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Volumn 67, Issue 2, 2010, Pages 120-133

A central role for the WH2 domain of Srv2/CAP in recharging actin monomers to drive actin turnover in vitro and in vivo

Author keywords

Actin; ADF cofilin; Profiling; Srv2 CAP; Turnover; WH2 domain; Yeast

Indexed keywords

ACTIN; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CYCLASE ASSOCIATED PROTEIN; FUNGAL PROTEIN; G ACTIN; MONOMER; MUTANT PROTEIN; SRV2 PROTEIN; UNCLASSIFIED DRUG; WH2 PROTEIN; CYTOSKELETON PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; SIGNAL TRANSDUCING ADAPTOR PROTEIN; SRV2 PROTEIN, S CEREVISIAE;

EID: 77951917756     PISSN: 19493584     EISSN: 19493592     Source Type: Journal    
DOI: 10.1002/cm.20429     Document Type: Article
Times cited : (57)

References (44)
  • 1
    • 0347664159 scopus 로고    scopus 로고
    • Coordinated regulation of actin filament turnover by a high-molecular weight Srv2/CAP complex, cofilin, profilin, and Aip1
    • Balcer HI, Goodman AL, Rodal AA, Smith E, Kugler J, Heuser JE, Goode BL. 2003. Coordinated regulation of actin filament turnover by a high-molecular weight Srv2/CAP complex, cofilin, profilin, and Aip1. Curr Biol 13:2159-2169.
    • (2003) Curr Biol , vol.13 , pp. 2159-2169
    • Balcer, H.I.1    Goodman, A.L.2    Rodal, A.A.3    Smith, E.4    Kugler, J.5    Heuser, J.E.6    Goode, B.L.7
  • 2
    • 2342514815 scopus 로고    scopus 로고
    • Cyclase-associated protein 1 (CAP1) promotes cofilin-induced actin dynamics in mammalian nonmuscle cells
    • Bertling E, Hotulainen P, Mattila P, Matilainen T, Salminen M, Lappalainen P. 2004. Cyclase-associated protein 1 (CAP1) promotes cofilin-induced actin dynamics in mammalian nonmuscle cells. Mol Biol Cell 15:2324-2334.
    • (2004) Mol Biol Cell , vol.15 , pp. 2324-2334
    • Bertling, E.1    Hotulainen, P.2    Mattila, P.3    Matilainen, T.4    Salminen, M.5    Lappalainen, P.6
  • 4
    • 0032566659 scopus 로고    scopus 로고
    • Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin
    • Blanchoin L, Pollard TD. 1998. Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin. J Biol Chem 273: 25106-25111.
    • (1998) J Biol Chem , vol.273 , pp. 25106-25111
    • Blanchoin, L.1    Pollard, T.D.2
  • 5
    • 36249032075 scopus 로고    scopus 로고
    • Analysis of the function of Spire in actin assembly and its synergy with formin and profilin
    • Bosch M, Le K, Bugyi B, Correia J, Renault L, Carlier MF. 2007. Analysis of the function of Spire in actin assembly and its synergy with formin and profilin. Mol Cell 28:555-568.
    • (2007) Mol Cell , vol.28 , pp. 555-568
    • Bosch, M.1    Le, K.2    Bugyi, B.3    Correia, J.4    Renault, L.5    Carlier, M.F.6
  • 6
    • 0021111905 scopus 로고
    • On the mechanism of actin monomer-polymer subunit exchange at steady-state
    • Brenner S, Korn E. 1983. On the mechanism of actin monomer-polymer subunit exchange at steady-state. J Biol Chem 258:5013-5020.
    • (1983) J Biol Chem , vol.258 , pp. 5013-5020
    • Brenner, S.1    Korn, E.2
  • 7
    • 0024527982 scopus 로고
    • Role of nucleotide hydrolysis in the dynamics of actin filaments and microtubules
    • Carlier MF. 1989. Role of nucleotide hydrolysis in the dynamics of actin filaments and microtubules. Int Rev Cytol 115:139-170.
    • (1989) Int Rev Cytol , vol.115 , pp. 139-170
    • Carlier, M.F.1
  • 9
    • 34547803604 scopus 로고    scopus 로고
    • Identification of Arabidopsis cyclase-associated protein 1 as the first nucleotide exchange factor for plant actin
    • Chaudhry F, Guérin C, von Witsch M, Blanchoin L, Staiger C. 2007. Identification of Arabidopsis cyclase-associated protein 1 as the first nucleotide exchange factor for plant actin. Mol Biol Cell 18:3002-3014.
    • (2007) Mol Biol Cell , vol.18 , pp. 3002-3014
    • Chaudhry, F.1    Guérin, C.2    Von Witsch, M.3    Blanchoin, L.4    Staiger, C.5
  • 10
    • 28044470753 scopus 로고    scopus 로고
    • Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly
    • Chereau D, Kerff F, Graceffa P, Grabarek Z, Langsetma K, Dominguez R. 2005. Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly. Proc Nat Acad Sci USA 102:16644-16649.
    • (2005) Proc Nat Acad Sci USA , vol.102 , pp. 16644-16649
    • Chereau, D.1    Kerff, F.2    Graceffa, P.3    Grabarek, Z.4    Langsetma, K.5    Dominguez, R.6
  • 13
    • 35348969696 scopus 로고    scopus 로고
    • The β-thymosin/WH2 fold
    • Dominguez R. 2007. The β-thymosin/WH2 fold. Annal N Y Acad Sci 1112:86-94.
    • (2007) Annal N y Acad Sci , vol.1112 , pp. 86-94
    • Dominguez, R.1
  • 15
    • 0026543510 scopus 로고
    • ASP-56, a new actin sequestering protein from the pig platelets with homology to CAP, an adenylate cyclase-associated protein from yeast
    • Gieselmann R, Mann K. 1992. ASP-56, a new actin sequestering protein from the pig platelets with homology to CAP, an adenylate cyclase-associated protein from yeast. FEBS Lett 298:149-153.
    • (1992) FEBS Lett , vol.298 , pp. 149-153
    • Gieselmann, R.1    Mann, K.2
  • 16
    • 0027104517 scopus 로고
    • The control of actin nucleotide exchange by thymosin ß4 and profilin. A potential regulatory mechanism for actin polymerization in cells
    • Goldschmidt-Clermont P, Furman M, Wachsstock D, Safer D, Nachmias V, Pollard T. 1992. The control of actin nucleotide exchange by thymosin ß4 and profilin. A potential regulatory mechanism for actin polymerization in cells. Mol Biol Cell 3:1015-1024.
    • (1992) Mol Biol Cell , vol.3 , pp. 1015-1024
    • Goldschmidt-Clermont, P.1    Furman, M.2    Wachsstock, D.3    Safer, D.4    Nachmias, V.5    Pollard, T.6
  • 18
    • 0027439319 scopus 로고
    • Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments
    • Hawkins M, Pope B, Maciver SK, Weeds AG. 1993. Human actin depolymerizing 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
  • 19
    • 0027494863 scopus 로고
    • Analysis of the interaction of actin depolymerizing factor with G- and F-actin
    • Hayden SM, Miller PS, Brauweiler A, Bamburg JR. 1993. Analysis of the interaction of actin depolymerizing factor with G- and F-actin. Biochemistry 32:9994-10004.
    • (1993) Biochemistry , vol.32 , pp. 9994-10004
    • Hayden, S.M.1    Miller, P.S.2    Brauweiler, A.3    Bamburg, J.R.4
  • 21
    • 0036205611 scopus 로고    scopus 로고
    • Cyclase-associated proteins: CAPacity for linking signal transduction and actin polymerization
    • Hubberstey AV, Mottillo EP. 2002. Cyclase-associated proteins: CAPacity for linking signal transduction and actin polymerization. FASEB J 16:487-499.
    • (2002) FASEB J , vol.16 , pp. 487-499
    • Hubberstey, A.V.1    Mottillo, E.P.2
  • 22
    • 70249116807 scopus 로고    scopus 로고
    • Actin dynamics at the leading edge: From simple machinery to complex networks
    • Insall R, Machesky L. 2009. Actin dynamics at the leading edge: from simple machinery to complex networks. Dev Cell 17:310-322.
    • (2009) Dev Cell , vol.17 , pp. 310-322
    • Insall, R.1    Machesky, L.2
  • 23
    • 0023637721 scopus 로고
    • Actin polymerization and ATP hydrolysis
    • Korn ED, Carlier, M-F, Pantaloni D. 1987. Actin polymerization and ATP hydrolysis. Science 238:638-644.
    • (1987) Science , vol.238 , pp. 638-644
    • Korn, E.D.1    Carlier, M.-F.2    Pantaloni, D.3
  • 24
    • 0035214288 scopus 로고    scopus 로고
    • Chlamydomonas reinhardtii produces a profilin with unusual biochemical properties
    • Kovar DR, Yang P, Sale WS, Drobak BK, Staiger CJ. 2001. Chlamydomonas reinhardtii produces a profilin with unusual biochemical properties. J Cell Sci 114:4293-4305.
    • (2001) J Cell Sci , vol.114 , pp. 4293-4305
    • Kovar, D.R.1    Yang, P.2    Sale, W.S.3    Drobak, B.K.4    Staiger, C.J.5
  • 26
    • 0030880186 scopus 로고    scopus 로고
    • Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis
    • Lappalainen P, Fedorov EV, Fedorov AA, Almo SC, Drubin DG. 1997. Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis. EMBO J 16:5520-5530.
    • (1997) EMBO J , vol.16 , pp. 5520-5530
    • Lappalainen, P.1    Fedorov, E.V.2    Fedorov, A.A.3    Almo, S.C.4    Drubin, D.G.5
  • 27
    • 0031027546 scopus 로고    scopus 로고
    • Evidence for physical and functional interactions among two Saccharomyces cerevisiae SH3 domain proteins, an adenylyl cyclase-associated protein and the actin cytoskeleton
    • Lila T, Drubin D. 1997. Evidence for physical and functional interactions among two Saccharomyces cerevisiae SH3 domain proteins, an adenylyl cyclase-associated protein and the actin cytoskeleton. Mol Biol Cell 8: 367-385.
    • (1997) Mol Biol Cell , vol.8 , pp. 367-385
    • Lila, T.1    Drubin, D.2
  • 28
    • 0028357931 scopus 로고
    • Actophorin preferentially binds monomeric ADP-actin over ATP-bound actin: Consequences for cell locomotion
    • Maciver SK, Weeds AG. 1994. Actophorin preferentially binds monomeric ADP-actin over ATP-bound actin: consequences for cell locomotion. FEBS Lett 347:251-256.
    • (1994) FEBS Lett , vol.347 , pp. 251-256
    • Maciver, S.K.1    Weeds, A.G.2
  • 29
    • 6344225310 scopus 로고    scopus 로고
    • A high affinity interaction with ADP-actin monomers underlies the mechanism and in vivo function of Srv2/cyclaseassociated protein (CAP)
    • Mattila PK, Quintero-Monzon O, Kugler J, Moseley JB, Almo SC, Lappalainen P, Goode BL. 2004. A high affinity interaction with ADP-actin monomers underlies the mechanism and in vivo function of Srv2/cyclaseassociated protein (CAP). Mol Biol Cell 15:5158-5171.
    • (2004) Mol Biol Cell , vol.15 , pp. 5158-5171
    • Mattila, P.K.1    Quintero-Monzon, O.2    Kugler, J.3    Moseley, J.B.4    Almo, S.C.5    Lappalainen, P.6    Goode, B.L.7
  • 30
    • 0019194944 scopus 로고
    • Acanthamoeba profilin interacts with G-actin to increase the rate of exchange of actin-bound adenosine 5'-triphosphate
    • Mockrin SC, Korn ED. 1980. Acanthamoeba profilin interacts with G-actin to increase the rate of exchange of actin-bound adenosine 5'-triphosphate. Biochemistry 19:5359-5362.
    • (1980) Biochemistry , vol.19 , pp. 5359-5362
    • Mockrin, S.C.1    Korn, E.D.2
  • 31
    • 0037093266 scopus 로고    scopus 로고
    • Human CAP1 is a key factor in the recycling of cofilin and actin for rapid actin turnover
    • Moriyama K, Yahara I. 2002. Human CAP1 is a key factor in the recycling of cofilin and actin for rapid actin turnover. J Cell Sci 115:1591-1601.
    • (2002) J Cell Sci , vol.115 , pp. 1591-1601
    • Moriyama, K.1    Yahara, I.2
  • 32
    • 0021964668 scopus 로고
    • Opposite effects of cofilin and profilin from porcine brain on rate of exchange of actin-bound adenosine 5'-triphosphate
    • Nishida E. 1985. Opposite effects of cofilin and profilin from porcine brain on rate of exchange of actin-bound adenosine 5'-triphosphate. Biochemistry 24:1160-1164.
    • (1985) Biochemistry , vol.24 , pp. 1160-1164
    • Nishida, E.1
  • 33
    • 33847295719 scopus 로고    scopus 로고
    • Mechanism of depolymerization and severing of actin filaments and its significance in cytoskeletal dynamics
    • Ono S. 2007. Mechanism of depolymerization and severing of actin filaments and its significance in cytoskeletal dynamics. Int Rev Cytol 258:1-82.
    • (2007) Int Rev Cytol , vol.258 , pp. 1-82
    • Ono, S.1
  • 34
    • 0037138384 scopus 로고    scopus 로고
    • WH2 domain: A small, versatile adapter for actin monomers
    • Paunola E, Mattila P, Lappalainen P. 2001. WH2 domain: a small, versatile adapter for actin monomers. FEBS Lett 513:92-97.
    • (2001) FEBS Lett , vol.513 , pp. 92-97
    • Paunola, E.1    Mattila, P.2    Lappalainen, P.3
  • 35
    • 0022881322 scopus 로고
    • Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments
    • Pollard TD. 1986. Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments. J Cell Biol 103:2747-2754.
    • (1986) J Cell Biol , vol.103 , pp. 2747-2754
    • Pollard, T.D.1
  • 36
    • 67449107876 scopus 로고    scopus 로고
    • Reconstitution and dissection of the 600 kdA SRV2/CAP complex: Roles for oligomerization and cofilin-actin binding in driving actin turnover
    • Quintero-Monzon O, Jonasson EM, Bertling E, Talarico L, Chaudhry F, Sihvo M, Lappalainen P, Goode BL. 2009. Reconstitution and dissection of the 600 kdA SRV2/CAP complex: roles for oligomerization and cofilin-actin binding in driving actin turnover. J Biol Chem 284: 10923-10934.
    • (2009) J Biol Chem , vol.284 , pp. 10923-10934
    • Quintero-Monzon, O.1    Jonasson, E.M.2    Bertling, E.3    Talarico, L.4    Chaudhry, F.5    Sihvo, M.6    Lappalainen, P.7    Goode, B.L.8
  • 37
  • 38
    • 0033944260 scopus 로고    scopus 로고
    • Structural requirements for thymosin beta4 in its contact with actin. An NMR-analysis of thymosin beta4 mutants in solution and correlation with their biological activity
    • Simenel C, Van Troys M, Vanderkerckhove J, Ampe C, Delepierre M. 2000. Structural requirements for thymosin beta4 in its contact with actin. An NMR-analysis of thymosin beta4 mutants in solution and correlation with their biological activity. Eur J Biochem 267:3530-3538.
    • (2000) Eur J Biochem , vol.267 , pp. 3530-3538
    • Simenel, C.1    Van Troys, M.2    Vanderkerckhove, J.3    Ampe, C.4    Delepierre, M.5
  • 39
    • 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
    • Spudich JA, Watt S. 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 246:4866-4871.
    • (1971) J Biol Chem , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 40
    • 0032483044 scopus 로고    scopus 로고
    • Interactions of Acanthamoeba profilin with actin and nucleotides bound to actin
    • Vinson VK, Delacruz EM, Higgs HN, Pollard TD. 1998. Interactions of Acanthamoeba profilin with actin and nucleotides bound to actin. Biochemistry 37:10871-10880.
    • (1998) Biochemistry , vol.37 , pp. 10871-10880
    • Vinson, V.K.1    Delacruz, E.M.2    Higgs, H.N.3    Pollard, T.D.4
  • 41
    • 0025989194 scopus 로고
    • Evidence for a functional link between profilin and CAP in the yeast S. cerevisiae
    • Vojtek A, Haarer B, Field J, Gerst J, Pollard TD, Brown S, Wigler M. 1991. Evidence for a functional link between profilin and CAP in the yeast S. cerevisiae. Cell 66:497-505.
    • (1991) Cell , vol.66 , pp. 497-505
    • Vojtek, A.1    Haarer, B.2    Field, J.3    Gerst, J.4    Pollard, T.D.5    Brown, S.6    Wigler, M.7
  • 42
    • 0026693870 scopus 로고
    • The 70-kilodalton adenyl cyclase-associated protein is not essential for interaction of Saccharomyces cerevisiae adenyl cyclase with RAS proteins
    • Wang J, Suzuki N, Kataoka T. 1992. The 70-kilodalton adenyl cyclase-associated protein is not essential for interaction of Saccharomyces cerevisiae adenyl cyclase with RAS proteins. Mol Cell Biol 12:4937-4945.
    • (1992) Mol Cell Biol , vol.12 , pp. 4937-4945
    • Wang, J.1    Suzuki, N.2    Kataoka, T.3
  • 43
    • 0034698783 scopus 로고    scopus 로고
    • In vivo importance of actin nucleotide exchange catalyzed by profilin
    • Wolven A, Belmont L, Mahoney N, Almo S, Drubin D. 2000. In vivo importance of actin nucleotide exchange catalyzed by profilin. J Cell Biol 150: 895-903.
    • (2000) J Cell Biol , vol.150 , pp. 895-903
    • Wolven, A.1    Belmont, L.2    Mahoney, N.3    Almo, S.4    Drubin, D.5
  • 44
    • 11344253088 scopus 로고    scopus 로고
    • Structural evidence for variable oligomerization of the N-terminal domain of cyclase-associated protein (CAP)
    • Yusof A, Hu, N-J, Wlodawer A, Hofmann A. 2005. Structural evidence for variable oligomerization of the N-terminal domain of cyclase-associated protein (CAP). Proteins 58:255-262.
    • (2005) Proteins , vol.58 , pp. 255-262
    • Yusof, A.1    Hu, N.-J.2    Wlodawer, A.3    Hofmann, A.4


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