메뉴 건너뛰기




Volumn 289, Issue 4 58-4, 2005, Pages

PAK1 induces podosome formation in A7r5 vascular smooth muscle cells in a PAK-interacting exchange factor-dependent manner

Author keywords

Actin cytoskeleton; p21 activated kinase

Indexed keywords

ACTIN; ACTIN RELATED PROTEIN 2; ACTIN RELATED PROTEIN 3; ALPHA ACTININ; CONTACTIN; F ACTIN; G PROTEIN COUPLED RECEPTOR KINASE; P21 ACTIVATED KINASE; P21 ACTIVATED KINASE 1; PAK INTERACTING EXCHANGE FACTOR; PHORBOL ESTER; PROTEIN CDC42; PROTEIN KINASE; RAC PROTEIN; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; UNCLASSIFIED DRUG; VINCULIN;

EID: 25444450611     PISSN: 03636143     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpcell.00095.2005     Document Type: Article
Times cited : (64)

References (57)
  • 1
    • 0034697303 scopus 로고    scopus 로고
    • Regulation of microfilament reorganization and invasiveness of breast cancer cells by kinase dead p21-activated kinase-1
    • Adam L, Vadlamudi R, Mandal M, Chernoff J, and Kumar R. Regulation of microfilament reorganization and invasiveness of breast cancer cells by kinase dead p21-activated kinase-1. J Biol Chem 275: 12041-12050, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 12041-12050
    • Adam, L.1    Vadlamudi, R.2    Mandal, M.3    Chernoff, J.4    Kumar, R.5
  • 3
    • 0033529562 scopus 로고    scopus 로고
    • A tyrosine-phosphorylated protein that binds to an important regulatory region on the Cool family of p21-activated kinase-binding proteins
    • Bagrodia S, Bailey D, Lenard Z, Hart M, Guan JL, Premont RT, Taylor SJ, and Cerione RA. A tyrosine-phosphorylated protein that binds to an important regulatory region on the Cool family of p21-activated kinase-binding proteins. J Biol Chem 274: 22393-22400, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 22393-22400
    • Bagrodia, S.1    Bailey, D.2    Lenard, Z.3    Hart, M.4    Guan, J.L.5    Premont, R.T.6    Taylor, S.J.7    Cerione, R.A.8
  • 5
    • 11844280881 scopus 로고    scopus 로고
    • The Cool-2/α-Pix protein mediates a Cdc42-Rac signaling cascade
    • Baird D, Feng Q, and Cerione RA. The Cool-2/α-Pix protein mediates a Cdc42-Rac signaling cascade. Curr Biol 15: 1-10, 2005.
    • (2005) Curr Biol , vol.15 , pp. 1-10
    • Baird, D.1    Feng, Q.2    Cerione, R.A.3
  • 6
    • 0038554077 scopus 로고    scopus 로고
    • Biology of the p21 -activated kinases
    • Bokoch GM. Biology of the p21 -activated kinases. Annu Rev Biochem 72: 743-781, 2003.
    • (2003) Annu Rev Biochem , vol.72 , pp. 743-781
    • Bokoch, G.M.1
  • 7
    • 0035999990 scopus 로고    scopus 로고
    • Paxillin-dependent paxillin kinase linker and p21-activated kinase localization to focal adhesions involves a multistep activation pathway
    • Brown MC, West KA, and Turner CE. Paxillin-dependent paxillin kinase linker and p21-activated kinase localization to focal adhesions involves a multistep activation pathway. Mol Biol Cell 13: 1550-1565, 2002.
    • (2002) Mol Biol Cell , vol.13 , pp. 1550-1565
    • Brown, M.C.1    West, K.A.2    Turner, C.E.3
  • 8
    • 1642421365 scopus 로고    scopus 로고
    • Actin cytoskeleton remodelling via local inhibition of contractility at discrete microdomains
    • Burgstaller G and Gimona M. Actin cytoskeleton remodelling via local inhibition of contractility at discrete microdomains. J Cell Sci 117: 223-231, 2004.
    • (2004) J Cell Sci , vol.117 , pp. 223-231
    • Burgstaller, G.1    Gimona, M.2
  • 9
    • 0035883040 scopus 로고    scopus 로고
    • Configuration of human dendritic cell cytoskeleton by Rho GTPases, the WAS protein, and differentiation
    • Burns S, Thrasher AJ, Blundell MP, Machesky L, and Jones GE. Configuration of human dendritic cell cytoskeleton by Rho GTPases, the WAS protein, and differentiation. Blood 98: 1142-1149, 2001.
    • (2001) Blood , vol.98 , pp. 1142-1149
    • Burns, S.1    Thrasher, A.J.2    Blundell, M.P.3    Machesky, L.4    Jones, G.E.5
  • 10
    • 0035943704 scopus 로고    scopus 로고
    • Cytoskeletal changes regulated by the PAK4 serine/threonine kinase are mediated by LIM kinase 1 and cofilin
    • Dan C, Kelly A, Bernard O, and Minden A. Cytoskeletal changes regulated by the PAK4 serine/threonine kinase are mediated by LIM kinase 1 and cofilin. J Biol Chem 276: 32115-32121, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 32115-32121
    • Dan, C.1    Kelly, A.2    Bernard, O.3    Minden, A.4
  • 11
    • 0032472918 scopus 로고    scopus 로고
    • Membrane targeting of p21-activated kinase 1 (PAK1) induces neurite outgrowth from PC12 cells
    • Daniels RH, Hall PS, and Bokoch GM. Membrane targeting of p21-activated kinase 1 (PAK1) induces neurite outgrowth from PC12 cells. EMBO J 17: 754-764, 1998.
    • (1998) EMBO J , vol.17 , pp. 754-764
    • Daniels, R.H.1    Hall, P.S.2    Bokoch, G.M.3
  • 12
    • 0034811439 scopus 로고    scopus 로고
    • p21-activated kinase 1 participates in tracheal smooth muscle cell migration by signaling to p38 MAPK
    • Dechert MA, Holder JM, and Gerthoffer WT. p21-Activated kinase 1 participates in tracheal smooth muscle cell migration by signaling to p38 MAPK. Am J Physiol Cell Physiol 281: C123-C132, 2001.
    • (2001) Am J Physiol Cell Physiol , vol.281
    • Dechert, M.A.1    Holder, J.M.2    Gerthoffer, W.T.3
  • 13
    • 0037329229 scopus 로고    scopus 로고
    • Podosomes display actin turnover and dynamic self-organization in osteoclasts expressing actin-green fluorescent protein
    • Destaing O, Saltel F, Géminard JC, Jurdic P, and Bard F. Podosomes display actin turnover and dynamic self-organization in osteoclasts expressing actin-green fluorescent protein. Mol Biol Cell 14: 407-416, 2003.
    • (2003) Mol Biol Cell , vol.14 , pp. 407-416
    • Destaing, O.1    Saltel, F.2    Géminard, J.C.3    Jurdic, P.4    Bard, F.5
  • 14
    • 0033194037 scopus 로고    scopus 로고
    • Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics
    • Edwards DC, Sanders LC, Bokoch GM, and Gill GN. Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Nat Cell Biol 1: 253-259, 1999.
    • (1999) Nat Cell Biol , vol.1 , pp. 253-259
    • Edwards, D.C.1    Sanders, L.C.2    Bokoch, G.M.3    Gill, G.N.4
  • 15
    • 4644343782 scopus 로고    scopus 로고
    • Novel regulatory mechanisms for the Dbl family guanine nucleotide exchange factor Cool-2/α-Pix
    • Feng Q, Baird D, and Cerione RA. Novel regulatory mechanisms for the Dbl family guanine nucleotide exchange factor Cool-2/α-Pix. EMBO J 23: 3492-3504, 2004.
    • (2004) EMBO J , vol.23 , pp. 3492-3504
    • Feng, Q.1    Baird, D.2    Cerione, R.A.3
  • 17
    • 0032561355 scopus 로고    scopus 로고
    • Differential effects of PAK1-activating mutations reveal activity-dependent and -independent effects on cytoskeletal regulation
    • Frost JA, Khokhlatchev A, Stippec S, White MA, and Cobb MH. Differential effects of PAK1-activating mutations reveal activity-dependent and -independent effects on cytoskeletal regulation. J Biol Chem 273: 28191-28198, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 28191-28198
    • Frost, J.A.1    Khokhlatchev, A.2    Stippec, S.3    White, M.A.4    Cobb, M.H.5
  • 18
    • 0034441863 scopus 로고    scopus 로고
    • Remodeling of the actin cytoskeleton in the contracting A7r5 smooth muscle cell
    • Fultz ME, Li C, Geng W, and Wright GL. Remodeling of the actin cytoskeleton in the contracting A7r5 smooth muscle cell. J Muscle Res Cell Motil 21: 775-787, 2000.
    • (2000) J Muscle Res Cell Motil , vol.21 , pp. 775-787
    • Fultz, M.E.1    Li, C.2    Geng, W.3    Wright, G.L.4
  • 19
    • 0038308424 scopus 로고    scopus 로고
    • Calponin repeats regulate actin filament stability and formation of podosomes in smooth muscle cells
    • Gimona M, Kaverina I, Resch GP, Vignal E, and Burgstaller G. Calponin repeats regulate actin filament stability and formation of podosomes in smooth muscle cells. Mol Biol Cell 14: 2482-2491, 2003.
    • (2003) Mol Biol Cell , vol.14 , pp. 2482-2491
    • Gimona, M.1    Kaverina, I.2    Resch, G.P.3    Vignal, E.4    Burgstaller, G.5
  • 21
    • 0036033308 scopus 로고    scopus 로고
    • Conventional protein kinase C mediates phorbol-dibutyrate-induced cytoskeletal remodeling in A7r5 smooth muscle cells
    • Hai CM, Hahne P, Harrington EO, and Gimona M. Conventional protein kinase C mediates phorbol-dibutyrate-induced cytoskeletal remodeling in A7r5 smooth muscle cells. Exp Cell Res 280: 64-74, 2002.
    • (2002) Exp Cell Res , vol.280 , pp. 64-74
    • Hai, C.M.1    Hahne, P.2    Harrington, E.O.3    Gimona, M.4
  • 22
    • 0035937140 scopus 로고    scopus 로고
    • Interaction of paxillin with p21-activated kinase (PAK): Association of paxillin α with the kinase-inactive and the Cdc42-activated-forms of PAK3
    • Hashimoto S, Tsubouchi A, Mazaki Y, and Sabe H. Interaction of paxillin with p21-activated kinase (PAK): association of paxillin α with the kinase-inactive and the Cdc42-activated-forms of PAK3. J Biol Chem 276: 6037-6045, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 6037-6045
    • Hashimoto, S.1    Tsubouchi, A.2    Mazaki, Y.3    Sabe, H.4
  • 23
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: Structural basis for regulation
    • Johnson LN, Noble ME, and Owen DJ. Active and inactive protein kinases: structural basis for regulation. Cell 85: 149-158, 1996.
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.2    Owen, D.J.3
  • 24
    • 0348143126 scopus 로고    scopus 로고
    • Podosome formation in cultured A7r5 vascular smooth muscle cells requires Arp2/3-dependent de-novo actin polymerization at discrete microdomains
    • Kaverina I, Stradal TE, and Gimona M. Podosome formation in cultured A7r5 vascular smooth muscle cells requires Arp2/3-dependent de-novo actin polymerization at discrete microdomains. J Cell Sci 116: 4915-4924, 2003.
    • (2003) J Cell Sci , vol.116 , pp. 4915-4924
    • Kaverina, I.1    Stradal, T.E.2    Gimona, M.3
  • 25
    • 0017104962 scopus 로고
    • Characterization of two putative smooth muscle cell lines from rat thoracic aorta
    • Kimes BW and Brandt BL. Characterization of two putative smooth muscle cell lines from rat thoracic aorta. Exp Cell Res 98: 349-366, 1976.
    • (1976) Exp Cell Res , vol.98 , pp. 349-366
    • Kimes, B.W.1    Brandt, B.L.2
  • 26
    • 0033571033 scopus 로고    scopus 로고
    • A role for p21-activated kinase in endothelial cell migration
    • Kiosses WB, Daniels RH, Otey C, Bokoch GM, and Schwartz MA. A role for p21-activated kinase in endothelial cell migration. J Cell Biol 147: 831-844, 1999.
    • (1999) J Cell Biol , vol.147 , pp. 831-844
    • Kiosses, W.B.1    Daniels, R.H.2    Otey, C.3    Bokoch, G.M.4    Ma, S.5
  • 27
    • 0034604338 scopus 로고    scopus 로고
    • Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch
    • Lei M, Lu W, Meng W, Parrini MC, Eck MJ, Mayer BJ, and Harrison SC. Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch. Cell 102: 387-397, 2000.
    • (2000) Cell , vol.102 , pp. 387-397
    • Lei, M.1    Lu, W.2    Meng, W.3    Parrini, M.C.4    Eck, M.J.5    Mayer, B.J.6    Harrison, S.C.7
  • 28
    • 0038433238 scopus 로고    scopus 로고
    • Podosomes: Adhesion hot-spots of invasive cells
    • Linder S and Aepfelbacher M. Podosomes: adhesion hot-spots of invasive cells. Trends Cell Biol 13: 376-385, 2003.
    • (2003) Trends Cell Biol , vol.13 , pp. 376-385
    • Linder, S.1    Aepfelbacher, M.2
  • 29
    • 0034234559 scopus 로고    scopus 로고
    • The polarization defect of Wiskott-Aldrich syndrome macrophages is linked to dislocalization of the Arp2/3 complex
    • Linder S, Higgs H, Hüfner K, Schwarz K, Pannicke U, and Aepfelbacher M. The polarization defect of Wiskott-Aldrich syndrome macrophages is linked to dislocalization of the Arp2/3 complex. J Immunol 165: 221-225, 2000.
    • (2000) J Immunol , vol.165 , pp. 221-225
    • Linder, S.1    Higgs, H.2    Hüfner, K.3    Schwarz, K.4    Pannicke, U.5    Aepfelbacher, M.6
  • 30
    • 0033578374 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein regulates podosomes in primary human macrophages
    • Linder S, Nelson D, Weiss M, and Aepfelbacher M. Wiskott-Aldrich syndrome protein regulates podosomes in primary human macrophages. Proc Natl Acad Sci USA 96: 9648-9653, 1999.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9648-9653
    • Linder, S.1    Nelson, D.2    Weiss, M.3    Aepfelbacher, M.4
  • 31
    • 1942518365 scopus 로고    scopus 로고
    • GIT1 activates p21-activated kinase through a mechanism independent of p21 binding
    • Loo TH, Ng YW, Lim L, and Manser E. GIT1 activates p21-activated kinase through a mechanism independent of p21 binding. Mol Cell Biol 24: 3849-3859, 2004.
    • (2004) Mol Cell Biol , vol.24 , pp. 3849-3859
    • Loo, T.H.1    Ng, Y.W.2    Lim, L.3    Manser, E.4
  • 32
    • 0031036626 scopus 로고    scopus 로고
    • Expression of constitutively active α-PAK reveals effects of the kinase on actin and focal complexes
    • Manser E, Huang HY, Loo TH, Chen XQ, Dong JM, Leung T, and Lim L. Expression of constitutively active α-PAK reveals effects of the kinase on actin and focal complexes. Mol Cell Biol 17: 1129-1143, 1997.
    • (1997) Mol Cell Biol , vol.17 , pp. 1129-1143
    • Manser, E.1    Huang, H.Y.2    Loo, T.H.3    Chen, X.Q.4    Dong, J.M.5    Leung, T.6    Lim, L.7
  • 34
    • 0036468250 scopus 로고    scopus 로고
    • Essential role of neural Wiskott-Aldrich syndrome protein in podosome formation and degradation of extracellular matrix in src-transformed fibroblasts
    • Mizutani K, Miki H, He H, Maruta H, and Takenawa T. Essential role of neural Wiskott-Aldrich syndrome protein in podosome formation and degradation of extracellular matrix in src-transformed fibroblasts. Cancer Res 62: 669-674, 2002.
    • (2002) Cancer Res , vol.62 , pp. 669-674
    • Mizutani, K.1    Miki, H.2    He, H.3    Maruta, H.4    Takenawa, T.5
  • 35
    • 0032479975 scopus 로고    scopus 로고
    • PAK promotes morphological changes by acting upstream of Rac
    • Obermeier A, Ahmed S, Manser E, Yen SC, Hall C, and Lim L. PAK promotes morphological changes by acting upstream of Rac. EMBO J 17: 4328-4339, 1998.
    • (1998) EMBO J , vol.17 , pp. 4328-4339
    • Obermeier, A.1    Ahmed, S.2    Manser, E.3    Yen, S.C.4    Hall, C.5    Lim, L.6
  • 37
    • 0035921432 scopus 로고    scopus 로고
    • Abp1p and cortactin, new "hand-holds" for actin
    • Olazabal IM and Machesky LM. Abp1p and cortactin, new "hand-holds" for actin. J Cell Biol 154: 679-682, 2001.
    • (2001) J Cell Biol , vol.154 , pp. 679-682
    • Olazabal, I.M.1    Machesky, L.M.2
  • 38
    • 0034094811 scopus 로고    scopus 로고
    • Rho and Rac exert antagonistic functions on spreading of macrophage-derived multinucleated cells and are not required for actin fiber formation
    • Ory S, Munari-Silem Y, Fort P, and Jurdic P. Rho and Rac exert antagonistic functions on spreading of macrophage-derived multinucleated cells and are not required for actin fiber formation. J Cell Sci 113: 1177-1188, 2000.
    • (2000) J Cell Sci , vol.113 , pp. 1177-1188
    • Ory, S.1    Munari-Silem, Y.2    Fort, P.3    Jurdic, P.4
  • 41
    • 0034698059 scopus 로고    scopus 로고
    • The GIT family of ADP-ribosylation factor GTPase-activating proteins: Functional diversity of GIT2 through alternative splicing
    • Premont RT, Claing A, Vitale N, Perry SJ, and Lefkowitz RJ. The GIT family of ADP-ribosylation factor GTPase-activating proteins: functional diversity of GIT2 through alternative splicing. J Biol Chem 275: 22373-22380, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 22373-22380
    • Premont, R.T.1    Claing, A.2    Vitale, N.3    Perry, S.J.4    Lefkowitz, R.J.5
  • 42
    • 0033605738 scopus 로고    scopus 로고
    • Inhibition of myosin light chain kinase by p21-activated kinase
    • Sanders LC, Matsumura F, Bokoch GM, and de Lanerolle P. Inhibition of myosin light chain kinase by p21-activated kinase. Science 283: 2083-2085, 1999.
    • (1999) Science , vol.283 , pp. 2083-2085
    • Sanders, L.C.1    Matsumura, F.2    Bokoch, G.M.3    De Lanerolle, P.4
  • 43
    • 0033577902 scopus 로고    scopus 로고
    • p21-activated kinase 1 (Pak1) regulates cell motility in mammalian fibroblasts
    • Sells MA, Boyd JT, and Chernoff J. p21-Activated kinase 1 (Pak1) regulates cell motility in mammalian fibroblasts. J Cell Biol 145: 837-849, 1999.
    • (1999) J Cell Biol , vol.145 , pp. 837-849
    • Sells, M.A.1    Boyd, J.T.2    Chernoff, J.3
  • 45
    • 0024514444 scopus 로고
    • Comparison of the regional distribution of calspectin (non-erythroid spectrin or fodrin), α-actinin, vinculin nonerythroid protein 4.1, and calpactin in normal and avian sarcoma virus- or Rous sarcoma virus-induced transformed cells
    • Sobue K, Kanda K, Miyamoto I, Iida K, Yahara I, Hirai R, and Hiragun A. Comparison of the regional distribution of calspectin (non-erythroid spectrin or fodrin), α-actinin, vinculin nonerythroid protein 4.1, and calpactin in normal and avian sarcoma virus- or Rous sarcoma virus-induced transformed cells. Exp Cell Res 181: 256-262, 1989.
    • (1989) Exp Cell Res , vol.181 , pp. 256-262
    • Sobue, K.1    Kanda, K.2    Miyamoto, I.3    Iida, K.4    Yahara, I.5    Hirai, R.6    Hiragun, A.7
  • 46
    • 2542451854 scopus 로고    scopus 로고
    • Constitutive p21-activated kinase (PAK) activation in breast cancer cells as a result of mislocalization of PAK to focal adhesions
    • Stofega MR, Sanders LC, Gardiner EM, and Bokoch GM. Constitutive p21-activated kinase (PAK) activation in breast cancer cells as a result of mislocalization of PAK to focal adhesions. Mol Biol Cell 15: 2965-2977, 2004.
    • (2004) Mol Biol Cell , vol.15 , pp. 2965-2977
    • Stofega, M.R.1    Sanders, L.C.2    Gardiner, E.M.3    Bokoch, G.M.4
  • 47
    • 0027516325 scopus 로고
    • Morphological and biochemical analyses of contractile proteins (actin, myosin, caldesmon and tropomyosin) in normal and transformed cells
    • Tanaka J, Watanabe T, Nakamura N, and Sobue K. Morphological and biochemical analyses of contractile proteins (actin, myosin, caldesmon and tropomyosin) in normal and transformed cells. J Cell Sci 104: 595-606, 1993.
    • (1993) J Cell Sci , vol.104 , pp. 595-606
    • Tanaka, J.1    Watanabe, T.2    Nakamura, N.3    Sobue, K.4
  • 49
  • 50
    • 0037114750 scopus 로고    scopus 로고
    • Cdc42/Rac1-dependent activation of the p21-activated kinase (PAK) regulates human platelet lamellipodia spreading: Implication of the cortical-actin binding protein cortactin
    • Vidal C, Geny B, Melle J, Jandrot-Perrus M, and Fontenay-Roupie M. Cdc42/Rac1-dependent activation of the p21-activated kinase (PAK) regulates human platelet lamellipodia spreading: implication of the cortical-actin binding protein cortactin. Blood 100: 4462-4469, 2002.
    • (2002) Blood , vol.100 , pp. 4462-4469
    • Vidal, C.1    Geny, B.2    Melle, J.3    Jandrot-Perrus, M.4    Fontenay-Roupie, M.5
  • 52
    • 0031696485 scopus 로고    scopus 로고
    • Translocation of cortactin to the cell periphery is mediated by the small GTPase Rac1
    • Weed SA, Du Y, and Parsons JT. Translocation of cortactin to the cell periphery is mediated by the small GTPase Rac1. J Cell Sci 111: 2433-2443, 1998.
    • (1998) J Cell Sci , vol.111 , pp. 2433-2443
    • Weed, S.A.1    Du, Y.2    Parsons, J.T.3
  • 53
    • 0035475450 scopus 로고    scopus 로고
    • Cortactin: Coupling membrane dynamics to cortical actin assembly
    • Weed SA and Parsons JT. Cortactin: coupling membrane dynamics to cortical actin assembly. Oncogene 20: 6418-6434, 2001.
    • (2001) Oncogene , vol.20 , pp. 6418-6434
    • Weed, S.A.1    Parsons, J.T.2
  • 54
    • 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 MD, DePace AH, Verma S, Iwamatsu A, and Mitchison TJ. 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.
    • (1997) J Cell Biol , vol.138 , pp. 375-384
    • Welch, M.D.1    DePace, A.H.2    Verma, S.3    Iwamatsu, A.4    Mitchison, T.J.5
  • 56
    • 0031948850 scopus 로고    scopus 로고
    • A conserved negative regulatory region in αPAK: Inhibition of PAK kinases reveals their morphological roles downstream of Cdc42 and Racl
    • Zhao ZS, Manser E, Chen XQ, Chong C, Leung T, and Lim L. A conserved negative regulatory region in αPAK: inhibition of PAK kinases reveals their morphological roles downstream of Cdc42 and Racl. Mol Cell Biol 18: 2153-2163, 1998.
    • (1998) Mol Cell Biol , vol.18 , pp. 2153-2163
    • Zhao, Z.S.1    Manser, E.2    Chen, X.Q.3    Chong, C.4    Leung, T.5    Lim, L.6
  • 57
    • 0033843129 scopus 로고    scopus 로고
    • Coupling of PAK-interacting exchange factor PIX to GIT1 promotes focal complex disassembly
    • Zhao ZS, Manser E, Loo TH, and Lim L. Coupling of PAK-interacting exchange factor PIX to GIT1 promotes focal complex disassembly. Mol Cell Biol 20: 6354-6363, 2000.
    • (2000) Mol Cell Biol , vol.20 , pp. 6354-6363
    • Zhao, Z.S.1    Manser, E.2    Loo, T.H.3    Lim, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.