메뉴 건너뛰기




Volumn 193, Issue 7, 2011, Pages 1289-1303

Pak1 regulates focal adhesion strength, myosin IIA distribution, and actin dynamics to optimize cell migration

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; F ACTIN; MYOSIN IIA; P21 ACTIVATED KINASE 1; PROTEIN CDC42; RAC PROTEIN;

EID: 79960228959     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201010059     Document Type: Article
Times cited : (81)

References (51)
  • 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., R. Vadlamudi, M. Mandal, J. Chernoff, and R. Kumar. 2000. Regulation of microfilament reorganization and invasiveness of breast cancer cells by kinase dead p21-activated kinase-1. J. Biol. Chem. 275:12041-12050.
    • (2000) J. Biol. Chem. , vol.275 , pp. 12041-12050
    • Adam, L.1    Vadlamudi, R.2    Mandal, M.3    Chernoff, J.4    Kumar, R.5
  • 2
    • 0037282555 scopus 로고    scopus 로고
    • A high-speed multispectral spinning-disk confocal microscope system for fluorescent speckle microscopy of living cells
    • Adams, M.C., W.C. Salmon, S.L. Gupton, C.S. Cohan, T. Wittmann, N. Prigozhina, and C.M. Waterman-Storer. 2003. A high-speed multispectral spinning-disk confocal microscope system for fluorescent speckle microscopy of living cells. Methods. 29:29-41.
    • (2003) Methods , vol.29 , pp. 29-41
    • Adams, M.C.1    Salmon, W.C.2    Gupton, S.L.3    Cohan, C.S.4    Wittmann, T.5    Prigozhina, N.6    Waterman-Storer, C.M.7
  • 3
    • 7944222012 scopus 로고    scopus 로고
    • Signal analysis of total internal reflection fluorescent speckle microscopy (TIR-FSM) and wide-field epi-fluorescence FSM of the actin cytoskeleton and focal adhesions in living cells
    • Adams, M.C., A. Matov, D. Yarar, S.L. Gupton, G. Danuser, and C.M. Waterman-Storer. 2004. Signal analysis of total internal reflection fluorescent speckle microscopy (TIR-FSM) and wide-field epi-fluorescence FSM of the actin cytoskeleton and focal adhesions in living cells. J. Microsc. 216:138-152.
    • (2004) J. Microsc. , vol.216 , pp. 138-152
    • Adams, M.C.1    Matov, A.2    Yarar, D.3    Gupton, S.L.4    Danuser, G.5    Waterman-Storer, C.M.6
  • 4
    • 0034671927 scopus 로고    scopus 로고
    • Vascular endothelial growth factor up-regulation via p21-activated kinase-1 signaling regulates heregulin-beta1-mediated angiogenesis
    • Bagheri-Yarmand, R., R.K. Vadlamudi, R.A. Wang, J. Mendelsohn, and R. Kumar. 2000. Vascular endothelial growth factor up-regulation via p21-activated kinase-1 signaling regulates heregulin-beta1-mediated angiogenesis. J. Biol. Chem. 275:39451-39457.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39451-39457
    • Bagheri-Yarmand, R.1    Vadlamudi, R.K.2    Wang, R.A.3    Mendelsohn, J.4    Kumar, R.5
  • 5
    • 0038554077 scopus 로고    scopus 로고
    • Biology of the p21-activated kinases
    • Bokoch, G.M. 2003. Biology of the p21-activated kinases. Annu. Rev. Biochem. 72:743-781.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 743-781
    • Bokoch, G.M.1
  • 6
    • 3042847368 scopus 로고    scopus 로고
    • Rac-induced increase of phosphorylation of myosin regulatory light chain in HeLa cells
    • Brzeska, H., J. Szczepanowska, F. Matsumura, and E.D. Korn. 2004. Rac-induced increase of phosphorylation of myosin regulatory light chain in HeLa cells. Cell Motil. Cytoskeleton. 58:186-199.
    • (2004) Cell Motil. Cytoskeleton. , vol.58 , pp. 186-199
    • Brzeska, H.1    Szczepanowska, J.2    Matsumura, F.3    Korn, E.D.4
  • 9
    • 0032438538 scopus 로고    scopus 로고
    • Phosphorylation of non-muscle myosin II regulatory light chain by p21-activated kinase (gamma-PAK)
    • Chew, T.L., R.A. Masaracchia, Z.M. Goeckeler, and R.B. Wysolmerski. 1998. Phosphorylation of non-muscle myosin II regulatory light chain by p21-activated kinase (gamma-PAK). J. Muscle Res. Cell Motil. 19:839-854.
    • (1998) J. Muscle Res. Cell Motil. , vol.19 , pp. 839-854
    • Chew, T.L.1    Masaracchia, R.A.2    Goeckeler, Z.M.3    Wysolmerski, R.B.4
  • 10
    • 51049104617 scopus 로고    scopus 로고
    • Actin and alpha-actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motor-independent manner
    • Choi, C.K., M. Vicente-Manzanares, J. Zareno, L.A. Whitmore, A. Mogilner, and A.R. Horwitz. 2008. Actin and alpha-actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motor-independent manner. Nat. Cell Biol. 10:1039-1050.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1039-1050
    • Choi, C.K.1    Vicente-Manzanares, M.2    Zareno, J.3    Whitmore, L.A.4    Mogilner, A.5    Horwitz, A.R.6
  • 11
    • 77649210771 scopus 로고    scopus 로고
    • Stochastic model of integrin-mediated signaling and adhesion dynamics at the leading edges of migrating cells
    • Cirit, M., M. Krajcovic, C.K. Choi, E.S. Welf, A.F. Horwitz, and J.M. Haugh. 2010. Stochastic model of integrin-mediated signaling and adhesion dynamics at the leading edges of migrating cells. PLOS Comput. Biol. 6:e1000688.
    • (2010) PLOS Comput. Biol. , vol.6
    • Cirit, M.1    Krajcovic, M.2    Choi, C.K.3    Welf, E.S.4    Horwitz, A.F.5    Haugh, J.M.6
  • 12
    • 0035152391 scopus 로고    scopus 로고
    • Integrin-mediated adhesion regulates cell polarity and membrane protrusion through the Rho family of GTPases
    • Cox, E.A., S.K. Sastry, and A. Huttenlocher. 2001. Integrin-mediated adhesion regulates cell polarity and membrane protrusion through the Rho family of GTPases. Mol. Biol. Cell. 12:265-277.
    • (2001) Mol. Biol. Cell. , vol.12 , pp. 265-277
    • Cox, E.A.1    Sastry, S.K.2    Huttenlocher, A.3
  • 13
    • 33745027397 scopus 로고    scopus 로고
    • Quantitative fluorescent speckle microscopy of cytoskeleton dynamics
    • Danuser, G., and C.M. Waterman-Storer. 2006. Quantitative fluorescent speckle microscopy of cytoskeleton dynamics. Annu. Rev. Biophys. Biomol. Struct. 35:361-387.
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 361-387
    • Danuser, G.1    Waterman-Storer, C.M.2
  • 15
    • 0034595381 scopus 로고    scopus 로고
    • Adhesion to the extracellular matrix regulates the coupling of the small GTPase Rac to its effector PAK
    • del Pozo, M.A., L.S. Price, N.B. Alderson, X.D. Ren, and M.A. Schwartz. 2000. Adhesion to the extracellular matrix regulates the coupling of the small GTPase Rac to its effector PAK. EMBO J. 19:2008-2014.
    • (2000) EMBO J. , vol.19 , pp. 2008-2014
    • del Pozo, M.A.1    Price, L.S.2    Alderson, N.B.3    Ren, X.D.4    Schwartz, M.A.5
  • 16
    • 0025886995 scopus 로고
    • Mathematical model for the effects of adhesion and mechanics on cell migration speed
    • DiMilla, P.A., K. Barbee, and D.A. Lauffenburger. 1991. Mathematical model for the effects of adhesion and mechanics on cell migration speed. Biophys. J. 60:15-37.
    • (1991) Biophys. J. , vol.60 , pp. 15-37
    • DiMilla, P.A.1    Barbee, K.2    Lauffenburger, D.A.3
  • 18
    • 0033194037 scopus 로고    scopus 로고
    • Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics
    • Edwards, D.C., L.C. Sanders, G.M. Bokoch, and G.N. Gill. 1999. Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Nat. Cell Biol. 1:253-259.
    • (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
  • 19
    • 0037175402 scopus 로고    scopus 로고
    • The relationship between force and focal complex development
    • Galbraith, C.G., K.M. Yamada, and M.P. Sheetz. 2002. The relationship between force and focal complex development. J. Cell Biol. 159:695-705.
    • (2002) J. Cell Biol. , vol.159 , pp. 695-705
    • Galbraith, C.G.1    Yamada, K.M.2    Sheetz, M.P.3
  • 22
    • 33745245989 scopus 로고    scopus 로고
    • Spatiotemporal feedback between actomyosin and focal-adhesion systems optimizes rapid cell migration
    • Gupton, S.L., and C.M. Waterman-Storer. 2006. Spatiotemporal feedback between actomyosin and focal-adhesion systems optimizes rapid cell migration. Cell. 125:1361-1374.
    • (2006) Cell , vol.125 , pp. 1361-1374
    • Gupton, S.L.1    Waterman-Storer, C.M.2
  • 24
    • 75649094184 scopus 로고    scopus 로고
    • Identification of MYO18A as a novel interacting partner of the PAK2/betaPIX/GIT1 complex and its potential function in modulating epithelial cell migration
    • Hsu, R.M., M.H. Tsai, Y.J. Hsieh, P.C. Lyu, and J.S. Yu. 2010. Identification of MYO18A as a novel interacting partner of the PAK2/betaPIX/GIT1 complex and its potential function in modulating epithelial cell migration. Mol. Biol. Cell. 21:287-301.
    • (2010) Mol. Biol. Cell. , vol.21 , pp. 287-301
    • Hsu, R.M.1    Tsai, M.H.2    Hsieh, Y.J.3    Lyu, P.C.4    Yu, J.S.5
  • 26
    • 0028998794 scopus 로고
    • Regulation of human leukocyte p21-activated kinases through G protein- coupled receptors
    • Knaus, U.G., S. Morris, H.J. Dong, J. Chernoff, and G.M. Bokoch. 1995. Regulation of human leukocyte p21-activated kinases through G protein- coupled receptors. Science. 269:221-223.
    • (1995) Science , vol.269 , pp. 221-223
    • Knaus, U.G.1    Morris, S.2    Dong, H.J.3    Chernoff, J.4    Bokoch, G.M.5
  • 28
    • 42049092972 scopus 로고    scopus 로고
    • Regulation of actin assembly associated with protrusion and adhesion in cell migration
    • Le Clainche, C., and M.F. Carlier. 2008. Regulation of actin assembly associated with protrusion and adhesion in cell migration. Physiol. Rev. 88:489-513.
    • (2008) Physiol. Rev. , vol.88 , pp. 489-513
    • Le Clainche, C.1    Carlier, M.F.2
  • 29
    • 33645796494 scopus 로고    scopus 로고
    • Morphodynamic profiling of protrusion phenotypes
    • Machacek, M., and G. Danuser. 2006. Morphodynamic profiling of protrusion phenotypes. Biophys. J. 90:1439-1452.
    • (2006) Biophys. J. , vol.90 , pp. 1439-1452
    • Machacek, M.1    Danuser, G.2
  • 30
    • 0031036626 scopus 로고    scopus 로고
    • Expression of constitutively active alpha-PAK reveals effects of the kinase on actin and focal complexes
    • Manser, E., H.Y. Huang, T.H. Loo, X.Q. Chen, J.M. Dong, T. Leung, and L. Lim. 1997. Expression of constitutively active alpha-PAK reveals effects of the kinase on actin and focal complexes. Mol. Cell. Biol. 17:1129-1143.
    • (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
  • 32
    • 33646776346 scopus 로고    scopus 로고
    • Paxillin phosphorylation at Ser273 localizes a GIT1-PIX-PAK complex and regulates adhesion and protrusion dynamics
    • Nayal, A., D.J. Webb, C.M. Brown, E.M. Schaefer, M. Vicente-Manzanares, and A.R. Horwitz. 2006. Paxillin phosphorylation at Ser273 localizes a GIT1-PIX-PAK complex and regulates adhesion and protrusion dynamics. J. Cell Biol. 173:587-589.
    • (2006) J. Cell Biol. , vol.173 , pp. 587-589
    • Nayal, A.1    Webb, D.J.2    Brown, C.M.3    Schaefer, E.M.4    Vicente-Manzanares, M.5    Horwitz, A.R.6
  • 33
    • 77954626097 scopus 로고    scopus 로고
    • Why an A-loop phospho-mimetic fails to activate PAK1: understanding an inaccessible kinase state by molecular dynamics simulations
    • Ng, Y.W., D. Raghunathan, P.M. Chan, Y. Baskaran, D.J. Smith, C.H. Lee, C. Verma, and E. Manser. 2010. Why an A-loop phospho-mimetic fails to activate PAK1: understanding an inaccessible kinase state by molecular dynamics simulations. Structure. 18:879-890.
    • (2010) Structure , vol.18 , pp. 879-890
    • Ng, Y.W.1    Raghunathan, D.2    Chan, P.M.3    Baskaran, Y.4    Smith, D.J.5    Lee, C.H.6    Verma, C.7    Manser, E.8
  • 34
    • 0031034352 scopus 로고    scopus 로고
    • Integrin-ligand binding properties govern cell migration speed through cell-substratum adhesiveness
    • Palecek, S.P., J.C. Loftus, M.H. Ginsberg, D.A. Lauffenburger, and A.F. Horwitz. 1997. Integrin-ligand binding properties govern cell migration speed through cell-substratum adhesiveness. Nature. 385:537-540.
    • (1997) Nature , vol.385 , pp. 537-540
    • Palecek, S.P.1    Loftus, J.C.2    Ginsberg, M.H.3    Lauffenburger, D.A.4    Horwitz, A.F.5
  • 35
    • 69949177832 scopus 로고    scopus 로고
    • Dissecting activation of the PAK1 kinase at protrusions in living cells
    • Parrini, M.C., J. Camonis, M. Matsuda, and J. de Gunzburg. 2009. Dissecting activation of the PAK1 kinase at protrusions in living cells. J. Biol. Chem. 284:24133-24143.
    • (2009) J. Biol. Chem. , vol.284 , pp. 24133-24143
    • Parrini, M.C.1    Camonis, J.2    Matsuda, M.3    de Gunzburg, J.4
  • 36
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard, T.D., and G.G. Borisy. 2003. Cellular motility driven by assembly and disassembly of actin filaments. Cell. 112:453-465.
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 37
    • 4544309783 scopus 로고    scopus 로고
    • Two distinct actin networks drive the protrusion of migrating cells
    • Ponti, A., M. Machacek, S.L. Gupton, C.M. Waterman-Storer, and G. Danuser. 2004. Two distinct actin networks drive the protrusion of migrating cells. Science. 305:1782-1786.
    • (2004) Science , vol.305 , pp. 1782-1786
    • Ponti, A.1    Machacek, M.2    Gupton, S.L.3    Waterman-Storer, C.M.4    Danuser, G.5
  • 39
    • 0033605738 scopus 로고    scopus 로고
    • Inhibition of myosin light chain kinase by p21-activated kinase
    • Sanders, L.C., F. Matsumura, G.M. Bokoch, and P. de Lanerolle. 1999. Inhibition of myosin light chain kinase by p21-activated kinase. Science. 283:2083-2085.
    • (1999) Science , vol.283 , pp. 2083-2085
    • Sanders, L.C.1    Matsumura, F.2    Bokoch, G.M.3    de Lanerolle, P.4
  • 41
    • 0033577902 scopus 로고    scopus 로고
    • p21-activated kinase 1 (Pak1) regulates cell motility in mammalian fibroblasts
    • Sells, M.A., J.T. Boyd, and J. Chernoff. 1999. p21-activated kinase 1 (Pak1) regulates cell motility in mammalian fibroblasts. J. Cell Biol. 145:837-849.
    • (1999) J. Cell Biol. , vol.145 , pp. 837-849
    • Sells, M.A.1    Boyd, J.T.2    Chernoff, J.3
  • 42
    • 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, M.R., L.C. Sanders, E.M. Gardiner, and G.M. Bokoch. 2004. 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) Mol. Biol. Cell. , vol.15 , pp. 2965-2977
    • Stofega, M.R.1    Sanders, L.C.2    Gardiner, E.M.3    Bokoch, G.M.4
  • 43
    • 33646889963 scopus 로고    scopus 로고
    • Activation of myosin in HeLa cells causes redistribution of focal adhesions and F-actin from cell center to cell periphery
    • Szczepanowska, J., E.D. Korn, and H. Brzeska. 2006. Activation of myosin in HeLa cells causes redistribution of focal adhesions and F-actin from cell center to cell periphery. Cell Motil. Cytoskeleton. 63:356-374.
    • (2006) Cell Motil. Cytoskeleton. , vol.63 , pp. 356-374
    • Szczepanowska, J.1    Korn, E.D.2    Brzeska, H.3
  • 44
    • 33847354235 scopus 로고    scopus 로고
    • Regulation of protrusion, adhesion dynamics, and polarity by myosins IIA and IIB in migrating cells
    • Vicente-Manzanares, M., J. Zareno, L. Whitmore, C.K. Choi, and A.F. Horwitz. 2007. Regulation of protrusion, adhesion dynamics, and polarity by myosins IIA and IIB in migrating cells. J. Cell Biol. 176:573-580.
    • (2007) J. Cell Biol. , vol.176 , pp. 573-580
    • Vicente-Manzanares, M.1    Zareno, J.2    Whitmore, L.3    Choi, C.K.4    Horwitz, A.F.5
  • 46
    • 0035833251 scopus 로고    scopus 로고
    • The LD4 motif of paxillin regulates cell spreading and motility through an interaction with paxillin kinase linker (PKL)
    • West, K.A., H. Zhang, M.C. Brown, S.N. Nikolopoulos, M.C. Riedy, A.F. Horwitz, and C.E. Turner. 2001. The LD4 motif of paxillin regulates cell spreading and motility through an interaction with paxillin kinase linker (PKL). J. Cell Biol. 154:161-176.
    • (2001) J. Cell Biol. , vol.154 , pp. 161-176
    • West, K.A.1    Zhang, H.2    Brown, M.C.3    Nikolopoulos, S.N.4    Riedy, M.C.5    Horwitz, A.F.6    Turner, C.E.7
  • 47
    • 0038457895 scopus 로고    scopus 로고
    • Regulation of leading edge microtubule and actin dynamics downstream of Rac1
    • Wittmann, T., G.M. Bokoch, and C.M. Waterman-Storer. 2003. Regulation of leading edge microtubule and actin dynamics downstream of Rac1. J. Cell Biol. 161:845-851.
    • (2003) J. Cell Biol. , vol.161 , pp. 845-851
    • Wittmann, T.1    Bokoch, G.M.2    Waterman-Storer, C.M.3
  • 48
    • 0344465841 scopus 로고    scopus 로고
    • Early molecular events in the assembly of matrix adhesions at the leading edge of migrating cells
    • Zaidel-Bar, R., C. Ballestrem, Z. Kam, and B. Geiger. 2003. Early molecular events in the assembly of matrix adhesions at the leading edge of migrating cells. J. Cell Sci. 116:4605-4613.
    • (2003) J. Cell Sci. , vol.116 , pp. 4605-4613
    • Zaidel-Bar, R.1    Ballestrem, C.2    Kam, Z.3    Geiger, B.4
  • 49
    • 33846781373 scopus 로고    scopus 로고
    • A paxillin tyrosine phosphorylation switch regulates the assembly and form of cell-matrix adhesions
    • Zaidel-Bar, R., R. Milo, Z. Kam, and B. Geiger. 2007. A paxillin tyrosine phosphorylation switch regulates the assembly and form of cell-matrix adhesions. J. Cell Sci. 12:137-148.
    • (2007) J. Cell Sci. , vol.12 , pp. 137-148
    • Zaidel-Bar, R.1    Milo, R.2    Kam, Z.3    Geiger, B.4
  • 51
    • 0033843129 scopus 로고    scopus 로고
    • Coupling of PAK-interacting exchange factor PIX to GIT1 promotes focal complex disassembly
    • Zhao, Z.S., E. Manser, T.H. Loo, and L. Lim. 2000. Coupling of PAK-interacting exchange factor PIX to GIT1 promotes focal complex disassembly. Mol. Cell. Biol. 20:6354-6363.
    • (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.