메뉴 건너뛰기




Volumn 9, Issue 4, 1998, Pages 841-852

Arp2/3 complex from Acanthamoeba binds profilin and cross-links actin filaments

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CELL PROTEIN; PROFILIN;

EID: 0031922638     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.9.4.841     Document Type: Article
Times cited : (76)

References (46)
  • 2
    • 0029800868 scopus 로고    scopus 로고
    • Fission yeast Sop2p: A novel and evolutionary conserved protein that interacts with Arp3p and modulates profilin function
    • Balasubramanian, M.K., Feoktistova, A., McCollum, D., and Gould, K.L. (1996). Fission yeast Sop2p: a novel and evolutionary conserved protein that interacts with Arp3p and modulates profilin function. EMBO J. 15, 6426-6437.
    • (1996) EMBO J. , vol.15 , pp. 6426-6437
    • Balasubramanian, M.K.1    Feoktistova, A.2    McCollum, D.3    Gould, K.L.4
  • 3
    • 0028046084 scopus 로고
    • Actobindin binds with high affinity to a covalently cross-linked actin dimer
    • Bubb, M.R., Lewis, M.S., and Korn, E.D. (1994). Actobindin binds with high affinity to a covalently cross-linked actin dimer. J. Biol. Chem. 269, 25587-25591.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25587-25591
    • Bubb, M.R.1    Lewis, M.S.2    Korn, E.D.3
  • 4
    • 0021984210 scopus 로고
    • Effects of capping protein on the kinetics of actin polymerization
    • Cooper, J.A., and Pollard, T.D. (1985). Effects 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
  • 7
    • 0017109215 scopus 로고
    • Fluorescent antibody localization of myosin in the cytoplasm, cleavage furrow, and mitotic spindle of human cells
    • Fujiwara, K., and Pollard, T.D. (1976). Fluorescent antibody localization of myosin in the cytoplasm, cleavage furrow, and mitotic spindle of human cells. J. Cell Biol. 71, 848-875.
    • (1976) J. Cell Biol. , vol.71 , pp. 848-875
    • Fujiwara, K.1    Pollard, T.D.2
  • 8
    • 0017303511 scopus 로고
    • Characterization of a cytoplasmic actin isolated from Acanthamoeba castellanii by a new method
    • Gordon, D.J., Eisenberg, E., and Korn, E.D. (1976). Characterization of a cytoplasmic actin isolated from Acanthamoeba castellanii by a new method. J. Biol. Chem. 251, 4778-4786.
    • (1976) J. Biol. Chem. , vol.251 , pp. 4778-4786
    • Gordon, D.J.1    Eisenberg, E.2    Korn, E.D.3
  • 9
    • 0030479303 scopus 로고    scopus 로고
    • Centractin (Apr1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles
    • Holleran, E.A., Tokito, M.K., Karki, S., Holzbaur, E.L.F. (1996) Centractin (Apr1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles. J. Cell Biol. 135, 1815-1830.
    • (1996) J. Cell Biol. , vol.135 , pp. 1815-1830
    • Holleran, E.A.1    Tokito, M.K.2    Karki, S.3    Holzbaur, E.L.F.4
  • 10
    • 0024470502 scopus 로고
    • Characterization of renatured profilin purified by urea elution from poly-L-proline agarose columns
    • Kaiser, D.A., Goldschmidt-Clermont, P.J., Levine, B.A., and Pollard, T.D. (1989). Characterization of renatured profilin purified by urea elution from poly-L-proline agarose columns. Cell Motil. 24, 251-262.
    • (1989) Cell Motil. , vol.24 , pp. 251-262
    • Kaiser, D.A.1    Goldschmidt-Clermont, P.J.2    Levine, B.A.3    Pollard, T.D.4
  • 11
    • 0029966344 scopus 로고    scopus 로고
    • Characterization of actin and poly-L-proline binding sites of Acanthamoeba profilin with monoclonal antibodies and by mutagenesis
    • Kaiser, D.A., and Pollard, T.D. (1996). Characterization of actin and poly-L-proline binding sites of Acanthamoeba profilin with monoclonal antibodies and by mutagenesis. J. Mol. Biol. 255, 89-107.
    • (1996) J. Mol. Biol. , vol.255 , pp. 89-107
    • Kaiser, D.A.1    Pollard, T.D.2
  • 12
    • 0022621479 scopus 로고
    • Purification and characterization of two isoforms of Acanthamoeba profilin
    • Kaiser, D.A., Sato, M., Ebert, R., and Pollard, T.D. (1986). Purification and characterization of two isoforms of Acanthamoeba profilin. J. Cell Biol. 102, 221-226.
    • (1986) J. Cell Biol. , vol.102 , pp. 221-226
    • Kaiser, D.A.1    Sato, M.2    Ebert, R.3    Pollard, T.D.4
  • 13
    • 0028786352 scopus 로고
    • Sequences, structural models, and cellular localization of the actin-related proteins Arp2 and Arp3 from Acanthamoeba
    • Kelleher, J.F., Atkinson, S.J., and Pollard., T.D. (1995). Sequences, structural models, and cellular localization of the actin-related proteins Arp2 and Arp3 from Acanthamoeba. J. Cell Biol. 131, 385-397.
    • (1995) J. Cell Biol. , vol.131 , pp. 385-397
    • Kelleher, J.F.1    Atkinson, S.J.2    Pollard, T.D.3
  • 14
    • 0021175074 scopus 로고
    • Monoclonal antibodies demonstrate limited structural homology between myosin isozymes from Acanthamoeba
    • Kiehart, D.P., Kaiser, D.A., and Pollard, T.D. (1984). Monoclonal antibodies demonstrate limited structural homology between myosin isozymes from Acanthamoeba. J. Cell Biol. 99, 1002-1014.
    • (1984) J. Cell Biol. , vol.99 , pp. 1002-1014
    • Kiehart, D.P.1    Kaiser, D.A.2    Pollard, T.D.3
  • 15
    • 0025884502 scopus 로고
    • Purification of myosin-I and myosin-I heavy chain kinase
    • Lynch, T.J., Brzeska, H., Baines, I.C., and Korn, E.D. (1991). Purification of myosin-I and myosin-I heavy chain kinase. Methods Enzymol. 196, 12-23.
    • (1991) Methods Enzymol. , vol.196 , pp. 12-23
    • Lynch, T.J.1    Brzeska, H.2    Baines, I.C.3    Korn, E.D.4
  • 16
    • 0031104928 scopus 로고    scopus 로고
    • Cell motility: Complex dynamics at the leading edge
    • Machesky, L.M. (1997). Cell motility: complex dynamics at the leading edge. Curr. Biol. 7, R164-R167.
    • (1997) Curr. Biol. , vol.7
    • Machesky, L.M.1
  • 17
    • 0028136434 scopus 로고
    • Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin agarose
    • Machesky, L.M., Atkinson, S.J., Ampe, C., Vandekerckhove, J., and Pollard, T.D. (1994). Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin agarose. J. Cell Biol. 127, 107-115.
    • (1994) J. Cell Biol. , vol.127 , pp. 107-115
    • Machesky, L.M.1    Atkinson, S.J.2    Ampe, C.3    Vandekerckhove, J.4    Pollard, T.D.5
  • 18
    • 0026352811 scopus 로고
    • The actin filament severing protein actophorin catalyzes the formation of rigid bundles of actin filaments crosslinked with alpha-actinin
    • Maciver, S.K., Wachsstock, D., Schwarz, W.H., and Pollard, T.D. (1991). The actin filament severing protein actophorin catalyzes the formation of rigid bundles of actin filaments crosslinked with alpha-actinin. J. Cell Biol. 115, 1621-1628.
    • (1991) J. Cell Biol. , vol.115 , pp. 1621-1628
    • Maciver, S.K.1    Wachsstock, D.2    Schwarz, W.H.3    Pollard, T.D.4
  • 19
    • 0019135186 scopus 로고
    • Identification of a factor in conventional muscle actin preparation which inhibits actin filament self-association
    • MacLean-Fletcher, S., and Pollard, T.D. (1980). Identification of a factor in conventional muscle actin preparation which inhibits actin filament self-association. Biochem. Biophys. Res. Commun. 96, 18-27.
    • (1980) Biochem. Biophys. Res. Commun. , vol.96 , pp. 18-27
    • MacLean-Fletcher, S.1    Pollard, T.D.2
  • 20
    • 0029849062 scopus 로고    scopus 로고
    • The Schizosaccharomyces pombe actin-related protein, Arp3, is a component of the cortical actin cytoskeleton and interacts with profilin
    • McCollum, D., Feoktistova, A., Morphew, M., Balasubramanian, M., Gould, K.L. (1996). The Schizosaccharomyces pombe actin-related protein, Arp3, is a component of the cortical actin cytoskeleton and interacts with profilin. EMBO J. 15, 6438-6446.
    • (1996) EMBO J. , vol.15 , pp. 6438-6446
    • McCollum, D.1    Feoktistova, A.2    Morphew, M.3    Balasubramanian, M.4    Gould, K.L.5
  • 21
    • 0021099241 scopus 로고
    • Kinetics of polymerization and ATP hydrolysis by covalently cross-linked actin dimers
    • Mockrin, S.C., and Korn, E.D. (1983). Kinetics of polymerization and ATP hydrolysis by covalently cross-linked actin dimers. J. Biol. Chem. 258, 3215-3221.
    • (1983) J. Biol. Chem. , vol.258 , pp. 3215-3221
    • Mockrin, S.C.1    Korn, E.D.2
  • 22
    • 0030813921 scopus 로고    scopus 로고
    • The yeast actin-related protein Arp2p is required for the internalization step of endocytosis
    • Moreau, V., Galan, J.M., Devilliers, G., Haguenauer-Tsapis, R., and Winsor, B. (1997). The yeast actin-related protein Arp2p is required for the internalization step of endocytosis. Mol. Biol. Cell 8, 1361-1375.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1361-1375
    • Moreau, V.1    Galan, J.M.2    Devilliers, G.3    Haguenauer-Tsapis, R.4    Winsor, B.5
  • 23
    • 0029959468 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae actin-related protein Arp2 is involved in the actin cytoskeleton
    • Moreau, V., Madania, A., Martin, R.P., and Winsor, B. (1996). The Saccharomyces cerevisiae actin-related protein Arp2 is involved in the actin cytoskeleton. J. Cell Biol. 134, 117-132.
    • (1996) J. Cell Biol. , vol.134 , pp. 117-132
    • Moreau, V.1    Madania, A.2    Martin, R.P.3    Winsor, B.4
  • 25
    • 0031051993 scopus 로고    scopus 로고
    • Structure, subunit topology, and actin-binding activity of the Arp2/3 complex from Acanthamoeba
    • Mullins, R.D., Stafford, W.F., and Pollard, T.D. (1997). Structure, subunit topology, and actin-binding activity of the Arp2/3 complex from Acanthamoeba. J. Cell Biol. 136, 331-343.
    • (1997) J. Cell Biol. , vol.136 , pp. 331-343
    • Mullins, R.D.1    Stafford, W.F.2    Pollard, T.D.3
  • 26
    • 0032568650 scopus 로고    scopus 로고
    • The interaction of Arp2/3 complex with actin: Nucleation, high-affinity pointed end capping, and formation of branching networks of filaments
    • in press
    • Mullins, R.D., Heuser, J.A., Pollard, T.D. (1998). The interaction of Arp2/3 complex with actin: nucleation, high-affinity pointed end capping, and formation of branching networks of filaments. Proc. Natl. Acad. Sci. USA (in press).
    • (1998) Proc. Natl. Acad. Sci. USA
    • Mullins, R.D.1    Heuser, J.A.2    Pollard, T.D.3
  • 28
    • 0021705094 scopus 로고
    • Purification of a high molecular-weight actin filament gelation protein from Acanthamoeba that shares antigenic determinants with vertebate spectrins
    • Pollard, T.D. (1984). Purification of a high molecular-weight actin filament gelation protein from Acanthamoeba that shares antigenic determinants with vertebate spectrins. J. Cell Biol. 99, 1970-1980.
    • (1984) J. Cell Biol. , vol.99 , pp. 1970-1980
    • Pollard, T.D.1
  • 30
    • 0021297595 scopus 로고
    • Rheological properties of living cytoplasm: A preliminary investigation of squid axoplasm
    • Sato, M., Wong, T.Z., Brown, D., and Allen, R.D. (1984). Rheological properties of living cytoplasm: a preliminary investigation of squid axoplasm. Cell Motil. 4, 7-23.
    • (1984) Cell Motil. , vol.4 , pp. 7-23
    • Sato, M.1    Wong, T.Z.2    Brown, D.3    Allen, R.D.4
  • 31
    • 2642690895 scopus 로고
    • Deductions from hydrodynamic and thermodynamic measurements
    • Schachman, H.K. (1960). Deductions from hydrodynamic and thermodynamic measurements. Brookhaven Symp. Biol. 13, 49-70.
    • (1960) Brookhaven Symp. Biol. , vol.13 , pp. 49-70
    • Schachman, H.K.1
  • 32
    • 0007970907 scopus 로고
    • Ultracentrifuge studies with absorption optics. II. Incorporation of a monochrometer and its application to the study of proteins and interacting systems
    • Schachman, H.K., Gropper, L., Hanlon, S., and Putney, F. (1962). Ultracentrifuge studies with absorption optics. II. Incorporation of a monochrometer and its application to the study of proteins and interacting systems. Arch. Biochem. Biophys. 99, 175-190.
    • (1962) Arch. Biochem. Biophys. , vol.99 , pp. 175-190
    • Schachman, H.K.1    Gropper, L.2    Hanlon, S.3    Putney, F.4
  • 33
    • 0030908903 scopus 로고    scopus 로고
    • The isolated comet tail pseudopodium of Listeria monocytogenes: A tail of two actin filament populations, long and axial and short and random
    • Sechi, A.S., Wehland, J., Small, J.V. (1997). The isolated comet tail pseudopodium of Listeria monocytogenes: a tail of two actin filament populations, long and axial and short and random. J. Cell Biol. 137, 155-167.
    • (1997) J. Cell Biol. , vol.137 , pp. 155-167
    • Sechi, A.S.1    Wehland, J.2    Small, J.V.3
  • 34
    • 0029000811 scopus 로고
    • Actin filament organization in the fish keratocyte lamellipodium
    • Small, J.V., Herzog, M., and Anderson, K. (1995). Actin filament organization in the fish keratocyte lamellipodium. J. Cell Biol. 129, 1275-1286.
    • (1995) J. Cell Biol. , vol.129 , pp. 1275-1286
    • Small, J.V.1    Herzog, M.2    Anderson, K.3
  • 35
    • 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, I.A., and 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, I.A.1    Watt, S.2
  • 36
    • 0030740007 scopus 로고    scopus 로고
    • Identification of actin-binding proteins from sea urchin eggs by F-actin affinity column chromatography
    • Terasaki, A.G., Ohnuma, M., and Mabuchi, I. (1997). Identification of actin-binding proteins from sea urchin eggs by F-actin affinity column chromatography. J. Biochem. 122, 226-236.
    • (1997) J. Biochem. , vol.122 , pp. 226-236
    • Terasaki, A.G.1    Ohnuma, M.2    Mabuchi, I.3
  • 37
    • 0019503649 scopus 로고
    • Actin filaments elongate from their membrane-associated ends
    • Tilney, L.G., Bonder, E.M., and DeRosier, D.J. (1981). Actin filaments elongate from their membrane-associated ends. J. Cell Biol. 90, 485-494.
    • (1981) J. Cell Biol. , vol.90 , pp. 485-494
    • Tilney, L.G.1    Bonder, E.M.2    DeRosier, D.J.3
  • 39
    • 0024363256 scopus 로고
    • Acanthamoeba actin and profilin can be crosslinked between glutamic acid 364 of actin and lysine 115 of profilin
    • Vandekerchove, J., Kaiser, D.A., and Pollard, T.D. (1989). Acanthamoeba actin and profilin can be crosslinked between glutamic acid 364 of actin and lysine 115 of profilin. J. Cell Biol. 109, 619-626.
    • (1989) J. Cell Biol. , vol.109 , pp. 619-626
    • Vandekerchove, J.1    Kaiser, D.A.2    Pollard, T.D.3
  • 40
    • 0027162413 scopus 로고
    • Affinity of alpha-actinin for actin filaments determines the structure and mechanical properties of actin filament gels
    • Wachsstock, D.H., Schwarz, W.H., and Pollard, T.D. (1993a). Affinity of alpha-actinin for actin filaments determines the structure and mechanical properties of actin filament gels. Biophys. J. 65, 205-214.
    • (1993) Biophys. J. , vol.65 , pp. 205-214
    • Wachsstock, D.H.1    Schwarz, W.H.2    Pollard, T.D.3
  • 41
    • 0027162413 scopus 로고
    • Structure and mechanical properties of actin filament gels
    • Wachsstock, D.H., Schwarz, W.H., Pollard, T.D. (1993b). Structure and mechanical properties of actin filament gels. Biophys. J. 65, 205-214.
    • (1993) Biophys. J. , vol.65 , pp. 205-214
    • Wachsstock, D.H.1    Schwarz, W.H.2    Pollard, T.D.3
  • 42
    • 0022390903 scopus 로고
    • Exchange of actin subunits at the leading edge of living fibroblasts: Possible role of treadmilling
    • Wang, Y. (1985). Exchange of actin subunits at the leading edge of living fibroblasts: Possible role of treadmilling. J. Cell Biol. 101, 597-602.
    • (1985) J. Cell Biol. , vol.101 , pp. 597-602
    • Wang, Y.1
  • 43
    • 0031021153 scopus 로고    scopus 로고
    • Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes
    • Welch, M.D., Iwamatsu, A., and Mitchison, T.J. (1997a). Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes. Nature 385, 265-269.
    • (1997) Nature , vol.385 , pp. 265-269
    • Welch, M.D.1    Iwamatsu, A.2    Mitchison, T.J.3
  • 44
    • 0030802671 scopus 로고    scopus 로고
    • The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly
    • Welch, M.D., Iwamatsu, A., and Mitchison, T.J. (1997b). The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly. J. Cell Biol. 138, 375-384.
    • (1997) J. Cell Biol. , vol.138 , pp. 375-384
    • Welch, M.D.1    Iwamatsu, A.2    Mitchison, T.J.3
  • 45
    • 0031193920 scopus 로고    scopus 로고
    • The complex containing actin-related proteins Arp2 and Arp3 is required for the motility and integrity of yeast actin patches
    • Winter, D., Podtelejnikov, A.V., Mann, M., and Li, R. (1997). The complex containing actin-related proteins Arp2 and Arp3 is required for the motility and integrity of yeast actin patches. Curr. Biol. 7, 519-529.
    • (1997) Curr. Biol. , vol.7 , pp. 519-529
    • Winter, D.1    Podtelejnikov, A.V.2    Mann, M.3    Li, R.4
  • 46
    • 0026754022 scopus 로고
    • Localization of myosin-I and myosin-II in Acanthamoeba
    • Yonemura, S.Y., and Pollard, T.D. (1992). Localization of myosin-I and myosin-II in Acanthamoeba. J. Cell Sci. 102, 629-642.
    • (1992) J. Cell Sci. , vol.102 , pp. 629-642
    • Yonemura, S.Y.1    Pollard, T.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.