메뉴 건너뛰기




Volumn 4, Issue 1, 1997, Pages 12-18

Rho GTPases and leukocyte cytoskeletal regulation

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATASE; RHO FACTOR;

EID: 0031046030     PISSN: 10656251     EISSN: None     Source Type: Journal    
DOI: 10.1097/00062752-199704010-00003     Document Type: Review
Times cited : (31)

References (83)
  • 1
    • 0030021649 scopus 로고    scopus 로고
    • Signal transduction and actin filament organization
    • Zigmond SH: Signal transduction and actin filament organization. Curr Opin Cell Biol 1996, 8:66-73. Excellent review of the actin cytoskeleton.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 66-73
    • Zigmond, S.H.1
  • 2
    • 0028366744 scopus 로고
    • Actin polymerization and leukocyte function
    • Howard TH, Watts RG: Actin polymerization and leukocyte function. Curr Opin Hematol 1994, 1:61-68.
    • (1994) Curr Opin Hematol , vol.1 , pp. 61-68
    • Howard, T.H.1    Watts, R.G.2
  • 3
    • 0030222377 scopus 로고    scopus 로고
    • Rho: A connection between membrane receptor signaling and the cytoskeleton
    • Machesky LM, Hall A: Rho: a connection between membrane receptor signaling and the cytoskeleton. Trends Cell Biol 1996, 6:304-310. Excellent recent review on the actin cytoskeleton, with emphasis on regulation by the Rho GTPase family. Discusses Rho GTPase effectors, possible mechanisms of actin filament rearrangement, and actin-binding proteins that may be regulatory targets.
    • (1996) Trends Cell Biol , vol.6 , pp. 304-310
    • Machesky, L.M.1    Hall, A.2
  • 4
    • 0028961293 scopus 로고
    • Rho, Rac, and CDC42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes CD, Hall A: Rho, Rac, and CDC42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 1995, 81:53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 5
    • 0029099616 scopus 로고    scopus 로고
    • Chemoattractant signaling and leukocyte activation
    • Bokoch GM: Chemoattractant signaling and leukocyte activation. Blood 1996, 86:1649-1660. Comprehensive update on chemoattractant signaling in leukocytes and the involvement of small GTPases in leukocyte activation.
    • (1996) Blood , vol.86 , pp. 1649-1660
    • Bokoch, G.M.1
  • 6
    • 0029815128 scopus 로고    scopus 로고
    • Interplay between Ras-related and heterotrimeric GTP binding proteins: Lifestyles of the BIG and LITTLE
    • Bokoch GM: Interplay between Ras-related and heterotrimeric GTP binding proteins: lifestyles of the BIG and LITTLE. FASEB J 1996, 10:1290-1295.
    • (1996) FASEB J , vol.10 , pp. 1290-1295
    • Bokoch, G.M.1
  • 7
    • 0027732538 scopus 로고
    • Proteins regulating Ras and its relatives
    • Boguski MS, McCormick F: Proteins regulating Ras and its relatives. Nature 1993, 366:643-654.
    • (1993) Nature , vol.366 , pp. 643-654
    • Boguski, M.S.1    McCormick, F.2
  • 8
    • 0027232605 scopus 로고
    • Emerging concepts in the ras superfamily of GTP-binding proteins
    • Bokoch GM, Der CJ: Emerging concepts in the ras superfamily of GTP-binding proteins. FASEB J 1993, 7:750-759.
    • (1993) FASEB J , vol.7 , pp. 750-759
    • Bokoch, G.M.1    Der, C.J.2
  • 9
    • 0028081350 scopus 로고
    • Guanine nucleotide exchange regulates membrane translocation of Rac/Rho GTP-binding proteins
    • Bokoch GM, Bohl BP, Chuang TH: Guanine nucleotide exchange regulates membrane translocation of Rac/Rho GTP-binding proteins. J Biol Chem 1994, 269:31674-31679.
    • (1994) J Biol Chem , vol.269 , pp. 31674-31679
    • Bokoch, G.M.1    Bohl, B.P.2    Chuang, T.H.3
  • 10
    • 0028225439 scopus 로고
    • Identification of an invasion-inducing gene, Tiam-1, that encodes a protein with homology to GDP-GTP exchangers for Rho-like proteins
    • Habets GGM, Schultese HM, Zuydgeest D, van der Kammen RA, Stam JC, Berns A, Collard JG: Identification of an invasion-inducing gene, Tiam-1, that encodes a protein with homology to GDP-GTP exchangers for Rho-like proteins. Cell 1994, 77:537-549.
    • (1994) Cell , vol.77 , pp. 537-549
    • Habets, G.G.M.1    Schultese, H.M.2    Zuydgeest, D.3    Van Der Kammen, R.A.4    Stam, J.C.5    Berns, A.6    Collard, J.G.7
  • 12
    • 0024451176 scopus 로고
    • Guanine nucleotide-induced polymerization of actin in electropermeabilized human neutrophils
    • Therrien S, Naccache PH: Guanine nucleotide-induced polymerization of actin in electropermeabilized human neutrophils. J Cell Biol 1989, 109:1125-1132.
    • (1989) J Cell Biol , vol.109 , pp. 1125-1132
    • Therrien, S.1    Naccache, P.H.2
  • 13
    • 0024439874 scopus 로고
    • Actin assembly in electropermeabilized neutrophils: Role of G-proteins
    • Downey GP, Chan CK, Grinstein S: Actin assembly in electropermeabilized neutrophils: role of G-proteins. Biochem Biophys Res Commun 1989, 164:700-705.
    • (1989) Biochem Biophys Res Commun , vol.164 , pp. 700-705
    • Downey, G.P.1    Chan, C.K.2    Grinstein, S.3
  • 14
    • 0025264696 scopus 로고
    • Involvement of GTP-binding proteins in actin polymerization in human neutrophils
    • Bengtsson T, Sarndahl E, Stendahl O, Andersson T: Involvement of GTP-binding proteins in actin polymerization in human neutrophils. Proc Natl Acad Sci U S A 1990, 87:2921-2925.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 2921-2925
    • Bengtsson, T.1    Sarndahl, E.2    Stendahl, O.3    Andersson, T.4
  • 15
    • 0028846966 scopus 로고
    • Actin polymerization induced by GTPγS in permeabilized neutrophils is induced and maintained by free barbed ends
    • Tardif M, Huang S, Redmond T, Safer D, Pring M, Zigmond SH: Actin polymerization induced by GTPγS in permeabilized neutrophils is induced and maintained by free barbed ends. J Biol Chem 1995, 270:28075-28083.
    • (1995) J Biol Chem , vol.270 , pp. 28075-28083
    • Tardif, M.1    Huang, S.2    Redmond, T.3    Safer, D.4    Pring, M.5    Zigmond, S.H.6
  • 16
    • 0029089841 scopus 로고
    • ADP-ribosylation of Rho enhances actin polymerization-coupled shape oscillations in human neutrophils
    • Ehrengruber MU, Boquet P, Coates TD, Deranleau DA: ADP-ribosylation of Rho enhances actin polymerization-coupled shape oscillations in human neutrophils. FEBS Lett 1995, 372:161-164. Describes the involvement of Rho in coordinated cycles of actin and cell shape oscillations, possibly related to neutrophil motility. Inactivation of Rho by C3 exoenzyme affects actin polymerization and depolymerization oscillations, but not nucleation in response to chemoattractants.
    • (1995) FEBS Lett , vol.372 , pp. 161-164
    • Ehrengruber, M.U.1    Boquet, P.2    Coates, T.D.3    Deranleau, D.A.4
  • 17
    • 0028259050 scopus 로고
    • ADP-ribosylation of the GTP-binding protein RHO by Clostridium limosum exoenzyme affects basal, but not N-formyl-peptide-stimulated, actin polymerization in human myeloid leukaemic (HL60) cells
    • Koch G, Norgauer J, Aktories K: ADP-ribosylation of the GTP-binding protein RHO by Clostridium limosum exoenzyme affects basal, but not N-formyl-peptide-stimulated, actin polymerization in human myeloid leukaemic (HL60) cells. Biochem J 1994, 299:775-779.
    • (1994) Biochem J , vol.299 , pp. 775-779
    • Koch, G.1    Norgauer, J.2    Aktories, K.3
  • 18
    • 0030059222 scopus 로고    scopus 로고
    • Role of Rho in chemoattractant-activated leukocyte adhesion through integrins
    • Laudanna C, Campbell JJ, Butcher EC: Role of Rho in chemoattractant-activated leukocyte adhesion through integrins. Science 1996, 271:981-983. Analysis of the N-formylpeptide and interleukin-8 chemoattractant receptors transfected into lymphocytes indicates they stimulate guanine nucleotide exchange on the Rho GTPase. Inactivation of Rho using C3 exoenzyme inhibits integrin-mediated cell adhesion, thus implicating Rho in the regulation of rapid leukocyte adhesion during chemotaxis.
    • (1996) Science , vol.271 , pp. 981-983
    • Laudanna, C.1    Campbell, J.J.2    Butcher, E.C.3
  • 19
    • 0027471215 scopus 로고
    • Inhibition of PMA-induced, LFA-1-dependent lymphocyte aggregation by ADP ribosylation of the small molecular weight GTP binding protein, rho
    • Tominaga T, Sugie K, Morii N, Fukata J, Uchida A, Imura H, Narumiya S: Inhibition of PMA-induced, LFA-1-dependent lymphocyte aggregation by ADP ribosylation of the small molecular weight GTP binding protein, rho. J Cell Biol 1993, 120:1529-1537.
    • (1993) J Cell Biol , vol.120 , pp. 1529-1537
    • Tominaga, T.1    Sugie, K.2    Morii, N.3    Fukata, J.4    Uchida, A.5    Imura, H.6    Narumiya, S.7
  • 20
    • 0025833804 scopus 로고
    • ADP-ribosylation of a small size GTP-binding protein in bovine neutrophils by the C3 exoenzyme of Clostridium botulinum and effect on the cell motility
    • Stasia M, Jovan A, Bourmeyster N, Boquet P, Vignais P: ADP-ribosylation of a small size GTP-binding protein in bovine neutrophils by the C3 exoenzyme of Clostridium botulinum and effect on the cell motility. Biochem Biophys Res Commun 1991, 180:615-622.
    • (1991) Biochem Biophys Res Commun , vol.180 , pp. 615-622
    • Stasia, M.1    Jovan, A.2    Bourmeyster, N.3    Boquet, P.4    Vignais, P.5
  • 21
    • 0028070036 scopus 로고
    • Actin filament organization in activated mast cells is regulated by heterotrimeric and small GTP-binding proteins
    • Norman JC, Price LS, Ridley AJ, Hall A, Koffer A: Actin filament organization in activated mast cells is regulated by heterotrimeric and small GTP-binding proteins. J Cell Biol 1994, 126:1005-1015.
    • (1994) J Cell Biol , vol.126 , pp. 1005-1015
    • Norman, J.C.1    Price, L.S.2    Ridley, A.J.3    Hall, A.4    Koffer, A.5
  • 22
    • 0029876343 scopus 로고    scopus 로고
    • Purification and identification of FOAD-II, a cytosolic protein that regulates secretion in streptolysin-O permeabilized mast cells, as a Rac/RhoGDI complex
    • O'Sullivan AJ, Brown AM, Freeman HNM, Gomperts BD: Purification and identification of FOAD-II, a cytosolic protein that regulates secretion in streptolysin-O permeabilized mast cells, as a Rac/RhoGDI complex. Mol Biol Cell 1996, 7:397-408.
    • (1996) Mol Biol Cell , vol.7 , pp. 397-408
    • O'Sullivan, A.J.1    Brown, A.M.2    Freeman, H.N.M.3    Gomperts, B.D.4
  • 23
    • 0028958547 scopus 로고
    • Chronic myeloid leukemia granulocytes exhibit reduced actin polymerization after chemotactic peptide stimulation
    • Tarachandani A, Advani SH, Bhisey AN: Chronic myeloid leukemia granulocytes exhibit reduced actin polymerization after chemotactic peptide stimulation. Hematol Pathol 1994, 9:27-35.
    • (1994) Hematol Pathol , vol.9 , pp. 27-35
    • Tarachandani, A.1    Advani, S.H.2    Bhisey, A.N.3
  • 25
    • 0028078824 scopus 로고
    • A brain serine/threonine protein kinase activated by Cdc42 and Rac1
    • Manser E, Leung T, Salihuddin H, Zhao Z, Lim L: A brain serine/threonine protein kinase activated by Cdc42 and Rac1. Nature 1994, 367:40-46.
    • (1994) Nature , vol.367 , pp. 40-46
    • Manser, E.1    Leung, T.2    Salihuddin, H.3    Zhao, Z.4    Lim, L.5
  • 26
    • 0028998794 scopus 로고
    • Regulation of human leukocyte p21-activated kinases through G protein-coupled receptors
    • Knaus UG, Morris S, Dong H, Chernoff J, Bokoch GM: Regulation of human leukocyte p21-activated kinases through G protein-coupled receptors. Science 1995, 269:221-223. Chemoattractants are shown to rapidly activate PAKs, which are downstream effectors of Rac and Cdc42. PAKs may regulate phagocyte activation by phosphorylating the p47phox component of the NADPH oxidase.
    • (1995) Science , vol.269 , pp. 221-223
    • Knaus, U.G.1    Morris, S.2    Dong, H.3    Chernoff, J.4    Bokoch, G.M.5
  • 27
    • 0029780095 scopus 로고    scopus 로고
    • The renaturable 69 and 63 kDa protein kinases that undergo rapid activation in chemoattractant-stimulated neutrophils are p21-activated kinases (Paks)
    • Ding J, Knaus UG, Lian JP, Bokoch GM, Badwey JA: The renaturable 69 and 63 kDa protein kinases that undergo rapid activation in chemoattractant-stimulated neutrophils are p21-activated kinases (Paks). J Biol Chem 1996, 271:24869-24873.
    • (1996) J Biol Chem , vol.271 , pp. 24869-24873
    • Ding, J.1    Knaus, U.G.2    Lian, J.P.3    Bokoch, G.M.4    Badwey, J.A.5
  • 28
    • 0029091498 scopus 로고
    • Ste20-like protein kinases are required for normal localization of cell growth and for cytokinesis in budding yeast
    • Cvrcková F, De Virgilio C, Manser E, Pringle JR, Nasmyth K: Ste20-like protein kinases are required for normal localization of cell growth and for cytokinesis in budding yeast Genes Dev 1995, 9:1817-1830.
    • (1995) Genes Dev , vol.9 , pp. 1817-1830
    • Cvrcková, F.1    De Virgilio, C.2    Manser, E.3    Pringle, J.R.4    Nasmyth, K.5
  • 29
    • 0028884447 scopus 로고
    • Pheromone response in yeast: Association of Bem1p with proteins of the MAP kinase cascade and actin
    • Leeuw T, Forrest-Lieuvin A, Wu C, Chenevert J, Clark K, Whiteway M, Thomas DY, Leberer E: Pheromone response in yeast: association of Bem1p with proteins of the MAP kinase cascade and actin. Science 1995, 270:1210-1213. First report that shows a direct link between a downstream effector of a Rho family protein and F-actin. Bem1 may act as a bridge between Ste20 (effector of Cdc42) and actin, as observed by coimmunoprecipitation experiments.
    • (1995) Science , vol.270 , pp. 1210-1213
    • Leeuw, T.1    Forrest-Lieuvin, A.2    Wu, C.3    Chenevert, J.4    Clark, K.5    Whiteway, M.6    Thomas, D.Y.7    Leberer, E.8
  • 31
    • 0029008280 scopus 로고
    • Regulation of the polarization of T cells toward antigen-presenting cells by Ras-related GTPase CDC42
    • Stowers L, Yelon D, Berg LJ, Chant J: Regulation of the polarization of T cells toward antigen-presenting cells by Ras-related GTPase CDC42. Proc Natl Acad Sci U S A 1995, 92:5027-5031.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 5027-5031
    • Stowers, L.1    Yelon, D.2    Berg, L.J.3    Chant, J.4
  • 32
    • 0029757748 scopus 로고    scopus 로고
    • Identification of a novel Rac1-interacting protein involved in membrane ruffling
    • Van Aelst L, Joneson T, Bar-Sagi D: Identification of a novel Rac1-interacting protein involved in membrane ruffling. EMBO J 1996, 15:3778-3786. Reports on POR1, a novel protein that interacts with Rac 1 and may play a role downstream of Rac 1 in regulating membrane ruffling in fibroblasts.
    • (1996) EMBO J , vol.15 , pp. 3778-3786
    • Van Aelst, L.1    Joneson, T.2    Bar-Sagi, D.3
  • 34
    • 0029891491 scopus 로고    scopus 로고
    • IQGAP1, a calmodulin-binding protein with a rasGAP-related domain, is a potential effector for CDC42Hs
    • Hart MJ, Callow MG, Souza B, Polakis P: IQGAP1, a calmodulin-binding protein with a rasGAP-related domain, is a potential effector for CDC42Hs. EMBO J 1996, 15:2997-3005. This paper and that by Brill et al. (Mol Cell Biol 1996, 16:4869-4878) identify IQGAP as an effector target for Cdc42Hs.
    • (1996) EMBO J , vol.15 , pp. 2997-3005
    • Hart, M.J.1    Callow, M.G.2    Souza, B.3    Polakis, P.4
  • 35
    • 0029784514 scopus 로고    scopus 로고
    • The Ras GTPase-activating-protein-related human protein IQGAP2 harbors a potential actin binding domain and interacts with calmodulin and Rho family GTPases
    • Brill S, Li S, Lyman CW, Church DM, Wasmuth JJ, Weissbach L, Bernards A, Snijders AJ: The Ras GTPase-activating-protein-related human protein IQGAP2 harbors a potential actin binding domain and interacts with calmodulin and Rho family GTPases. Mol Cell Biol 1996, 16:4869-4878. This paper and that by Hart et al. (EMBO J 1996, 15:2997-3005) identify IQGAP as an effector target for Cdc42Hs. IQGAP may play a role in regulating Cdc42-mediated changes in the actin cytoskeleton because IQGAP has a putative actin-binding domain and is colocalized with actin to cortical extensions.
    • (1996) Mol Cell Biol , vol.16 , pp. 4869-4878
    • Brill, S.1    Li, S.2    Lyman, C.W.3    Church, D.M.4    Wasmuth, J.J.5    Weissbach, L.6    Bernards, A.7    Snijders, A.J.8
  • 36
    • 0027937223 scopus 로고
    • Isolation of a novel gene mutated in Wiskott-Aldrich syndrome
    • Derry JMJ, Ochs HD, Francke U: Isolation of a novel gene mutated in Wiskott-Aldrich syndrome. Cell 1994, 78:635-644.
    • (1994) Cell , vol.78 , pp. 635-644
    • Derry, J.M.J.1    Ochs, H.D.2    Francke, U.3
  • 37
    • 0030006284 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein, a novel effector for the GTPase Cdc42Hs, is implicated in actin polymerization
    • Symons M, Derry JMJ, Karlak B, Jiang S, Lemahieu V, McCormick F, Francke U, Abo A: Wiskott-Aldrich syndrome protein, a novel effector for the GTPase Cdc42Hs, is implicated in actin polymerization. Cell 1996, 84:723-734. Identifies WASP from neutrophil cytosol as a Cdc42Hs-binding protein using an overlay method. Expression of WASP produced clusters of WASP and F-actin, suggesting that WASP may be involved in Cdc42-mediated reorganization of the actin cytoskeleton.
    • (1996) Cell , vol.84 , pp. 723-734
    • Symons, M.1    Derry, J.M.J.2    Karlak, B.3    Jiang, S.4    Lemahieu, V.5    McCormick, F.6    Francke, U.7    Abo, A.8
  • 38
    • 0029680639 scopus 로고    scopus 로고
    • Two GTPases, Cdc42 and Rac, bind directly to a protein implicated in the immune deficiency disorder Wiskott-Aldrich syndrome
    • Aspenström P, Lindberg U, Hall A: Two GTPases, Cdc42 and Rac, bind directly to a protein implicated in the immune deficiency disorder Wiskott-Aldrich syndrome. Curr Biol 1996, 6:70-75. Yeast two-hybrid screening identified the WASP protein as a target of Cdc42. This report identified the Cdc42/Rac binding domain of WASP.
    • (1996) Curr Biol , vol.6 , pp. 70-75
    • Aspenström, P.1    Lindberg, U.2    Hall, A.3
  • 40
    • 0028260527 scopus 로고
    • A novel protein kinase with leucine zipper-like sequences: Its catalytic domain is highly homologous to that of protein kinase C
    • Mukai H, Ono Y: A novel protein kinase with leucine zipper-like sequences: its catalytic domain is highly homologous to that of protein kinase C. Biochem Biophys Res Commun 1994, 199:897-904.
    • (1994) Biochem Biophys Res Commun , vol.199 , pp. 897-904
    • Mukai, H.1    Ono, Y.2
  • 43
    • 0029889591 scopus 로고    scopus 로고
    • Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the Rho-binding domain
    • Reid T, Furuyashiki T, Ishizaki T, Watanabe G, Watanabe N, Fujisawa K, Morii N, Madaule P, Narumiya S: Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the Rho-binding domain. J Biol Chem 1996, 271:13556-13560.
    • (1996) J Biol Chem , vol.271 , pp. 13556-13560
    • Reid, T.1    Furuyashiki, T.2    Ishizaki, T.3    Watanabe, G.4    Watanabe, N.5    Fujisawa, K.6    Morii, N.7    Madaule, P.8    Narumiya, S.9
  • 44
    • 0028863142 scopus 로고
    • A novel serine/threonine kinase binding the Ras-related RhoA-GTPase which translocates the kinase to peripheral membranes
    • Leung T, Manser E, Tan L, Lim L: A novel serine/threonine kinase binding the Ras-related RhoA-GTPase which translocates the kinase to peripheral membranes. J Biol Chem 1995, 270:29051-29054. Reports on the isolation of rat cDNA encoding a serine-threonine kinase that binds RhoA, termed Rokα for RHoA-binding kinase. Rokα was recruited to membranes upon transfection of cultured cells with a dominant active form of Rho and was localized with cytoskeletal actin.
    • (1995) J Biol Chem , vol.270 , pp. 29051-29054
    • Leung, T.1    Manser, E.2    Tan, L.3    Lim, L.4
  • 45
    • 9244220646 scopus 로고    scopus 로고
    • The small GTP-binding protein Rho binds to and activates a 160 kDa ser/thr protein kinase homologous to myotonic dystrophy kinase
    • Ishizaki T, Maekawa M, Fujisawa K, Okawa K, Iwamatsu A, Fujita A, Watanabe N, Saito Y, Kakizuka A, Morii N, et al.: The small GTP-binding protein Rho binds to and activates a 160 kDa ser/thr protein kinase homologous to myotonic dystrophy kinase. EMBO J 1996, 15:1885-1893. Purified Rho kinase as a platelet protein that, when bound to Rho-GTP, exhibited enhanced autophosphorylation and kinase activity.
    • (1996) EMBO J , vol.15 , pp. 1885-1893
    • Ishizaki, T.1    Maekawa, M.2    Fujisawa, K.3    Okawa, K.4    Iwamatsu, A.5    Fujita, A.6    Watanabe, N.7    Saito, Y.8    Kakizuka, A.9    Morii, N.10
  • 46
    • 9244257348 scopus 로고    scopus 로고
    • Rho-associated kinase, a novel serine/threonine kinase, as a putative target for the small GTP binding protein Rho
    • Matsui T, Amano M, Yamamoto T, Chihara K, Nakafuku M, Ito M, Nakano T, Okawa K, Iwamatsu A, Kaibuchi K: Rho-associated kinase, a novel serine/threonine kinase, as a putative target for the small GTP binding protein Rho. EMBO J 1996, 15:2208-2216. Purified Rho kinase from bovine brain. Rho kinase was recruited to the membrane in the presence of activated Rho.
    • (1996) EMBO J , vol.15 , pp. 2208-2216
    • Matsui, T.1    Amano, M.2    Yamamoto, T.3    Chihara, K.4    Nakafuku, M.5    Ito, M.6    Nakano, T.7    Okawa, K.8    Iwamatsu, A.9    Kaibuchi, K.10
  • 47
    • 9444242736 scopus 로고    scopus 로고
    • Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase)
    • Kimura K, Ito M, Amano M, Chihara K, Fukata Y, Kakafuku M, Yamamori B, Feng J, Nakano T, Okawa K, et al.: Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase). Science 1996, 273:245-248. Presents evidence for the interaction of RhoA-GTP with myosin phosphatase, which regulates myosin light-chain phosphorylation. Rho activates Rho kinase, which phosphorylates the myosin binding subunit of myosin phosphatase. This phosphorylation inhibits myosin phosphatase activity and consequently increases myosin light-chain phosphorylation.
    • (1996) Science , vol.273 , pp. 245-248
    • Kimura, K.1    Ito, M.2    Amano, M.3    Chihara, K.4    Fukata, Y.5    Kakafuku, M.6    Yamamori, B.7    Feng, J.8    Nakano, T.9    Okawa, K.10
  • 48
    • 0029786313 scopus 로고    scopus 로고
    • Phosphorylation and activation of myosin by Rho-associated kinase (Rho-kinase)
    • Amano M, Ito M, Kimura K, Fukata Y, Chihara K, Nakano T, Matsuura Y, Kaibuchi K: Phosphorylation and activation of myosin by Rho-associated kinase (Rho-kinase). J Biol Chem 1996, 271:20246-20249. Implicates Rho in actomyosin-mediated contraction by showing that Rho kinase, which is activated by Rho-GTP, directly phosphorylates myosin light chain.
    • (1996) J Biol Chem , vol.271 , pp. 20246-20249
    • Amano, M.1    Ito, M.2    Kimura, K.3    Fukata, Y.4    Chihara, K.5    Nakano, T.6    Matsuura, Y.7    Kaibuchi, K.8
  • 50
    • 0028980248 scopus 로고
    • Involvement of Rho in GTPγS-induced enhancement of phosphorylation of 20kDa myosin light chain in vascular smooth muscle cells: Inhibition of phosphatase activity
    • Noda M, Yasuda-Fukazawa C, Moriishi K, Kato I, Okuda T, Kurokawa K, Takuwa Y: Involvement of Rho in GTPγS-induced enhancement of phosphorylation of 20kDa myosin light chain in vascular smooth muscle cells: inhibition of phosphatase activity. FEBS Lett 1992, 367:246-250.
    • (1992) FEBS Lett , vol.367 , pp. 246-250
    • Noda, M.1    Yasuda-Fukazawa, C.2    Moriishi, K.3    Kato, I.4    Okuda, T.5    Kurokawa, K.6    Takuwa, Y.7
  • 51
    • 0029995797 scopus 로고    scopus 로고
    • Rho-stimulated contractility drives the formation of stress fibers and focal adhesions
    • Chrzanowska-Wodnicka M, Burridge K: Rho-stimulated contractility drives the formation of stress fibers and focal adhesions. J Cell Biol 1996, 13:1403-1415.
    • (1996) J Cell Biol , vol.13 , pp. 1403-1415
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 52
    • 0029991890 scopus 로고    scopus 로고
    • Human myosin-1Xb, an unconventional myosin with a Chimerin-like rho/rac GTPase-activating protein domain in its tail
    • Wirth JA, Jensen KA, Post PL, Bement WM, Mooseker MS: Human myosin-1Xb, an unconventional myosin with a Chimerin-like rho/rac GTPase-activating protein domain in its tail. J Cell Sci 1996, 100:653-661. Describes structure of myosin-1Xb, which is abundant in cells of myeloid origin. The N-terminus of myosin-1Xb contains a chimerin-like, putative GAP domain of the Rho family.
    • (1996) J Cell Sci , vol.100 , pp. 653-661
    • Wirth, J.A.1    Jensen, K.A.2    Post, P.L.3    Bement, W.M.4    Mooseker, M.S.5
  • 53
    • 0028911031 scopus 로고
    • A novel type of myosin implicated in signalling by rho family GTPases
    • Reinhard J, Scheel AA, Diekmann D, Hall A, Ruppert C, Bähler M: A novel type of myosin implicated in signalling by rho family GTPases. EMBO J 1995, 14:697-704. The unconventional myosin, myosin-1Xb, acts as a Rho family GAP and is a potential regulatory component modulating the action of the Rho family members toward the actin cytoskeleton.
    • (1995) EMBO J , vol.14 , pp. 697-704
    • Reinhard, J.1    Scheel, A.A.2    Diekmann, D.3    Hall, A.4    Ruppert, C.5    Bähler, M.6
  • 55
    • 0028853289 scopus 로고
    • A dual functional signal mediator showing RhoGAP and phospholipase C-δ stimulating activities
    • Homma Y, Emori Y: A dual functional signal mediator showing RhoGAP and phospholipase C-δ stimulating activities. EMBO J 1995, 14:286-291.
    • (1995) EMBO J , vol.14 , pp. 286-291
    • Homma, Y.1    Emori, Y.2
  • 56
    • 0023157142 scopus 로고
    • Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate
    • Janmey PA, Stossel TP: Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate. Nature 1987, 325:362-364.
    • (1987) Nature , vol.325 , pp. 362-364
    • Janmey, P.A.1    Stossel, T.P.2
  • 57
    • 0026756594 scopus 로고
    • Requirement of phosphatidylinositol 4,5-bisphosphate for α-actinin function
    • Fukami K, Furuhashi K, Inagaki M, Endo T, Hatano S, Takenawa T: Requirement of phosphatidylinositol 4,5-bisphosphate for α-actinin function. Nature 1992, 3359:150-152.
    • (1992) Nature , vol.3359 , pp. 150-152
    • Fukami, K.1    Furuhashi, K.2    Inagaki, M.3    Endo, T.4    Hatano, S.5    Takenawa, T.6
  • 58
    • 0027358716 scopus 로고
    • Profilin as a potential mediator of membrane-cytoskeleton communication
    • Machesky LM, Pollard TD: Profilin as a potential mediator of membrane-cytoskeleton communication. Trends Cell Biol 1993, 3:381-385.
    • (1993) Trends Cell Biol , vol.3 , pp. 381-385
    • Machesky, L.M.1    Pollard, T.D.2
  • 59
    • 0027299745 scopus 로고
    • On the crawling of animal cells
    • Stossel TP: On the crawling of animal cells. Science 1993, 260:1086-1096.
    • (1993) Science , vol.260 , pp. 1086-1096
    • Stossel, T.P.1
  • 60
    • 0027059245 scopus 로고
    • Role of gelsolin interaction with actin in regulation and creation of actin nuclei in chemotactic peptide activated polymorphonuclear neutrophils
    • Deaton JD, Guerrero T, Howard TH: Role of gelsolin interaction with actin in regulation and creation of actin nuclei in chemotactic peptide activated polymorphonuclear neutrophils. Mol Biol Cell 1992, 3:1427-1435.
    • (1992) Mol Biol Cell , vol.3 , pp. 1427-1435
    • Deaton, J.D.1    Guerrero, T.2    Howard, T.H.3
  • 61
    • 0028914814 scopus 로고
    • Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin
    • Witke W, Sharpe AH, Hartwig JH, Azuma T, Stossel TP, Kwiatkowski DJ: Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin. Cell 1995, 81:41-51.
    • (1995) Cell , vol.81 , pp. 41-51
    • Witke, W.1    Sharpe, A.H.2    Hartwig, J.H.3    Azuma, T.4    Stossel, T.P.5    Kwiatkowski, D.J.6
  • 62
    • 0028897520 scopus 로고
    • Role of gelsolin in the formation and organization of tritonsoluble F-actin during myeloid differentiation of HL-60 cells
    • Watts RG: Role of gelsolin in the formation and organization of tritonsoluble F-actin during myeloid differentiation of HL-60 cells. Blood 1995, 85:2212-2221.
    • (1995) Blood , vol.85 , pp. 2212-2221
    • Watts, R.G.1
  • 63
    • 0028985349 scopus 로고
    • Dynamics of triton-insoluble and triton-soluble F-actin pools in calcium-activated human polymorphonuclear leukocytes: Evidence for regulation by gelsolin
    • Watts RG, Deaton JD, Howard TH: Dynamics of triton-insoluble and triton-soluble F-actin pools in calcium-activated human polymorphonuclear leukocytes: evidence for regulation by gelsolin. Cell Motil Cytoskeleton 1995, 30:136-145.
    • (1995) Cell Motil Cytoskeleton , vol.30 , pp. 136-145
    • Watts, R.G.1    Deaton, J.D.2    Howard, T.H.3
  • 64
    • 0028036684 scopus 로고
    • The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells
    • Chong L, Traynor-Kaplan A, Bokoch GM, Schwartz MA: The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells. Cell 1994, 79:507-513.
    • (1994) Cell , vol.79 , pp. 507-513
    • Chong, L.1    Traynor-Kaplan, A.2    Bokoch, G.M.3    Schwartz, M.A.4
  • 65
    • 0030001638 scopus 로고    scopus 로고
    • Physical association of the small GTPase Rho with a 68-kDa phosphatidylinositol 4-phosphate 5-kinase in Swiss 3T3 cells
    • Ren X, Bokoch GM, Traynor-Kaplan A, Jenkins GH, Anderson RA, Schwartz MA: Physical association of the small GTPase Rho with a 68-kDa phosphatidylinositol 4-phosphate 5-kinase in Swiss 3T3 cells. Mol Biol Cell 1996, 7:435-442.
    • (1996) Mol Biol Cell , vol.7 , pp. 435-442
    • Ren, X.1    Bokoch, G.M.2    Traynor-Kaplan, A.3    Jenkins, G.H.4    Anderson, R.A.5    Schwartz, M.A.6
  • 66
    • 0029023942 scopus 로고
    • Rho family GTPases bind to phosphoinositide kinases
    • Tolias K, Cantley LC, Carpenter CL: Rho family GTPases bind to phosphoinositide kinases. J Biol Chem 1995, 270:17656-17659.
    • (1995) J Biol Chem , vol.270 , pp. 17656-17659
    • Tolias, K.1    Cantley, L.C.2    Carpenter, C.L.3
  • 67
    • 0029117595 scopus 로고
    • Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets
    • 2 synthesis through stimulation of P15-kinase activity and promotes uncapping of actin filaments. A causal signaling pathway from the receptor through Rac to actin is proposed.
    • (1995) Cell , vol.82 , pp. 643-653
    • Hartwig, J.H.1    Bokoch, G.M.2    Carpenter, C.3    Janmey, P.4    Taylor, L.5    Stossel, T.P.6
  • 69
    • 0028338545 scopus 로고
    • Activation of phosphoinositide 3-kinase activity by CDC42Hs binding to p85
    • Zheng Y, Bagrodia S, Cerione RA: Activation of phosphoinositide 3-kinase activity by CDC42Hs binding to p85. J Biol Chem 1994, 269:18727-18730.
    • (1994) J Biol Chem , vol.269 , pp. 18727-18730
    • Zheng, Y.1    Bagrodia, S.2    Cerione, R.A.3
  • 70
    • 0027374497 scopus 로고
    • Activation of platelet phosphatidylinositide 3-kinase requires the small GTP-binding protein Rho
    • Zhang J, King WG, Dillon S, Hall A, Feig L, Rittenhouse SE: Activation of platelet phosphatidylinositide 3-kinase requires the small GTP-binding protein Rho. J Biol Chem 1993, 268:22251-22254.
    • (1993) J Biol Chem , vol.268 , pp. 22251-22254
    • Zhang, J.1    King, W.G.2    Dillon, S.3    Hall, A.4    Feig, L.5    Rittenhouse, S.E.6
  • 72
    • 0028837170 scopus 로고
    • Activation of the small GTP-binding proteins Rho and Rac by growth factor receptors
    • Nobes CO, Hawkins P, Stephens L, Hall A: Activation of the small GTP-binding proteins Rho and Rac by growth factor receptors. J Cell Sci 1995, 108:225-233.
    • (1995) J Cell Sci , vol.108 , pp. 225-233
    • Nobes, C.O.1    Hawkins, P.2    Stephens, L.3    Hall, A.4
  • 73
    • 0027372389 scopus 로고
    • Neutrophil phospholipase D is activated by a membrane-associated Rho family small molecular weight GTP-binding protein
    • Bowman EP, Uhlinger DJ, Lambeth JD: Neutrophil phospholipase D is activated by a membrane-associated Rho family small molecular weight GTP-binding protein. J Biol Chem 1993, 268:21509-21512.
    • (1993) J Biol Chem , vol.268 , pp. 21509-21512
    • Bowman, E.P.1    Uhlinger, D.J.2    Lambeth, J.D.3
  • 74
    • 0027999909 scopus 로고
    • Activation of rat liver phospholipase D by the small GTP-bindlng protein RhoA
    • Malcolm KC, Ross AH, Qiu RG, Symons M, Exton JH: Activation of rat liver phospholipase D by the small GTP-bindlng protein RhoA. J Biol Chem 1994, 269:25951-25954.
    • (1994) J Biol Chem , vol.269 , pp. 25951-25954
    • Malcolm, K.C.1    Ross, A.H.2    Qiu, R.G.3    Symons, M.4    Exton, J.H.5
  • 75
    • 0029020350 scopus 로고
    • Resolved phospholipase D activity is modulated by cytosolic factors other than Arf
    • Singer WD, Brown HA, Bokoch GM, Sternweis PC: Resolved phospholipase D activity is modulated by cytosolic factors other than Arf. J Biol Chem 1995, 270:14944-14950.
    • (1995) J Biol Chem , vol.270 , pp. 14944-14950
    • Singer, W.D.1    Brown, H.A.2    Bokoch, G.M.3    Sternweis, P.C.4
  • 77
    • 0027756153 scopus 로고
    • Activation of actin polymerization by phosphatidic acid derived from phosphatidylcholine in IIC9 fibroblasts
    • Ha K, Exton JH: Activation of actin polymerization by phosphatidic acid derived from phosphatidylcholine in IIC9 fibroblasts. J Cell Biol 1993, 123:1789-1796.
    • (1993) J Cell Biol , vol.123 , pp. 1789-1796
    • Ha, K.1    Exton, J.H.2
  • 79
    • 0028169005 scopus 로고
    • Interaction of Rac with p67phox and regulation of phagocytic NADPH oxidase activity
    • Diekmann D, Abo A, Johnston C, Segal AW, Hall A: Interaction of Rac with p67phox and regulation of phagocytic NADPH oxidase activity. Science 1994, 265:531-533.
    • (1994) Science , vol.265 , pp. 531-533
    • Diekmann, D.1    Abo, A.2    Johnston, C.3    Segal, A.W.4    Hall, A.5
  • 82
    • 0028820587 scopus 로고
    • Rho family GTPases regulate p38 mitogen-activated protein kinase through the downstream mediator Pak1
    • Zhang S, Han J, Sells MA, Chernoff J, Knaus UG, Ulevitch RJ, Bokoch GM: Rho family GTPases regulate p38 mitogen-activated protein kinase through the downstream mediator Pak1. J Biol Chem 1995, 270:23934-23936.
    • (1995) J Biol Chem , vol.270 , pp. 23934-23936
    • Zhang, S.1    Han, J.2    Sells, M.A.3    Chernoff, J.4    Knaus, U.G.5    Ulevitch, R.J.6    Bokoch, G.M.7
  • 83
    • 0028875683 scopus 로고
    • Cdc42 and PAK-mediated signaling leads to Jun kinase and p38 mitogen-activated protein kinase activation
    • Bagrodia S, Dérijard B, Davis RJ, Cerione RA: Cdc42 and PAK-mediated signaling leads to Jun kinase and p38 mitogen-activated protein kinase activation. J Biol Chem 1995, 270:27995-27998.
    • (1995) J Biol Chem , vol.270 , pp. 27995-27998
    • Bagrodia, S.1    Dérijard, B.2    Davis, R.J.3    Cerione, R.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.