry. 32:9985-9993.
    • (1993) Biochemistry , vol.32 , pp. 9985-9993
    • Hawkins, M.1    Pope, B.2    Maciver, S.K.3    Weeds, A.G.4
  • 33
    • 34247361650 scopus 로고    scopus 로고
    • Chemotaxis in the absence of PIP3 gradients
    • Hoeller, O., and R.R. Kay. 2007. Chemotaxis in the absence of PIP3 gradients. Curr. Biol. 17:813-817.
    • (2007) Curr. Biol , vol.17 , pp. 813-817
    • Hoeller, O.1    Kay, R.R.2
  • 34
    • 0034113924 scopus 로고    scopus 로고
    • Actin filaments are severed by both native and recombinant dictyostelium cofilin but to different extents
    • Ichetovkin, I., J. Han, K.M. Pang, D.A. Knecht, and J.S. Condeelis. 2000. Actin filaments are severed by both native and recombinant dictyostelium cofilin but to different extents. CellMotil. Cytoskeleton. 45:293-306.
    • (2000) CellMotil. Cytoskeleton , vol.45 , pp. 293-306
    • Ichetovkin, I.1    Han, J.2    Pang, K.M.3    Knecht, D.A.4    Condeelis, J.S.5
  • 35
    • 0037039167 scopus 로고    scopus 로고
    • Cofilin produces newly polymerized actin filaments that are preferred for dendritic nucleation by the Arp2/3 complex
    • Ichetovkin, I., W. Grant, and J. Condeelis. 2002. Cofilin produces newly polymerized actin filaments that are preferred for dendritic nucleation by the Arp2/3 complex. Curr. Biol. 12:79-84.
    • (2002) Curr. Biol , vol.12 , pp. 79-84
    • Ichetovkin, I.1    Grant, W.2    Condeelis, J.3
  • 36
    • 0032843103 scopus 로고    scopus 로고
    • Localized depolymerization of the major sperm protein cytoskeleton correlates with the forward movement of the cell body in the amoeboid movement of nematode sperm
    • Italiano, J.E. Jr., M. Stewart, and T.M. Roberts. 1999. Localized depolymerization of the major sperm protein cytoskeleton correlates with the forward movement of the cell body in the amoeboid movement of nematode sperm. J. Cell Biol. 146:1087-1096.
    • (1999) J. Cell Biol , vol.146 , pp. 1087-1096
    • Italiano Jr., J.E.1    Stewart, M.2    Roberts, T.M.3
  • 38
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids
    • Jorgensen, W.L., D.S. Maxwell, and J. Tirado-Rives. 1996. Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids. J. Am. Chem. Soc. 118:11225-11236.
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 39
    • 0035913529 scopus 로고    scopus 로고
    • Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides
    • Kaminski, G.A., R.A. Friesner, J. Tirado-Rives, and W.L. Jorgensen. 2001. Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides. J. Phys. Chem. B. 105:6474-6487.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 6474-6487
    • Kaminski, G.A.1    Friesner, R.A.2    Tirado-Rives, J.3    Jorgensen, W.L.4
  • 40
    • 0028353858 scopus 로고
    • Regulation of the Ascaris major sperm protein (MSP) cytoskeleton by intracellular pH
    • King, K.L., J. Essig, T.M. Roberts, and T.S. Moerland. 1994. Regulation of the Ascaris major sperm protein (MSP) cytoskeleton by intracellular pH. CellMotil. Cytoskeleton. 27:193-205.
    • (1994) CellMotil. Cytoskeleton , vol.27 , pp. 193-205
    • King, K.L.1    Essig, J.2    Roberts, T.M.3    Moerland, T.S.4
  • 41
    • 0034061827 scopus 로고    scopus 로고
    • Polarization of Na(+)/H(+) and Cl(-)/HCO (3)(-) exchangers in migrating renal epithelial cells
    • Klein, M., P. Seeger, B. Schuricht, S.L. Alper, and A. Schwab. 2000. Polarization of Na(+)/H(+) and Cl(-)/HCO (3)(-) exchangers in migrating renal epithelial cells. J. Gen. Physiol. 115:599-608.
    • (2000) J. Gen. Physiol , vol.115 , pp. 599-608
    • Klein, M.1    Seeger, P.2    Schuricht, B.3    Alper, S.L.4    Schwab, A.5
  • 42
    • 0028204451 scopus 로고
    • Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy
    • Kraulis, P.J., P.J. Domaille, S.L. Campbell-Burk, T. Van Aken, and E.D. Laue. 1994. Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy. Biochemistry. 33:3515-3531.
    • (1994) Biochemistry , vol.33 , pp. 3515-3531
    • Kraulis, P.J.1    Domaille, P.J.2    Campbell-Burk, S.L.3    Van Aken, T.4    Laue, E.D.5
  • 43
    • 0001675681 scopus 로고
    • Fluorescent actin filaments move on myosin fixed to a glass surface
    • Kron, S.J., and J.A. Spudich. 1986. Fluorescent actin filaments move on myosin fixed to a glass surface. Proc. Natl. Acad. Sci. USA. 83:6272-6276.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6272-6276
    • Kron, S.J.1    Spudich, J.A.2
  • 44
    • 0025782977 scopus 로고
    • Assays for actin sliding movement over myosin-coated surfaces
    • Kron, S.J., Y.Y. Toyoshima, T.Q. Uyeda, and J.A. Spudich. 1991. Assays for actin sliding movement over myosin-coated surfaces. Methods Enzymol. 196:399-416.
    • (1991) Methods Enzymol , vol.196 , pp. 399-416
    • Kron, S.J.1    Toyoshima, Y.Y.2    Uyeda, T.Q.3    Spudich, J.A.4
  • 45
    • 32144433330 scopus 로고    scopus 로고
    • Cdc42 and PI(4,5)P2-induced actin assembly in Xenopus egg extracts
    • Lebensohn, A.M., L. Ma, H.Y. Ho, and M.W. Kirschner. 2006. Cdc42 and PI(4,5)P2-induced actin assembly in Xenopus egg extracts. Methods Enzymol. 406:156-173.
    • (2006) Methods Enzymol , vol.406 , pp. 156-173
    • Lebensohn, A.M.1    Ma, L.2    Ho, H.Y.3    Kirschner, M.W.4
  • 47
    • 33749239639 scopus 로고    scopus 로고
    • Oscillatory increases in alkalinity anticipate growth and may regulate actin dynamics in pollen tubes of lily
    • Lovy-Wheeler, A., J.G. Kunkel, E.G. Allwood, P.J. Hussey, and P.K. Hepler. 2006. Oscillatory increases in alkalinity anticipate growth and may regulate actin dynamics in pollen tubes of lily. Plant Cell. 18:2182-2193.
    • (2006) Plant Cell , vol.18 , pp. 2182-2193
    • Lovy-Wheeler, A.1    Kunkel, J.G.2    Allwood, E.G.3    Hussey, P.J.4    Hepler, P.K.5
  • 48
    • 15144352303 scopus 로고    scopus 로고
    • The effect of two actin depolymerizing factors (ADF/cofilins) on actin filament turnover: PH sensitivity of F-actin binding by human ADF, but not of Acanthamoeba actophorin
    • Maciver, S.K., B.J. Pope, S. Whytock, and A.G. Weeds. 1998. The effect of two actin depolymerizing factors (ADF/cofilins) on actin filament turnover: pH sensitivity of F-actin binding by human ADF, but not of Acanthamoeba actophorin. Eur. J. Biochem. 256:388-397.
    • (1998) Eur. J. Biochem , vol.256 , pp. 388-397
    • Maciver, S.K.1    Pope, B.J.2    Whytock, S.3    Weeds, A.G.4
  • 50
    • 0027176804 scopus 로고
    • Adhesion to fibronectin stimulates inositol lipid synthesis and enhances PDGF-induced inositol lipid breakdown
    • McNamee, H.P., D.E. Ingber, and M.A. Schwartz. 1993. Adhesion to fibronectin stimulates inositol lipid synthesis and enhances PDGF-induced inositol lipid breakdown. J. Cell Biol. 121:673-678.
    • (1993) J. Cell Biol , vol.121 , pp. 673-678
    • McNamee, H.P.1    Ingber, D.E.2    Schwartz, M.A.3
  • 51
    • 9244223045 scopus 로고    scopus 로고
    • Constant pH molecular dynamics in generalized Born implicit solvent
    • Mongan, J., D.A. Case, and J.A. McCammon. 2004. Constant pH molecular dynamics in generalized Born implicit solvent. J. Comput. Chem. 25:2038-2048.
    • (2004) J. Comput. Chem , vol.25 , pp. 2038-2048
    • Mongan, J.1    Case, D.A.2    McCammon, J.A.3
  • 52
    • 0029678546 scopus 로고    scopus 로고
    • Phosphorylation of Ser-3 of cofilin regulates its essential function on actin
    • Moriyama, K., K. Iida, and I. Yahara. 1996. Phosphorylation of Ser-3 of cofilin regulates its essential function on actin. Genes Cells. 1:73-86.
    • (1996) Genes Cells , vol.1 , pp. 73-86
    • Moriyama, K.1    Iida, K.2    Yahara, I.3
  • 54
    • 33750948427 scopus 로고    scopus 로고
    • Spatial and temporal control of cofilin activity is required for directional sensing during chemotaxis
    • Mouneimne, G., V. DesMarais, M. Sidani, E. Scemes, W. Wang, X. Song, R. Eddy, and J. Condeelis. 2006. Spatial and temporal control of cofilin activity is required for directional sensing during chemotaxis. Curr. Biol. 16:2193-2205.
    • (2006) Curr. Biol , vol.16 , pp. 2193-2205
    • Mouneimne, G.1    DesMarais, V.2    Sidani, M.3    Scemes, E.4    Wang, W.5    Song, X.6    Eddy, R.7    Condeelis, J.8
  • 55
    • 0037169335 scopus 로고    scopus 로고
    • Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin
    • Niwa, R., K. Nagata-Ohashi, M. Takeichi, K. Mizuno, and T. Uemura. 2002. Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin. Cell. 108:233-246.
    • (2002) Cell , vol.108 , pp. 233-246
    • Niwa, R.1    Nagata-Ohashi, K.2    Takeichi, M.3    Mizuno, K.4    Uemura, T.5
  • 56
    • 0028329791 scopus 로고
    • Actin polymerization, calcium-transients, and phospholipid metabolism in human neutrophils after stimulation with interleukin-8 and N-formyl peptide
    • Norgauer, J., J. Krutmann, G.J. Dobos, A.E. Traynor-Kaplan, Z.G. Oades, and I.U. Schraufstatter. 1994. Actin polymerization, calcium-transients, and phospholipid metabolism in human neutrophils after stimulation with interleukin-8 and N-formyl peptide. J. Invest. Dermatol. 102:310-314.
    • (1994) J. Invest. Dermatol , vol.102 , pp. 310-314
    • Norgauer, J.1    Krutmann, J.2    Dobos, G.J.3    Traynor-Kaplan, A.E.4    Oades, Z.G.5    Schraufstatter, I.U.6
  • 57
    • 0035951069 scopus 로고    scopus 로고
    • Identification of yeast cofilin residues specific for actin monomer and PIP2 binding
    • Ojala, P.J., V. Paavilainen, and P. Lappalainen. 2001. Identification of yeast cofilin residues specific for actin monomer and PIP2 binding. Biochemistry. 40:15562-15569.
    • (2001) Biochemistry , vol.40 , pp. 15562-15569
    • Ojala, P.J.1    Paavilainen, V.2    Lappalainen, P.3
  • 58
    • 1842479952 scopus 로고    scopus 로고
    • Exploring protein native states and large-scale conformational changes with a modified generalized born model
    • Onufriev, A., D. Bashford, and D.A. Case. 2004. Exploring protein native states and large-scale conformational changes with a modified generalized born model. Proteins. 55:383-394.
    • (2004) Proteins , vol.55 , pp. 383-394
    • Onufriev, A.1    Bashford, D.2    Case, D.A.3
  • 59
    • 8444247968 scopus 로고    scopus 로고
    • Rac regulation of chemotaxis and morphogenesis in Dictyostelium
    • Park, K.C., R.F. Meili, S. Lee, F. Apone, and R.A. Firtel. 2004. Rac regulation of chemotaxis and morphogenesis in Dictyostelium. EMBO J. 23:4177-4189.
    • (2004) EMBO J , vol.23 , pp. 4177-4189
    • Park, K.C.1    Meili, R.F.2    Lee, S.3    Apone, F.4    Firtel, R.A.5
  • 60
    • 18544363096 scopus 로고    scopus 로고
    • A developmentally regulated Na-H exchanger in Dictyostelium discoideum is necessary for cell polarity during chemotaxis
    • Patel, H., and D.L. Barber. 2005. A developmentally regulated Na-H exchanger in Dictyostelium discoideum is necessary for cell polarity during chemotaxis. J. Cell Biol. 169:321-329.
    • (2005) J. Cell Biol , vol.169 , pp. 321-329
    • Patel, H.1    Barber, D.L.2
  • 61
    • 34247644614 scopus 로고    scopus 로고
    • Regulation of actin filament assembly by Arp2/3 complex and formins
    • Pollard, T.D. 2007. Regulation of actin filament assembly by Arp2/3 complex and formins. Annu. Rev. Biophys. Biomol. Struct. 36:451-477.
    • (2007) Annu. Rev. Biophys. Biomol. Struct , vol.36 , pp. 451-477
    • Pollard, T.D.1
  • 62
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard, T.D., and G.G. Borisy. 2003. Cellular motility driven by assembly and disassembly of actin filaments. Cell. 112:453-465.
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 63
    • 0034640134 scopus 로고    scopus 로고
    • Uncoupling actin filament fragmentation by cofilin from increased sub-unit turnover
    • Pope, B.J., S.M. Gonsior, S. Yeoh, A. McGough, and A.G. Weeds. 2000. Uncoupling actin filament fragmentation by cofilin from increased sub-unit turnover. J. Mol. Biol. 298:649-661.
    • (2000) J. Mol. Biol , vol.298 , pp. 649-661
    • Pope, B.J.1    Gonsior, S.M.2    Yeoh, S.3    McGough, A.4    Weeds, A.G.5
  • 64
    • 1042289739 scopus 로고    scopus 로고
    • Solution structure of human cofilin: Actin binding, pH sensitivity, and relationship to actin-depolymerizing factor
    • Pope, B.J., K.M. Zierler-Gould, R. Kuhne, A.G. Weeds, and L.J. Ball. 2004. Solution structure of human cofilin: actin binding, pH sensitivity, and relationship to actin-depolymerizing factor. J. Biol. Chem. 279:4840-4848.
    • (2004) J. Biol. Chem , vol.279 , pp. 4840-4848
    • Pope, B.J.1    Zierler-Gould, K.M.2    Kuhne, R.3    Weeds, A.G.4    Ball, L.J.5
  • 65
    • 0344012465 scopus 로고    scopus 로고
    • Uniform cAMP stimulation of Dictyostelium cells induces localized patches of signal transduction and pseudopodia
    • Postma, M., J. Roelofs, J. Goedhart, T.W. Gadella, A.J. Visser, and P.J. Van Haastert. 2003. Uniform cAMP stimulation of Dictyostelium cells induces localized patches of signal transduction and pseudopodia. Mol. Biol. Cell. 14:5019-5027.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 5019-5027
    • Postma, M.1    Roelofs, J.2    Goedhart, J.3    Gadella, T.W.4    Visser, A.J.5    Van Haastert, P.J.6
  • 66
    • 0036174658 scopus 로고    scopus 로고
    • The changing face of the Na+/H+ exchanger, NHE1: Structure, regulation, and cellular actions
    • Putney, L.K., S.P. Denker, and D.L. Barber. 2002. The changing face of the Na+/H+ exchanger, NHE1: structure, regulation, and cellular actions. Annu. Rev. Pharmacol. Toxicol. 42:527-552.
    • (2002) Annu. Rev. Pharmacol. Toxicol , vol.42 , pp. 527-552
    • Putney, L.K.1    Denker, S.P.2    Barber, D.L.3
  • 67
    • 0033746761 scopus 로고    scopus 로고
    • Na+/H+ exchanger-dependent intracellular alkalinization is an early event in malignant transformation and plays an essential role in the development of subsequent transformation-associated phenotypes
    • Reshkin, S.J., A. Bellizzi, S. Caldeira, V. Albarani, I. Malanchi, M. Poignee, M. Alunni-Fabbroni, V. Casavola, and M. Tommasino. 2000. Na+/H+ exchanger-dependent intracellular alkalinization is an early event in malignant transformation and plays an essential role in the development of subsequent transformation-associated phenotypes. FASEB J. 14:2185-2197.
    • (2000) FASEB J , vol.14 , pp. 2185-2197
    • Reshkin, S.J.1    Bellizzi, A.2    Caldeira, S.3    Albarani, V.4    Malanchi, I.5    Poignee, M.6    Alunni-Fabbroni, M.7    Casavola, V.8    Tommasino, M.9
  • 68
  • 69
    • 8444221934 scopus 로고    scopus 로고
    • Localized Ras signaling at the leading edge regulates PI3K, cell polarity, and directional cell movement
    • Sasaki, A.T., C. Chun, K. Takeda, and R.A. Firtel. 2004. Localized Ras signaling at the leading edge regulates PI3K, cell polarity, and directional cell movement. J. Cell Biol. 167:505-518.
    • (2004) J. Cell Biol , vol.167 , pp. 505-518
    • Sasaki, A.T.1    Chun, C.2    Takeda, K.3    Firtel, R.A.4
  • 70
    • 0025745212 scopus 로고
    • Insoluble fibronectin activates the Na/H antiporter by clustering and immobilizing integrin alpha 5 beta 1, independent of cell shape
    • Schwartz, M.A., C. Lechene, and D.E. Ingber. 1991. Insoluble fibronectin activates the Na/H antiporter by clustering and immobilizing integrin alpha 5 beta 1, independent of cell shape. Proc. Natl. Acad. Sci. USA. 88:7849-7853.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7849-7853
    • Schwartz, M.A.1    Lechene, C.2    Ingber, D.E.3
  • 71
    • 31544450787 scopus 로고    scopus 로고
    • Novel procedure for modeling ligand/receptor induced fit effects
    • Sherman, W., T. Day, M.P. Jacobson, R.A. Friesner, and R. Farid. 2006. Novel procedure for modeling ligand/receptor induced fit effects. J. Med. Chem. 49:534-553.
    • (2006) J. Med. Chem , vol.49 , pp. 534-553
    • Sherman, W.1    Day, T.2    Jacobson, M.P.3    Friesner, R.A.4    Farid, R.5
  • 72
    • 33746861083 scopus 로고    scopus 로고
    • Initiation of cofilin activity in response to EGF is uncoupled from cofilin phosphorylation and dephosphorylation in carcinoma cells
    • Song, X., X. Chen, H. Yamaguchi, G. Mouneimne, J.S. Condeelis, and R.J. Eddy. 2006. Initiation of cofilin activity in response to EGF is uncoupled from cofilin phosphorylation and dephosphorylation in carcinoma cells. J. Cell Sci. 119:2871-2881.
    • (2006) J. Cell Sci , vol.119 , pp. 2871-2881
    • Song, X.1    Chen, X.2    Yamaguchi, H.3    Mouneimne, G.4    Condeelis, J.S.5    Eddy, R.J.6
  • 75
    • 30844466190 scopus 로고    scopus 로고
    • Protein complexes regulating Arp2/3-mediated actin assembly
    • Stradal, T.E., and G. Scita. 2006. Protein complexes regulating Arp2/3-mediated actin assembly. Curr. Opin. Cell Biol. 18:4-10.
    • (2006) Curr. Opin. Cell Biol , vol.18 , pp. 4-10
    • Stradal, T.E.1    Scita, G.2
  • 76
    • 0017847503 scopus 로고
    • Polymerization of actin. IV. Role of Ca++ and H+ in the assembly of actin and in membrane fusion in the acrosomal reaction of echinoderm sperm
    • Tilney, L.G., D.P. Kiehart, C. Sardet, and M. Tilney. 1978. Polymerization of actin. IV. Role of Ca++ and H+ in the assembly of actin and in membrane fusion in the acrosomal reaction of echinoderm sperm. J. Cell Biol. 77:536-550.
    • (1978) J. Cell Biol , vol.77 , pp. 536-550
    • Tilney, L.G.1    Kiehart, D.P.2    Sardet, C.3    Tilney, M.4
  • 77
    • 0031878095 scopus 로고    scopus 로고
    • Na-H exchange acts downstream of RhoA to regulate integrin-induced cell adhesion and spreading
    • Tominaga, T., and D.L. Barber. 1998. Na-H exchange acts downstream of RhoA to regulate integrin-induced cell adhesion and spreading. Mol. Biol. Cell. 9:2287-2303.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2287-2303
    • Tominaga, T.1    Barber, D.L.2
  • 78
    • 0025876242 scopus 로고
    • Regulation of movement speed by intracellular pH during Dictyostelium discoideum chemotaxis
    • Van Duijn, B., and K. Inouye. 1991. Regulation of movement speed by intracellular pH during Dictyostelium discoideum chemotaxis. Proc. Natl. Acad. Sci. USA. 88:4951-4955.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4951-4955
    • Van Duijn, B.1    Inouye, K.2
  • 79
    • 34249873508 scopus 로고    scopus 로고
    • Essential role of PI3-kinase and phospholipase A2 in Dictyostelium discoideum chemotaxis
    • van Haastert, P.J., I. Keizer-Gunnink, and A. Kortholt. 2007. Essential role of PI3-kinase and phospholipase A2 in Dictyostelium discoideum chemotaxis. J. Cell Biol. 177:809-816.
    • (2007) J. Cell Biol , vol.177 , pp. 809-816
    • van Haastert, P.J.1    Keizer-Gunnink, I.2    Kortholt, A.3
  • 81
    • 0034633937 scopus 로고    scopus 로고
    • The competitive interaction of actin and PIP2 with actophorin is based on overlapping target sites: Design of a gain-of-function mutant
    • Van Troys, M., D. Dewitte, J.L. Verschelde, M. Goethals, J. Vandekerckhove, and C. Ampe. 2000. The competitive interaction of actin and PIP2 with actophorin is based on overlapping target sites: design of a gain-of-function mutant. Biochemistry. 39:12181-12189.
    • (2000) Biochemistry , vol.39 , pp. 12181-12189
    • Van Troys, M.1    Dewitte, D.2    Verschelde, J.L.3    Goethals, M.4    Vandekerckhove, J.5    Ampe, C.6
  • 82
    • 0001398008 scopus 로고    scopus 로고
    • How well does a RESP (restrained electrostatic potential) model do in calculating the conformational energies of organic and biological molecules?
    • Wang, J., P. Cieplak, and P.A. Kollman. 2000. How well does a RESP (restrained electrostatic potential) model do in calculating the conformational energies of organic and biological molecules? J. Comput. Chem. 21:1049-1074.
    • (2000) J. Comput. Chem , vol.21 , pp. 1049-1074
    • Wang, J.1    Cieplak, P.2    Kollman, P.A.3
  • 83
    • 0035903087 scopus 로고    scopus 로고
    • The Nck-interacting kinase (NIK) phosphorylates the Na+-H+ exchanger NHE1 and regulates NHE1 activation by platelet-derived growth factor
    • Yan, W., K. Nehrke, J. Choi, and D.L. Barber. 2001. The Nck-interacting kinase (NIK) phosphorylates the Na+-H+ exchanger NHE1 and regulates NHE1 activation by platelet-derived growth factor. J. Biol. Chem. 276:31349-31356.
    • (2001) J. Biol. Chem , vol.276 , pp. 31349-31356
    • Yan, W.1    Nehrke, K.2    Choi, J.3    Barber, D.L.4
  • 84
    • 0025277362 scopus 로고
    • Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides
    • Yonezawa, N., E. Nishida, K. Iida, I. Yahara, and H. Sakai. 1990. Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides. J. Biol. Chem. 265:8382-8386.
    • (1990) J. Biol. Chem , vol.265 , pp. 8382-8386
    • Yonezawa, N.1    Nishida, E.2    Iida, K.3    Yahara, I.4    Sakai, H.5
  • 85
    • 0034722329 scopus 로고    scopus 로고
    • Phosphorylation of ADF/cofilin abolishes EGF-induced actin nu-cleation at the leading edge and subsequent lamellipod extension
    • Zebda, N., O. Bernard, M. Bailly, S. Welti, D.S. Lawrence, and J.S. Condeelis. 2000. Phosphorylation of ADF/cofilin abolishes EGF-induced actin nu-cleation at the leading edge and subsequent lamellipod extension. J. Cell Biol. 151:1119-1128.
    • (2000) J. Cell Biol , vol.151 , pp. 1119-1128
    • Zebda, N.1    Bernard, O.2    Bailly, M.3    Welti, S.4    Lawrence, D.S.5    Condeelis, J.S.6
  • 86
    • 16644388440 scopus 로고    scopus 로고
    • Backbone and sidechain 1H, 13C and 15N resonance assignments of human cofilin
    • Zierler-Gould, K.M., B.J. Pope, A.G. Weeds, and L.J. Ball. 2004. Backbone and sidechain 1H, 13C and 15N resonance assignments of human cofilin. J. Biomol. NMR. 29:429-430.
    • (2004) J. Biomol. NMR , vol.29 , pp. 429-430
    • Zierler-Gould, K.M.1    Pope, B.J.2    Weeds, A.G.3    Ball, L.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.