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Volumn 8, Issue 1, 1996, Pages 30-37

The actin-related proteins

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN RELATED PROTEIN; CELL PROTEIN; CYTOSKELETON PROTEIN; DYNEIN ADENOSINE TRIPHOSPHATASE; UNCLASSIFIED DRUG;

EID: 0030059701     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(96)80045-7     Document Type: Article
Times cited : (80)

References (56)
  • 2
    • 0025100372 scopus 로고
    • Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
    • Flaherty KM, DeLuca-Flaherty C, McKay DB: Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Nature 1990, 346:623-628.
    • (1990) Nature , vol.346 , pp. 623-628
    • Flaherty, K.M.1    DeLuca-Flaherty, C.2    McKay, D.B.3
  • 3
    • 0025753142 scopus 로고
    • Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein
    • Flaherty KM, McKay DB, Kabsch W, Holmes KC: Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein. Proc Natl Acad Sci USA 1991, 88:5041-5045.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5041-5045
    • Flaherty, K.M.1    McKay, D.B.2    Kabsch, W.3    Holmes, K.C.4
  • 4
    • 0026571486 scopus 로고
    • New yeast actin-like gene required late in the cell cycle
    • Schwob E, Martin RP: New yeast actin-like gene required late in the cell cycle. Nature 1992, 355:179-182.
    • (1992) Nature , vol.355 , pp. 179-182
    • Schwob, E.1    Martin, R.P.2
  • 5
    • 0026502684 scopus 로고
    • Identification of act2, an essential gene in the fission yeast Schizosaccharomyces pombe that encodes a protein related to actin
    • Lees-Miller JP, Henry G, Helfman DM: Identification of act2, an essential gene in the fission yeast Schizosaccharomyces pombe that encodes a protein related to actin. Proc Natl Acad Sci USA 1992, 89:80-83.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 80-83
    • Lees-Miller, J.P.1    Henry, G.2    Helfman, D.M.3
  • 6
    • 0026783380 scopus 로고
    • A vertebrate actin-related protein Is a component of a multisubunit complex involved in microtubule-based vesicle motility
    • Lees-Miller JP, Helfman DM, Schroer TA: A vertebrate actin-related protein Is a component of a multisubunit complex involved in microtubule-based vesicle motility. Nature 1992, 359:244-246.
    • (1992) Nature , vol.359 , pp. 244-246
    • Lees-Miller, J.P.1    Helfman, D.M.2    Schroer, T.A.3
  • 7
    • 0026686929 scopus 로고
    • Centractin is an actin homologue associated with the centrosome
    • Clark SW, Meyer DI: Centractin is an actin homologue associated with the centrosome. Nature 1992, 359:246-250.
    • (1992) Nature , vol.359 , pp. 246-250
    • Clark, S.W.1    Meyer, D.I.2
  • 9
    • 0027429118 scopus 로고
    • A Drosophila homologue of the Schizosaccharomyces pombe act2 gene
    • Fyrberg C, Fyrberg E: A Drosophila homologue of the Schizosaccharomyces pombe act2 gene. Biochem Genet 1993, 31:329-341.
    • (1993) Biochem Genet , vol.31 , pp. 329-341
    • Fyrberg, C.1    Fyrberg, E.2
  • 11
    • 0028049540 scopus 로고
    • Genes encoding actin-related proteins of Drosophila melanogaster
    • Fyrberg C, Ryan L, Kenton M, Fyrberg E: Genes encoding actin-related proteins of Drosophila melanogaster. J Mol Biol 1994, 241:498-503.
    • (1994) J Mol Biol , vol.241 , pp. 498-503
    • Fyrberg, C.1    Ryan, L.2    Kenton, M.3    Fyrberg, E.4
  • 12
    • 0028048630 scopus 로고
    • An essential gene of Saccharomyces cerevisiae coding for an actin-related protein
    • Harata M, Karwan A, Wintersberger U: An essential gene of Saccharomyces cerevisiae coding for an actin-related protein. Proc Natl Acad Sci USA 1994, 91:8258-8262.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8258-8262
    • Harata, M.1    Karwan, A.2    Wintersberger, U.3
  • 13
    • 0028025571 scopus 로고
    • A yeast actin-related protein homologous to that in vertebrate dynactin complex is important for spindle orientation and nuclear migration
    • Muhua L, Karpova TS, Cooper JA: A yeast actin-related protein homologous to that in vertebrate dynactin complex is important for spindle orientation and nuclear migration. Cell 1994, 78:669-679.
    • (1994) Cell , vol.78 , pp. 669-679
    • Muhua, L.1    Karpova, T.S.2    Cooper, J.A.3
  • 14
    • 0028074840 scopus 로고
    • ACT3: A putative centractin homologue in S. cerevisiae is required for proper orientation of the mitotic spindle
    • Clark SW, Meyer DI: ACT3: a putative centractin homologue in S. cerevisiae is required for proper orientation of the mitotic spindle. J Cell Biol 1994, 127:129-138.
    • (1994) J Cell Biol , vol.127 , pp. 129-138
    • Clark, S.W.1    Meyer, D.I.2
  • 15
    • 0028067033 scopus 로고
    • Cytoplasmic dynein and actin-related protein Arp1 are required for normal nuclear distribution in filamentous fungi
    • Plamann M, Minke PF, Tinsley JH, Bruno KS: Cytoplasmic dynein and actin-related protein Arp1 are required for normal nuclear distribution in filamentous fungi. J Cell Biol 1994, 127:139-149.
    • (1994) J Cell Biol , vol.127 , pp. 139-149
    • Plamann, M.1    Minke, P.F.2    Tinsley, J.H.3    Bruno, K.S.4
  • 16
    • 0028670191 scopus 로고
    • β-centractin: Characterization and distribution of a new member of the centractin family of actin-related proteins
    • CLark SW, Staub O, Clark IB, Holzbaur ELF, Paschal BM, Vallee RB, Meyer DI: β-centractin: characterization and distribution of a new member of the centractin family of actin-related proteins. Mol Biol Cell 1994, 5:1301-1310.
    • (1994) Mol Biol Cell , vol.5 , pp. 1301-1310
    • Clark, S.W.1    Staub, O.2    Clark, I.B.3    Holzbaur, E.L.F.4    Paschal, B.M.5    Vallee, R.B.6    Meyer, D.I.7
  • 17
    • 0028136434 scopus 로고
    • Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin-agarose
    • Machesky LM, Atkinson SJ, Ampe C, Vandekerckhove J, Pollard TD: Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin-agarose. J Cell Biol 1994, 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
    • 0029034391 scopus 로고
    • A fungal actin-related protein involved in nuclear migration
    • Robb MJ, Wilson MA, Vierula PJ: A fungal actin-related protein involved in nuclear migration. Mol Gen Genet 1995, 247:583-590.
    • (1995) Mol Gen Genet , vol.247 , pp. 583-590
    • Robb, M.J.1    Wilson, M.A.2    Vierula, P.J.3
  • 19
    • 0029257454 scopus 로고
    • Cloning and identification of arp1, an actin-related protein from Pneumocystis carinii
    • Christopher LJ, Fletcher LD, Dykstra CC: Cloning and identification of arp1, an actin-related protein from Pneumocystis carinii. J Eukaryotic Microbiol 1995, 42:142-149.
    • (1995) J Eukaryotic Microbiol , vol.42 , pp. 142-149
    • Christopher, L.J.1    Fletcher, L.D.2    Dykstra, C.C.3
  • 20
    • 0028966843 scopus 로고
    • An actin-related protein from Dictyostelium discoideum is developmentally regulated and associated with mitochondria
    • Murgia I, Maciver SK, Morandini P: An actin-related protein from Dictyostelium discoideum is developmentally regulated and associated with mitochondria. FEBS Lett 1995, 360:235-241.
    • (1995) FEBS Lett , vol.360 , pp. 235-241
    • Murgia, I.1    Maciver, S.K.2    Morandini, P.3
  • 21
    • 0028928993 scopus 로고
    • Isolation and characterization of a cDNa encoding a chicken actin-like protein
    • Michaille J-J, Gouy M, Blanchet S, Duret L: Isolation and characterization of a cDNA encoding a chicken actin-like protein. Gene 1995, 154:205-209.
    • (1995) Gene , vol.154 , pp. 205-209
    • Michaille, J.-J.1    Gouy, M.2    Blanchet, S.3    Duret, L.4
  • 22
    • 0028786352 scopus 로고
    • Sequences, structural models, and cellular localization of the actin-related proteins arp2 and arp3 from Acanthamoeba
    • Kelleher JF, Atkinson SJ, Pollard TD: Sequences, structural models, and cellular localization of the actin-related proteins arp2 and arp3 from Acanthamoeba. J Cell Biol 1995, 131:385-397.
    • (1995) J Cell Biol , vol.131 , pp. 385-397
    • Kelleher, J.F.1    Atkinson, S.J.2    Pollard, T.D.3
  • 24
  • 25
    • 0026687729 scopus 로고
    • An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin and hsp70 heat shock proteins
    • Bork P, Sander C, Valencia A: An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin and hsp70 heat shock proteins. Proc Natl Acad Sci USA 1992, 89:7290-7294.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 7290-7294
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 28
    • 0002237472 scopus 로고
    • Cytosolic hsp70s of Saccharomyces cerevisiae: Roles in protein synthesis, protein translocation, proteolysis and regulation
    • Edited by Morimoto RI, Tissieres A, Georgopoulos C. Cold Spring Harbor: Cold Spring Harbor Press
    • Craig EA, Baxter BK, Becker J, Halladay J, Ziegelhoffer T: Cytosolic hsp70s of Saccharomyces cerevisiae: roles in protein synthesis, protein translocation, proteolysis and regulation. In The Biology of Heat Shock Proteins and Molecular Chaperones. Edited by Morimoto RI, Tissieres A, Georgopoulos C. Cold Spring Harbor: Cold Spring Harbor Press; 1994:31-52.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 31-52
    • Craig, E.A.1    Baxter, B.K.2    Becker, J.3    Halladay, J.4    Ziegelhoffer, T.5
  • 29
    • 0028146484 scopus 로고
    • New insights into the interaction of cytoplasmic dynein with the actin-related protein, arp1
    • Schroer TA: New insights into the interaction of cytoplasmic dynein with the actin-related protein, arp1. J Cel Biol 1994, 127:1-4.
    • (1994) J Cel Biol , vol.127 , pp. 1-4
    • Schroer, T.A.1
  • 30
    • 0028540597 scopus 로고
    • Dynactin: Portrait of a dynein regulator
    • Allen V: Dynactin: portrait of a dynein regulator. Curr Biol 1994, 4:1000-1002.
    • (1994) Curr Biol , vol.4 , pp. 1000-1002
    • Allen, V.1
  • 31
    • 0025789647 scopus 로고
    • Two activators of microtubule-based vesicle transport
    • Schroer TA, Sheetz MP: Two activators of microtubule-based vesicle transport. J Cell Biol 1991, 115:1309-1318.
    • (1991) J Cell Biol , vol.115 , pp. 1309-1318
    • Schroer, T.A.1    Sheetz, M.P.2
  • 32
    • 0028304474 scopus 로고
    • Ultrastructural analysis of the dynactin complex: An actin-related protein is a component of a filament that resembles F-actin
    • Schafer DA, Gill SR, Cooper JA, Heuser JE, Schroer TA: Ultrastructural analysis of the dynactin complex: an actin-related protein is a component of a filament that resembles F-actin. J Cell Biol 1994, 126:403-412.
    • (1994) J Cell Biol , vol.126 , pp. 403-412
    • Schafer, D.A.1    Gill, S.R.2    Cooper, J.A.3    Heuser, J.E.4    Schroer, T.A.5
  • 33
    • 0028986631 scopus 로고
    • Glued component of the dynactin complex binds to both microtubules and the actin-related protein centractin (Arp-1)
    • Glued component of the dynactin complex binds to both microtubules and the actin-related protein centractin (Arp-1). Proc Natl Acad Sci USA 1995, 92:1634-1638.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1634-1638
    • Waterman-Storer, C.M.1    Karki, S.2    Holzbaur, E.L.F.3
  • 34
    • 0028863843 scopus 로고
    • The actin-related protein Act3p of Saccharomyces cerevisiae is located in the nucleus
    • Weber V, Harata M, Hauser H, Wintersberger U: The actin-related protein Act3p of Saccharomyces cerevisiae is located in the nucleus. Mol Biol Cell 1995, 6:1263-1270.
    • (1995) Mol Biol Cell , vol.6 , pp. 1263-1270
    • Weber, V.1    Harata, M.2    Hauser, H.3    Wintersberger, U.4
  • 35
    • 0017716157 scopus 로고
    • Diffusible and bound actin in nuclei of Xenopus laevis oocytes
    • Clark TG, Merriam RW: Diffusible and bound actin in nuclei of Xenopus laevis oocytes. Cell 1977, 12:883-891.
    • (1977) Cell , vol.12 , pp. 883-891
    • Clark, T.G.1    Merriam, R.W.2
  • 36
    • 0018601589 scopus 로고
    • An actin filament matrix in handisolated nuclei of X. laevis oocytes
    • Clark TG, Rosenbaum JL: An actin filament matrix in handisolated nuclei of X. laevis oocytes. Cell 1979, 18:1101-1108.
    • (1979) Cell , vol.18 , pp. 1101-1108
    • Clark, T.G.1    Rosenbaum, J.L.2
  • 37
    • 0019423975 scopus 로고
    • Involvement of contractile proteins in the changes in consistency of oocyte nucleoplasm of the newt Pleurodeles waltii
    • Gounon P, Karsenti E: Involvement of contractile proteins in the changes in consistency of oocyte nucleoplasm of the newt Pleurodeles waltii. J Cell Biol 1981, 88:410-421.
    • (1981) J Cell Biol , vol.88 , pp. 410-421
    • Gounon, P.1    Karsenti, E.2
  • 39
    • 0018595534 scopus 로고
    • Intranuclear injection of anti-actin antibodies into Xenopus oocytes blocks chromosome condensation
    • Rungger D, Rungger-Brandle E, Chaponnier C, Gabbiani G: Intranuclear injection of anti-actin antibodies into Xenopus oocytes blocks chromosome condensation. Nature 1979, 282:320-321.
    • (1979) Nature , vol.282 , pp. 320-321
    • Rungger, D.1    Rungger-Brandle, E.2    Chaponnier, C.3    Gabbiani, G.4
  • 40
    • 0021677114 scopus 로고
    • Microinjection of actin-binding proteins and actin antibodies demonstrates involvement of nudear actin in transcription of lampbrush chromosomes
    • Scheer U, Hinssen H, Franke WW, Jockusch B: Microinjection of actin-binding proteins and actin antibodies demonstrates involvement of nudear actin in transcription of lampbrush chromosomes. Cell 1984, 39:111-122.
    • (1984) Cell , vol.39 , pp. 111-122
    • Scheer, U.1    Hinssen, H.2    Franke, W.W.3    Jockusch, B.4
  • 41
    • 0022447223 scopus 로고
    • Preferential association of acidic actin with nuclei and nuclear matrix from mouse leukemia L5178Y cells
    • Nakayasu H, Ueda K: Preferential association of acidic actin with nuclei and nuclear matrix from mouse leukemia L5178Y cells. Exp Cell Res 1986, 163:327-336.
    • (1986) Exp Cell Res , vol.163 , pp. 327-336
    • Nakayasu, H.1    Ueda, K.2
  • 42
    • 0026345013 scopus 로고
    • Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dyneln
    • Gill SR, Schroer TA, Szilak I, Steuer ER, Sheetz MP, Cleveland DW: Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dyneln. J Cell Biol 1991, 115:1639-1650.
    • (1991) J Cell Biol , vol.115 , pp. 1639-1650
    • Gill, S.R.1    Schroer, T.A.2    Szilak, I.3    Steuer, E.R.4    Sheetz, M.P.5    Cleveland, D.W.6
  • 44
    • 0026539415 scopus 로고
    • Suppression of a myosin defect by a kinesin related gene
    • Lillie S, Brown S: Suppression of a myosin defect by a kinesin related gene. Nature 1992, 356:358-361.
    • (1992) Nature , vol.356 , pp. 358-361
    • Lillie, S.1    Brown, S.2
  • 45
    • 0028806377 scopus 로고
    • Affinity chromatography demonstrates a direct binding between cytoplasmic dynein and the dynactin complex
    • Karki S, Holzbaur ELF: Affinity chromatography demonstrates a direct binding between cytoplasmic dynein and the dynactin complex. J Biol Chem 1995, 270:28806-28811.
    • (1995) J Biol Chem , vol.270 , pp. 28806-28811
    • Karki, S.1    Elf, H.2
  • 47
    • 0028787443 scopus 로고
    • Regulation of cytoplasmic dynein function in vivo by the Drosophila Glued complex
    • McGrail M, Gepner J, Silvanovich A, Ludmann S, Serr M, Hays TS: Regulation of cytoplasmic dynein function in vivo by the Drosophila Glued complex. J Cell Biol 1995, 131:411-425.
    • (1995) J Cell Biol , vol.131 , pp. 411-425
    • McGrail, M.1    Gepner, J.2    Silvanovich, A.3    Ludmann, S.4    Serr, M.5    Hays, T.S.6
  • 48
    • 0027293897 scopus 로고
    • Chaperonin-mediated folding of vertebrate actin-related protein and gamma tubulin
    • Melki R, Vainberg IE, Chow RL, Cowan NJ: Chaperonin-mediated folding of vertebrate actin-related protein and gamma tubulin. J Cell Biol 1993, 122:1301-1310.
    • (1993) J Cell Biol , vol.122 , pp. 1301-1310
    • Melki, R.1    Vainberg, I.E.2    Chow, R.L.3    Cowan, N.J.4
  • 49
    • 0022555884 scopus 로고
    • Actin and actin-binding proteins: A critical evaluation of mechanisms and functions
    • Pollard TD, Cooper JA: Actin and actin-binding proteins: a critical evaluation of mechanisms and functions. Annu Rev Biochem 1986, 55:987-1035.
    • (1986) Annu Rev Biochem , vol.55 , pp. 987-1035
    • Pollard, T.D.1    Cooper, J.A.2
  • 51
    • 0029013908 scopus 로고
    • The role of ATP in the functional cycle of the DnaK chaperone system
    • McCarty JS, Buchberger A, Reinstein J, Bukau B: The role of ATP in the functional cycle of the DnaK chaperone system. J Mol Biol 1995, 249:126-137.
    • (1995) J Mol Biol , vol.249 , pp. 126-137
    • McCarty, J.S.1    Buchberger, A.2    Reinstein, J.3    Bukau, B.4
  • 52
    • 0002664005 scopus 로고
    • Interactions of vertebrate hsc70 and hsp70 with unfolded proteins and peptides
    • Edited by Morimoto RI, Tissieres A, Georgopoulos C. Cold Spring Harbor: Cold Spring Harbor Press
    • Hightower LE, Sadis SE, Takenaka IM: Interactions of vertebrate hsc70 and hsp70 with unfolded proteins and peptides. In The Biology of Heat Shock Proteins and Molecular Chaperones. Edited by Morimoto RI, Tissieres A, Georgopoulos C. Cold Spring Harbor: Cold Spring Harbor Press; 1994:179-207.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 179-207
    • Hightower, L.E.1    Sadis, S.E.2    Takenaka, I.M.3
  • 53
    • 0026669643 scopus 로고
    • Constitutive hsp70: Oligomerization and its dependence on ATP binding
    • Kim D, Lee YJ, Corry PM: Constitutive hsp70: oligomerization and its dependence on ATP binding. J Cell Physiol 1992, 153:353-361.
    • (1992) J Cell Physiol , vol.153 , pp. 353-361
    • Kim, D.1    Lee, Y.J.2    Corry, P.M.3
  • 54
    • 0028929052 scopus 로고
    • The DnaK chaperone system of Escherichia coli: Quaternary structures and interactions of the DnaK and GrpE components
    • Schonfeld H-J, Schmidt D, Schroder H, Bukau B: The DnaK chaperone system of Escherichia coli: quaternary structures and interactions of the DnaK and GrpE components. J Biol Chem 1995, 270:2183-2189.
    • (1995) J Biol Chem , vol.270 , pp. 2183-2189
    • Schonfeld, H.-J.1    Schmidt, D.2    Schroder, H.3    Bukau, B.4
  • 55
    • 0025910365 scopus 로고
    • Structure and function of signal-transducing GTP-binding proteins
    • Kaziro Y, Itoh H, Kozasa T, Nakafuku M, Satoh T: Structure and function of signal-transducing GTP-binding proteins. Annu Rev Biochem 1991, 60:349-400.
    • (1991) Annu Rev Biochem , vol.60 , pp. 349-400
    • Kaziro, Y.1    Itoh, H.2    Kozasa, T.3    Nakafuku, M.4    Satoh, T.5
  • 56
    • 0029913484 scopus 로고
    • Molecular characterization of 50kD subunit of dynactin reveals function for the complex in chromosome alignment and spindle organization during mitosis
    • in press
    • Echeverri CJ, Paschal BM, Vaughan KT, Vallee RB: Molecular characterization of 50kD subunit of dynactin reveals function for the complex in chromosome alignment and spindle organization during mitosis. J Cell Biol 1995, in press.
    • (1995) J Cell Biol
    • Echeverri, C.J.1    Paschal, B.M.2    Vaughan, K.T.3    Vallee, R.B.4


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