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Volumn 27, Issue 1, 2013, Pages 123-134

p210bcr-abl induces amoeboid motility by recruiting ADF/destrin through RhoA/ROCK1

Author keywords

Actin binding proteins; Cell migration; GTPases; Isoform selectivity; Leukemia; Signalplex

Indexed keywords

4 (1 AMINOETHYL) N (4 PYRIDYL)CYCLOHEXANECARBOXAMIDE; ACTIN DEPOLYMERIZING FACTOR; BCR ABL PROTEIN; COFILIN 1; MATRIGEL; MYOSIN; RHO KINASE; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; ROCK PROTEIN 1; UNCLASSIFIED DRUG; ADULT T CELL LEUKEMIA DERIVED FACTOR; ADULT T CELL LEUKEMIA-DERIVED FACTOR; CYTOKINE; PRIMER DNA; ROCK1 PROTEIN, MOUSE; TUMOR PROTEIN;

EID: 84871860380     PISSN: None     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.12-205112     Document Type: Article
Times cited : (18)

References (58)
  • 1
    • 14644425319 scopus 로고    scopus 로고
    • Mechanisms of BCR-ABL in the pathogenesis of chronic myelogenous leukaemia
    • Ren, R. (2005) Mechanisms of BCR-ABL in the pathogenesis of chronic myelogenous leukaemia. Nat. Rev. Cancer 5, 172-183
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 172-183
    • Ren, R.1
  • 2
    • 0025117392 scopus 로고
    • Induction of chronic myelogenous leukemia in mice by the P210bcr/abl gene of the Philadelphia chromosome
    • Daley, G. Q., Van Etten, R. A., and Baltimore, D. (1990) Induction of chronic myelogenous leukemia in mice by the P210bcr/abl gene of the Philadelphia chromosome. Science 247, 824-830
    • (1990) Science , vol.247 , pp. 824-830
    • Daley, G.Q.1    Van Etten, R.A.2    Baltimore, D.3
  • 4
    • 0000506439 scopus 로고    scopus 로고
    • p210 and p190(BCR/ABL) induce the tyrosine phosphorylation and DNA binding activity of multiple specific STAT family members
    • Ilaria, R. L., Jr., and Van Etten, R. A. (1996) p210 and p190(BCR/ABL) induce the tyrosine phosphorylation and DNA binding activity of multiple specific STAT family members. J. Biol. Chem. 271, 31704-31710
    • (1996) J. Biol. Chem. , vol.271 , pp. 31704-31710
    • Ilaria Jr., R.L.1    Van Etten, R.A.2
  • 5
    • 0025348013 scopus 로고
    • Tyrosine kinase activity and transformation potency of bcr-abl oncogene products
    • Lugo, T. G., Pendergast, A. M., Muller, A. J., and Witte, O. N. (1990) Tyrosine kinase activity and transformation potency of bcr-abl oncogene products. Science 247, 1079-1082
    • (1990) Science , vol.247 , pp. 1079-1082
    • Lugo, T.G.1    Pendergast, A.M.2    Muller, A.J.3    Witte, O.N.4
  • 7
    • 0141455972 scopus 로고    scopus 로고
    • Localization of BCR-ABL to F-actin regulates cell adhesion but does not attenuate CML development
    • DOI 10.1182/blood-2003-01-0062
    • Wertheim, J. A., Perera, S. A., Hammer, D. A., Ren, R., Boettiger, D., and Pear, W. S. (2003) Localization of BCR-ABL to F-actin regulates cell adhesion but does not attenuate CML development. Blood 102, 2220-2228 (Pubitemid 37122402)
    • (2003) Blood , vol.102 , Issue.6 , pp. 2220-2228
    • Wertheim, J.A.1    Perera, S.A.2    Hammer, D.A.3    Ren, R.4    Boettiger, D.5    Pear, W.S.6
  • 8
    • 40849120282 scopus 로고    scopus 로고
    • BCR/ABL expression of myeloid progenitors increases beta1-integrin mediated adhesion to stromal cells
    • Fierro, F. A., Taubenberger, A., Puech, P. H., Ehninger, G., Bornhauser, M., Muller, D. J., and Illmer, T. (2008) BCR/ABL expression of myeloid progenitors increases beta1-integrin mediated adhesion to stromal cells. J. Mol. Biol. 377, 1082-1093
    • (2008) J. Mol. Biol. , vol.377 , pp. 1082-1093
    • Fierro, F.A.1    Taubenberger, A.2    Puech, P.H.3    Ehninger, G.4    Bornhauser, M.5    Muller, D.J.6    Illmer, T.7
  • 9
    • 70450162852 scopus 로고    scopus 로고
    • p210(Bcr-Abl) desensitizes Cdc42 GTPase signaling for SDF-1alpha-directed migration in chronic myeloid leukemia cells
    • Chang, Y. C., Tien, S. C., Tien, H. F., Zhang, H., Bokoch, G. M., and Chang, Z. F. (2009) p210(Bcr-Abl) desensitizes Cdc42 GTPase signaling for SDF-1alpha-directed migration in chronic myeloid leukemia cells. Oncogene 28, 4105-4115
    • (2009) Oncogene , vol.28 , pp. 4105-4115
    • Chang, Y.C.1    Tien, S.C.2    Tien, H.F.3    Zhang, H.4    Bokoch, G.M.5    Chang, Z.F.6
  • 10
    • 16844380143 scopus 로고    scopus 로고
    • BCR-ABL inhibits SDF-1 chemotactic responce via alteration of CXCR4 signaling and down-regulation of CXCR4 expression
    • DOI 10.1158/0008-5472.CAN-04-2152
    • Geay, J. F., Buet, D., Zhang, Y., Foudi, A., Jarrier, P., Berthebaud, M., Turhan, A. G., Vainchenker, W., and Louache, F. (2005) p210BCR-ABL inhibits SDF-1 chemotactic response via alteration of CXCR4 signaling and down-regulation of CXCR4 expression. Cancer Res. 65, 2676-2683 (Pubitemid 40490067)
    • (2005) Cancer Research , vol.65 , Issue.7 , pp. 2676-2683
    • Geay, J.-F.1    Buet, D.2    Zhang, Y.3    Foudi, A.4    Jarrier, P.5    Berthebaud, M.6    Turhan, A.G.7    Vainchenker, W.8    Louache, F.9
  • 13
    • 42549093634 scopus 로고    scopus 로고
    • bcr-abl-expressing cells: Respective roles of Vav and Bcr-Abl GEFs
    • DOI 10.1038/sj.onc.1210933, PII 1210933
    • Daubon, T., Chasseriau, J., El Ali, A., Rivet, J., Kitzis, A., Constantin, B., and Bourmeyster, N. (2008) Differential motility of p190bcr-abl- and p210bcr-abl-expressing cells: respective roles of Vav and Bcr-Abl GEFs. Oncogene 27, 2673-2685 (Pubitemid 351581467)
    • (2008) Oncogene , vol.27 , Issue.19 , pp. 2673-2685
    • Daubon, T.1    Chasseriau, J.2    Ali, A.E.3    Rivet, J.4    Kitzis, A.5    Constantin, B.6    Bourmeyster, N.7
  • 14
    • 0142135501 scopus 로고    scopus 로고
    • bcr-abl
    • DOI 10.1038/sj.onc.1206626
    • Harnois, T., Constantin, B., Rioux, A., Grenioux, E., Kitzis, A., and Bourmeyster, N. (2003) Differential interaction and activation of Rho family GTPases by p210bcr-abl and p190bcr-abl. Oncogene 22, 6445-6454 (Pubitemid 37281691)
    • (2003) Oncogene , vol.22 , Issue.41 , pp. 6445-6454
    • Harnois, T.1    Constantin, B.2    Rioux, A.3    Grenioux, E.4    Kitzis, A.5    Bourmeyster, N.6
  • 15
    • 0345731237 scopus 로고    scopus 로고
    • Cell migration: Rho GTPases lead the way
    • DOI 10.1016/j.ydbio.2003.06.003
    • Raftopoulou, M., and Hall, A. (2004) Cell migration: Rho GTPases lead the way. Dev. Biol. 265, 23-32 (Pubitemid 38018819)
    • (2004) Developmental Biology , vol.265 , Issue.1 , pp. 23-32
    • Raftopoulou, M.1    Hall, A.2
  • 17
    • 44449097488 scopus 로고    scopus 로고
    • On the Rho'd: The regulation of membrane protrusions by Rho-GTPases
    • Ladwein, M., and Rottner, K. (2008) On the Rho'd: the regulation of membrane protrusions by Rho-GTPases. FEBS Lett. 582, 2066-2074
    • (2008) FEBS Lett. , vol.582 , pp. 2066-2074
    • Ladwein, M.1    Rottner, K.2
  • 18
    • 36248969983 scopus 로고    scopus 로고
    • Actin stress fibres
    • Pellegrin, S., and Mellor, H. (2007) Actin stress fibres. J. Cell Sci. 120, 3491-3499
    • (2007) J. Cell Sci. , vol.120 , pp. 3491-3499
    • Pellegrin, S.1    Mellor, H.2
  • 19
    • 70349314647 scopus 로고    scopus 로고
    • Mechanical modes of 'amoeboid' cell migration
    • Lammermann, T., and Sixt, M. (2009) Mechanical modes of 'amoeboid' cell migration. Curr. Opin. Cell Biol. 21, 636-644
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 636-644
    • Lammermann, T.1    Sixt, M.2
  • 20
    • 33750320965 scopus 로고    scopus 로고
    • Dissection of amoeboid movement into two mechanically distinct modes
    • DOI 10.1242/jcs.03152
    • Yoshida, K., and Soldati, T. (2006) Dissection of amoeboid movement into two mechanically distinct modes. J. Cell Sci. 119, 3833-3844 (Pubitemid 44614435)
    • (2006) Journal of Cell Science , vol.119 , Issue.18 , pp. 3833-3844
    • Yoshida, K.1    Soldati, T.2
  • 21
    • 0031044473 scopus 로고    scopus 로고
    • Dynamic imaging of neutrophil migration in three dimensions: Mechanical interactions between cells and matrix
    • Mandeville, J. T., Lawson, M. A., and Maxfield, F. R. (1997) Dynamic imaging of neutrophil migration in three dimensions: mechanical interactions between cells and matrix. J. Leukoc. Biol. 61, 188-200 (Pubitemid 27081380)
    • (1997) Journal of Leukocyte Biology , vol.61 , Issue.2 , pp. 188-200
    • Mandeville, J.T.H.1    Lawson, M.A.2    Maxfield, F.R.3
  • 22
    • 0038049137 scopus 로고    scopus 로고
    • Tumour-cell invasion and migration: Diversity and escape mechanisms
    • DOI 10.1038/nrc1075
    • Friedl, P., and Wolf, K. (2003) Tumour-cell invasion and migration: diversity and escape mechanisms. Nat. Rev. Cancer 3, 362-374 (Pubitemid 37328856)
    • (2003) Nature Reviews Cancer , vol.3 , Issue.5 , pp. 362-374
    • Friedl, P.1    Wolf, K.2
  • 23
    • 0042354574 scopus 로고    scopus 로고
    • Differing modes for tumour cell invasion have distinct requirements for Rho/ROCK signalling and extracellular proteolysis
    • DOI 10.1038/ncb1019
    • Sahai, E., and Marshall, C. J. (2003) Differing modes of tumour cell invasion have distinct requirements for Rho/ROCK signalling and extracellular proteolysis. Nat. Cell Biol. 5, 711-719 (Pubitemid 36986778)
    • (2003) Nature Cell Biology , vol.5 , Issue.8 , pp. 711-719
    • Sahai, E.1    Marshall, C.J.2
  • 24
    • 34347382959 scopus 로고    scopus 로고
    • Loss of p53 promotes RhoA-ROCK-dependent cell migration and invasion in 3D matrices
    • DOI 10.1083/jcb.200701120
    • Gadea, G., de Toledo, M., Anguille, C., and Roux, P. (2007) Loss of p53 promotes RhoA-ROCK-dependent cell migration and invasion in 3D matrices. J. Cell Biol. 178, 23-30 (Pubitemid 47026399)
    • (2007) Journal of Cell Biology , vol.178 , Issue.1 , pp. 23-30
    • Gadea, G.1    De Toledo, M.2    Anguille, C.3    Roux, P.4
  • 25
    • 33746562929 scopus 로고    scopus 로고
    • ROCK- and Myosin-Dependent Matrix Deformation Enables Protease-Independent Tumor-Cell Invasion In Vivo
    • DOI 10.1016/j.cub.2006.05.065, PII S0960982206017246
    • Wyckoff, J. B., Pinner, S. E., Gschmeissner, S., Condeelis, J. S., and Sahai, E. (2006) ROCK- and myosin-dependent matrix deformation enables protease-independent tumor-cell invasion in vivo. Curr. Biol. 16, 1515-1523 (Pubitemid 44142977)
    • (2006) Current Biology , vol.16 , Issue.15 , pp. 1515-1523
    • Wyckoff, J.B.1    Pinner, S.E.2    Gschmeissner, S.3    Condeelis, J.S.4    Sahai, E.5
  • 26
    • 12844269159 scopus 로고    scopus 로고
    • Actin-depolymerizing factor and cofilin-1 play overlapping roles in promoting rapid F-actin depolymerization in mammalian nonmuscle cells
    • DOI 10.1091/mbc.E04-07-0555
    • Hotulainen, P., Paunola, E., Vartiainen, M. K., and Lappalainen, P. (2005) Actin-depolymerizing factor and cofilin-1 play overlapping roles in promoting rapid F-actin depolymerization in mammalian nonmuscle cells. Mol. Biol. Cell 16, 649-664 (Pubitemid 40165562)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.2 , pp. 649-664
    • Hotulainen, P.1    Paunola, E.2    Vartiainen, M.K.3    Lappalainen, P.4
  • 27
    • 79960916563 scopus 로고    scopus 로고
    • In vitro analysis of chemotactic leukocyte migration in 3D environments
    • Sixt, M., and Lammermann, T. (2010) In vitro analysis of chemotactic leukocyte migration in 3D environments. Methods Mol. Biol. 769, 149-165
    • (2010) Methods Mol. Biol. , vol.769 , pp. 149-165
    • Sixt, M.1    Lammermann, T.2
  • 28
    • 14844333094 scopus 로고    scopus 로고
    • Global effects of BCR/ABL and TEL/PDGFRbeta expression on the proteome and phosphoproteome: Identification of the Rho pathway as a target of BCR/ABL
    • DOI 10.1074/jbc.M410598200
    • Unwin, R. D., Sternberg, D. W., Lu, Y., Pierce, A., Gilliland, D. G., and Whetton, A. D. (2005) Global effects of BCR/ABL and TEL/PDGFRbeta expression on the proteome and phosphoproteome: identification of the Rho pathway as a target of BCR/ABL. J. Biol. Chem. 280, 6316-6326 (Pubitemid 40341178)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.8 , pp. 6316-6326
    • Unwin, R.D.1    Sternberg, D.W.2    Lu, Y.3    Pierce, A.4    Gilliland, D.G.5    Whetton, A.D.6
  • 34
    • 2342436150 scopus 로고    scopus 로고
    • Cofilin Promotes Actin Polymerization and Defines the Direction of Cell Motility
    • DOI 10.1126/science.1094561
    • Ghosh, M., Song, X., Mouneimne, G., Sidani, M., Lawrence, D. S., and Condeelis, J. S. (2004) cofilin promotes actin polymerization and defines the direction of cell motility. Science 304, 743-746 (Pubitemid 38560882)
    • (2004) Science , vol.304 , Issue.5671 , pp. 743-746
    • Ghosh, M.1    Song, X.2    Mouneimne, G.3    Sidani, M.4    Lawrence, D.S.5    Condeelis, J.S.6
  • 35
    • 1642282882 scopus 로고    scopus 로고
    • Prespecification and plasticity: Shifting mechanisms of cell migration
    • Friedl, P. (2004) Prespecification and plasticity: shifting mechanisms of cell migration. Curr. Opin. Cell Biol. 16, 14-23
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 14-23
    • Friedl, P.1
  • 36
    • 38849185196 scopus 로고    scopus 로고
    • PDK1 regulates cancer cell motility by antagonising inhibition of ROCK1 by RhoE
    • DOI 10.1038/ncb1675, PII NCB1675
    • Pinner, S., and Sahai, E. (2008) PDK1 regulates cancer cell motility by antagonising inhibition of ROCK1 by RhoE. Nat. Cell Biol. 10, 127-137 (Pubitemid 351194042)
    • (2008) Nature Cell Biology , vol.10 , Issue.2 , pp. 127-137
    • Pinner, S.1    Sahai, E.2
  • 38
    • 79953743688 scopus 로고    scopus 로고
    • Rho-kinase in development and heart failure: Insights from genetic models
    • Shi, J., Zhang, L., and Wei, L. (2011) Rho-kinase in development and heart failure: insights from genetic models. Pediatr. Cardiol. 32, 297-304
    • (2011) Pediatr. Cardiol. , vol.32 , pp. 297-304
    • Shi, J.1    Zhang, L.2    Wei, L.3
  • 39
    • 78149353346 scopus 로고    scopus 로고
    • Rho-kinase/ROCK: A key regulator of the cytoskeleton and cell polarity
    • Amano, M., Nakayama, M., and Kaibuchi, K. (2010) Rho-kinase/ROCK: a key regulator of the cytoskeleton and cell polarity. Cytoskeleton (Hoboken) 67, 545-554
    • (2010) Cytoskeleton (Hoboken) , vol.67 , pp. 545-554
    • Amano, M.1    Nakayama, M.2    Kaibuchi, K.3
  • 40
    • 0035865682 scopus 로고    scopus 로고
    • LIM-kinase 2 induces formation of stress fibres, focal adhesions and membrane blebs, dependent on its activation by Rho-associated kinase-catalysed phosphorylation at threonine-505
    • DOI 10.1042/0264-6021:3540149
    • Amano, T., Tanabe, K., Eto, T., Narumiya, S., and Mizuno, K. (2001) LIM-kinase 2 induces formation of stress fibres, focal adhesions and membrane blebs, dependent on its activation by Rho-associated kinase-catalysed phosphorylation at threonine-505. Biochem. J. 354, 149-159 (Pubitemid 32183455)
    • (2001) Biochemical Journal , vol.354 , Issue.1 , pp. 149-159
    • Amano, T.1    Tanabe, K.2    Eto, T.3    Narumiya, S.4    Mizuno, K.5
  • 41
    • 34249315804 scopus 로고    scopus 로고
    • Lim kinases, regulators of actin dynamics
    • Bernard, O. (2007) Lim kinases, regulators of actin dynamics. Int. J. Biochem. Cell Biol. 39, 1071-1076
    • (2007) Int. J. Biochem. Cell Biol. , vol.39 , pp. 1071-1076
    • Bernard, O.1
  • 42
    • 77950859278 scopus 로고    scopus 로고
    • ADF/cofilin: A functional node in cell biology
    • Bernstein, B. W., and Bamburg, J. R. (2010) ADF/cofilin: a functional node in cell biology. Trends Cell Biol. 20, 187-195
    • (2010) Trends Cell Biol. , vol.20 , pp. 187-195
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 43
    • 0036153765 scopus 로고    scopus 로고
    • The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamics
    • DOI 10.1091/mbc.01-07-0331
    • Vartiainen, M. K., Mustonen, T., Mattila, P. K., Ojala, P. J., Thesleff, I., Partanen, J., and Lappalainen, P. (2002) The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamics. Mol. Biol. Cell 13, 183-194 (Pubitemid 34106068)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.1 , pp. 183-194
    • Vartiainen, M.K.1    Mustonen, T.2    Mattila, P.K.3    Ojala, P.J.4    Thesleff, I.5    Partanen, J.6    Lappalainen, P.7
  • 44
    • 0036304481 scopus 로고    scopus 로고
    • Determining the differences in actin binding by human ADF and cofilin
    • DOI 10.1006/jmbi.2001.5280
    • Yeoh, S., Pope, B., Mannherz, H. G., and Weeds, A. (2002) Determining the differences in actin binding by human ADF and cofilin. J. Mol. Biol. 315, 911-925 (Pubitemid 34729336)
    • (2002) Journal of Molecular Biology , vol.315 , Issue.4 , pp. 911-925
    • Yeoh, S.1    Pope, B.2    Mannherz, H.G.3    Weeds, A.4
  • 47
    • 11844276055 scopus 로고    scopus 로고
    • The actin depolymerizing factor n-cofilin is essential for neural tube morphogenesis and neural crest cell migration
    • DOI 10.1016/j.ydbio.2004.11.010, PII S0012160604008024
    • Gurniak, C. B., Perlas, E., and Witke, W. (2005) The actin depolymerizing factor n-cofilin is essential for neural tube morphogenesis and neural crest cell migration. Dev. Biol. 278, 231-241 (Pubitemid 40092863)
    • (2005) Developmental Biology , vol.278 , Issue.1 , pp. 231-241
    • Gurniak, C.B.1    Perlas, E.2    Witke, W.3
  • 48
    • 61849163272 scopus 로고    scopus 로고
    • Molecular biology of bcr-abl1-positive chronic myeloid leukemia
    • Quintas-Cardama, A., and Cortes, J. (2009) Molecular biology of bcr-abl1-positive chronic myeloid leukemia. Blood 113, 1619-1630
    • (2009) Blood , vol.113 , pp. 1619-1630
    • Quintas-Cardama, A.1    Cortes, J.2
  • 49
    • 34347374867 scopus 로고    scopus 로고
    • BMP gradients steer nerve growth cones by a balancing act of LIM kinase and Slingshot phosphatase on ADF/cofilin
    • DOI 10.1083/jcb.200703055
    • Wen, Z., Han, L., Bamburg, J. R., Shim, S., Ming, G. L., and Zheng, J. Q. (2007) BMP gradients steer nerve growth cones by a balancing act of LIM kinase and Slingshot phosphatase on ADF/cofilin. J. Cell Biol. 178, 107-119 (Pubitemid 47026406)
    • (2007) Journal of Cell Biology , vol.178 , Issue.1 , pp. 107-119
    • Wen, Z.1    Han, L.2    Bamburg, J.R.3    Shim, S.4    Ming, G.-L.5    Zheng, J.Q.6
  • 51
    • 0142245603 scopus 로고    scopus 로고
    • Amoeboid shape change and contact guidance: T-lymphocyte crawling through fibrillar collagen is independent of matrix remodeling by MMPs and other proteases
    • DOI 10.1182/blood-2002-12-3791
    • Wolf, K., Muller, R., Borgmann, S., Brocker, E. B., and Friedl, P. (2003) Amoeboid shape change and contact guidance: T-lymphocyte crawling through fibrillar collagen is independent of matrix remodeling by MMPs and other proteases. Blood 102, 3262-3269 (Pubitemid 37314765)
    • (2003) Blood , vol.102 , Issue.9 , pp. 3262-3269
    • Wolf, K.1    Muller, R.2    Borgmann, S.3    Brocker, E.-B.4    Friedl, P.5
  • 52
    • 33750289641 scopus 로고    scopus 로고
    • ROCK signaling mediates the adoption of different modes of migration and invasion in human mammary epithelial tumor cells
    • DOI 10.1016/j.yexcr.2006.08.025, PII S0014482706003375
    • Torka, R., Thuma, F., Herzog, V., and Kirfel, G. (2006) ROCK signaling mediates the adoption of different modes of migration and invasion in human mammary epithelial tumor cells. Exp. Cell Res. 312, 3857-3871 (Pubitemid 44633886)
    • (2006) Experimental Cell Research , vol.312 , Issue.19 , pp. 3857-3871
    • Torka, R.1    Thuma, F.2    Herzog, V.3    Kirfel, G.4
  • 53
    • 14744304060 scopus 로고    scopus 로고
    • Cdc42-MRCK and Rho-ROCK signalling cooperate in myosin phosphorylation and cell invasion
    • DOI 10.1038/ncb1230
    • Wilkinson, S., Paterson, H. F., and Marshall, C. J. (2005) Cdc42-MRCK and Rho-ROCK signalling cooperate in myosin phosphorylation and cell invasion. Nat. Cell Biol. 7, 255-261 (Pubitemid 40331126)
    • (2005) Nature Cell Biology , vol.7 , Issue.3 , pp. 255-261
    • Wilkinson, S.1    Paterson, H.F.2    Marshall, C.J.3
  • 54
    • 0030601313 scopus 로고    scopus 로고
    • Dephosphorylation of cofilin in polymorphonuclear leukocytes derived from peripheral blood
    • DOI 10.1006/excr.1996.0256
    • Okada, K., Takano-Ohmuro, H., Obinata, T., and Abe, H. (1996) Dephosphorylation of cofilin in polymorphonuclear leukocytes derived from peripheral blood. Exp. Cell Res. 227, 116-122 (Pubitemid 26293422)
    • (1996) Experimental Cell Research , vol.227 , Issue.1 , pp. 116-122
    • Okada, K.1    Takano-Ohmuro, H.2    Obinata, T.3    Abe, H.4
  • 55
    • 33847795985 scopus 로고    scopus 로고
    • Cofilin plays a critical role in IL-8-dependent chemotaxis of neutrophilic HL-60 cells through changes in phosphorylation
    • DOI 10.1189/jlb.0506314
    • Hirayama, A., Adachi, R., Otani, S., Kasahara, T., and Suzuki, K. (2007) cofilin plays a critical role in IL-8-dependent chemotaxis of neutrophilic HL-60 cells through changes in phosphorylation. J. Leukoc. Biol. 81, 720-728 (Pubitemid 46393549)
    • (2007) Journal of Leukocyte Biology , vol.81 , Issue.3 , pp. 720-728
    • Hirayama, A.1    Adachi, R.2    Otani, S.3    Kasahara, T.4    Suzuki, K.5
  • 56
    • 77956388103 scopus 로고    scopus 로고
    • An MEK-cofilin signalling module controls migration of human T cells in 3D but not 2D environments
    • Klemke, M., Kramer, E., Konstandin, M. H., Wabnitz, G. H., and Samstag, Y. (2010) An MEK-cofilin signalling module controls migration of human T cells in 3D but not 2D environments. EMBO J. 29, 2915-2929
    • (2010) EMBO J. , vol.29 , pp. 2915-2929
    • Klemke, M.1    Kramer, E.2    Konstandin, M.H.3    Wabnitz, G.H.4    Samstag, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.