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Volumn 135, Issue 1, 2008, Pages 123-136

A Tripartite Complex Containing MRCK Modulates Lamellar Actomyosin Retrograde Flow

Author keywords

CELLBIO

Indexed keywords

ADAPTOR PROTEIN; ALPHA TUBULIN; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOSIN II; PHOSPHOTRANSFERASE; PROTEIN CDC42; PROTEIN LRAP35A; PROTEIN MRCK; PROTEIN MYO18A; PROTEIN MYO2A; RAC PROTEIN; UNCLASSIFIED DRUG;

EID: 52949140261     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2008.09.018     Document Type: Article
Times cited : (112)

References (37)
  • 1
    • 33846286901 scopus 로고    scopus 로고
    • Shaping the actin cytoskeleton using microtubule tips
    • Basu R., and Chang F. Shaping the actin cytoskeleton using microtubule tips. Curr. Opin. Cell Biol. 19 (2007) 88-94
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 88-94
    • Basu, R.1    Chang, F.2
  • 3
    • 0033538521 scopus 로고    scopus 로고
    • The myotonic dystrophy kinase-related Cdc42-binding kinase is involved in the regulation of neurite outgrowth in PC12 cells
    • Chen X.Q., Tan I., Leung T., and Lim L. The myotonic dystrophy kinase-related Cdc42-binding kinase is involved in the regulation of neurite outgrowth in PC12 cells. J. Biol. Chem. 274 (1999) 19901-19905
    • (1999) J. Biol. Chem. , vol.274 , pp. 19901-19905
    • Chen, X.Q.1    Tan, I.2    Leung, T.3    Lim, L.4
  • 7
    • 17844379382 scopus 로고    scopus 로고
    • Nuclear movement regulated by Cdc42, MRCK, myosin, and actin flow establishes MTOC polarization in migrating cells
    • Gomes E.R., Jani S., and Gundersen G.G. Nuclear movement regulated by Cdc42, MRCK, myosin, and actin flow establishes MTOC polarization in migrating cells. Cell 121 (2005) 451-463
    • (2005) Cell , vol.121 , pp. 451-463
    • Gomes, E.R.1    Jani, S.2    Gundersen, G.G.3
  • 8
    • 34249019594 scopus 로고    scopus 로고
    • Co-operative Cdc42 and Rho signalling mediates ephrinB-triggered endothelial cell retraction
    • Groeger G., and Nobes C.D. Co-operative Cdc42 and Rho signalling mediates ephrinB-triggered endothelial cell retraction. Biochem. J. 404 (2007) 23-29
    • (2007) Biochem. J. , vol.404 , pp. 23-29
    • Groeger, G.1    Nobes, C.D.2
  • 9
    • 33745245989 scopus 로고    scopus 로고
    • Spatiotemporal feedback between actomyosin and focal-adhesion systems optimizes rapid cell migration
    • Gupton S.L., and Waterman-Storer C.M. Spatiotemporal feedback between actomyosin and focal-adhesion systems optimizes rapid cell migration. Cell 125 (2006) 1361-1374
    • (2006) Cell , vol.125 , pp. 1361-1374
    • Gupton, S.L.1    Waterman-Storer, C.M.2
  • 10
    • 35648943165 scopus 로고    scopus 로고
    • mDia2 regulates actin and focal adhesion dynamics and organization in the lamella for efficient epithelial cell migration
    • Gupton S.L., Eisenmann K., Alberts A.S., and Waterman-Storer C.M. mDia2 regulates actin and focal adhesion dynamics and organization in the lamella for efficient epithelial cell migration. J. Cell Sci. 120 (2007) 3475-3487
    • (2007) J. Cell Sci. , vol.120 , pp. 3475-3487
    • Gupton, S.L.1    Eisenmann, K.2    Alberts, A.S.3    Waterman-Storer, C.M.4
  • 12
    • 0032860424 scopus 로고    scopus 로고
    • Regulation of the cytoskeleton and cell adhesion by the Rho family GTPases in mammalian cells
    • Kaibuchi K., Kuroda S., and Amano M. Regulation of the cytoskeleton and cell adhesion by the Rho family GTPases in mammalian cells. Annu. Rev. Biochem. 68 (1999) 459-486
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 459-486
    • Kaibuchi, K.1    Kuroda, S.2    Amano, M.3
  • 15
    • 0344012487 scopus 로고    scopus 로고
    • Asymmetric distribution of myosin IIB in migrating endothelial cells is regulated by a rho-dependent kinase and contributes to tail retraction
    • Kolega J. Asymmetric distribution of myosin IIB in migrating endothelial cells is regulated by a rho-dependent kinase and contributes to tail retraction. Mol. Biol. Cell 14 (2003) 4745-4757
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4745-4757
    • Kolega, J.1
  • 16
    • 33749503375 scopus 로고    scopus 로고
    • The role of myosin II motor activity in distributing myosin asymmetrically and coupling protrusive activity to cell translocation
    • Kolega J. The role of myosin II motor activity in distributing myosin asymmetrically and coupling protrusive activity to cell translocation. Mol. Biol. Cell 17 (2006) 4435-4445
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4435-4445
    • Kolega, J.1
  • 17
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: a physical integrated molecular process
    • Lauffenburger D.A., and Horwitz A.F. Cell migration: a physical integrated molecular process. Cell 84 (1996) 359-369
    • (1996) Cell , vol.84 , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 18
    • 0031962372 scopus 로고    scopus 로고
    • Myotonic dystrophy kinase-related Cdc42-binding kinase acts as a Cdc42 effector in promoting cytoskeletal reorganization
    • Leung T., Chen X.Q., Manser E., and Lim L. Myotonic dystrophy kinase-related Cdc42-binding kinase acts as a Cdc42 effector in promoting cytoskeletal reorganization. Mol. Cell. Biol. 18 (1998) 130-140
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 130-140
    • Leung, T.1    Chen, X.Q.2    Manser, E.3    Lim, L.4
  • 20
    • 0030049170 scopus 로고    scopus 로고
    • Actin-based cell motility and cell locomotion
    • Mitchison T.J., and Cramer L.P. Actin-based cell motility and cell locomotion. Cell 84 (1996) 371-379
    • (1996) Cell , vol.84 , pp. 371-379
    • Mitchison, T.J.1    Cramer, L.P.2
  • 22
    • 41549108457 scopus 로고    scopus 로고
    • Building the actin cytoskeleton: filopodia contribute to the construction of contractile bundles in the lamella
    • Nemethova M., Auinger S., and Small J.V. Building the actin cytoskeleton: filopodia contribute to the construction of contractile bundles in the lamella. J. Cell Biol. 180 (2008) 1233-1244
    • (2008) J. Cell Biol. , vol.180 , pp. 1233-1244
    • Nemethova, M.1    Auinger, S.2    Small, J.V.3
  • 23
    • 4544336870 scopus 로고    scopus 로고
    • Expression of the human myotonic dystrophy kinase-related Cdc42-binding kinase gamma is regulated by promoter DNA methylation and Sp1 binding
    • Ng Y., Tan I., Lim L., and Leung T. Expression of the human myotonic dystrophy kinase-related Cdc42-binding kinase gamma is regulated by promoter DNA methylation and Sp1 binding. J. Biol. Chem. 279 (2004) 34156-34164
    • (2004) J. Biol. Chem. , vol.279 , pp. 34156-34164
    • Ng, Y.1    Tan, I.2    Lim, L.3    Leung, T.4
  • 24
    • 33646197411 scopus 로고    scopus 로고
    • Spatiotemporal dynamics of RhoA activity in migrating cells
    • Pertz O., Hodgson L., Klemke R.L., and Hahn K.M. Spatiotemporal dynamics of RhoA activity in migrating cells. Nature 440 (2006) 1069-1072
    • (2006) Nature , vol.440 , pp. 1069-1072
    • Pertz, O.1    Hodgson, L.2    Klemke, R.L.3    Hahn, K.M.4
  • 25
    • 0037459075 scopus 로고    scopus 로고
    • Cell motility driven by assembly and disassembly of actin filaments
    • Pollard T.D., and Borisy G.G. Cell motility driven by assembly and disassembly of actin filaments. Cell 112 (2003) 453-465
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 26
  • 27
    • 0345731237 scopus 로고    scopus 로고
    • Cell migration: Rho GTPases lead the way
    • Raftopoulou M., and Hall A. Cell migration: Rho GTPases lead the way. Dev. Biol. 265 (2004) 23-32
    • (2004) Dev. Biol. , vol.265 , pp. 23-32
    • Raftopoulou, M.1    Hall, A.2
  • 30
    • 0035933849 scopus 로고    scopus 로고
    • Activation of LIM kinases by myotonic dystrophy kinase-related Cdc42-binding kinase alpha
    • Sumi T., Matsumoto K., Shibuya A., and Nakamura T. Activation of LIM kinases by myotonic dystrophy kinase-related Cdc42-binding kinase alpha. J. Biol. Chem. 276 (2001) 23092-23096
    • (2001) J. Biol. Chem. , vol.276 , pp. 23092-23096
    • Sumi, T.1    Matsumoto, K.2    Shibuya, A.3    Nakamura, T.4
  • 31
    • 0035079891 scopus 로고    scopus 로고
    • Intermolecular and intramolecular interactions regulate catalytic activity of myotonic dystrophy kinase-related Cdc42-binding kinase alpha
    • Tan I., Seow K.T., Lim L., and Leung T. Intermolecular and intramolecular interactions regulate catalytic activity of myotonic dystrophy kinase-related Cdc42-binding kinase alpha. Mol. Cell. Biol. 21 (2001) 2767-2778
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2767-2778
    • Tan, I.1    Seow, K.T.2    Lim, L.3    Leung, T.4
  • 32
    • 0842288222 scopus 로고    scopus 로고
    • Distinct roles of MLCK and ROCK in the regulation of membrane protrusions and focal adhesion dynamics during cell migration of fibroblasts
    • Totsukawa G., Wu Y., Sasaki Y., Hartshorne D.J., Yamakita Y., Yamashiro S., and Matsumura F. Distinct roles of MLCK and ROCK in the regulation of membrane protrusions and focal adhesion dynamics during cell migration of fibroblasts. J. Cell Biol. 164 (2004) 427-439
    • (2004) J. Cell Biol. , vol.164 , pp. 427-439
    • Totsukawa, G.1    Wu, Y.2    Sasaki, Y.3    Hartshorne, D.J.4    Yamakita, Y.5    Yamashiro, S.6    Matsumura, F.7
  • 33
    • 33847354235 scopus 로고    scopus 로고
    • Regulation of protrusion, adhesion dynamics, and polarity by myosins IIA and IIB in migrating cells
    • Vicente-Manzanares M., Zareno J., Whitmore L., Choi C.K., and Horwitz A.F. Regulation of protrusion, adhesion dynamics, and polarity by myosins IIA and IIB in migrating cells. J. Cell Biol. 176 (2007) 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
  • 34
    • 14744304060 scopus 로고    scopus 로고
    • Cdc42-MRCK and Rho-ROCK signalling cooperate in myosin phosphorylation and cell invasion
    • Wilkinson S., Paterson H.F., and Marshall C.J. Cdc42-MRCK and Rho-ROCK signalling cooperate in myosin phosphorylation and cell invasion. Nat. Cell Biol. 7 (2005) 255-261
    • (2005) Nat. Cell Biol. , vol.7 , pp. 255-261
    • Wilkinson, S.1    Paterson, H.F.2    Marshall, C.J.3
  • 37
    • 0033843129 scopus 로고    scopus 로고
    • Coupling of PAK-interacting exchange factor PIX to GIT1 promotes focal complex disassembly
    • Zhao Z.S., Manser E., Loo T.H., and Lim L. Coupling of PAK-interacting exchange factor PIX to GIT1 promotes focal complex disassembly. Mol. Cell. Biol. 20 (2000) 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.