메뉴 건너뛰기




Volumn 93, Issue 4, 2013, Pages 611-622

C-Abl tyrosine kinase plays a critical role in β2 integrin-dependent neutrophil migration by regulating Vav1 activity

Author keywords

Acute inflammation; Cytoskeletal rearrangement; F actin; HL 60; Membrane protrusion; PMNs

Indexed keywords

ABELSON KINASE; CD18 ANTIGEN; PROLINE; PROTEIN SH2; PROTEIN SH3;

EID: 84875645787     PISSN: 07415400     EISSN: 19383673     Source Type: Journal    
DOI: 10.1189/jlb.1012487     Document Type: Article
Times cited : (25)

References (44)
  • 3
    • 33344468233 scopus 로고    scopus 로고
    • Neutrophils and immunity: Challenges and opportunities
    • Nathan, C. (2006) Neutrophils and immunity: challenges and opportunities. Nat. Rev. Immunol. 6, 173-182.
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 173-182
    • Nathan, C.1
  • 4
    • 72449160275 scopus 로고    scopus 로고
    • Mechanisms of immune complex-mediated neutrophil recruitment and tissue injury
    • Tanya, N. M., George, C. T., Naotake, T. (2009) Mechanisms of immune complex-mediated neutrophil recruitment and tissue injury. Circulation 120, 2012-2024.
    • (2009) Circulation , vol.120 , pp. 2012-2024
    • Tanya, N.M.1    George, C.T.2    Naotake, T.3
  • 6
    • 79961135745 scopus 로고    scopus 로고
    • Protein 4.1R regulates cell migration and IQGAP1 recruitment to the leading edge
    • Ruiz-Sáenz, A., Kremer, L., Alonso, M. A., Millán, J., Correas, I. (2011) Protein 4.1R regulates cell migration and IQGAP1 recruitment to the leading edge. J. Cell Sci. 124, 2529-2538.
    • (2011) J. Cell Sci. , vol.124 , pp. 2529-2538
    • Ruiz-Sáenz, A.1    Kremer, L.2    Alonso, M.A.3    Millán, J.4    Correas, I.5
  • 8
    • 0036391801 scopus 로고    scopus 로고
    • The Abl family kinases: Mechanisms of regulation and signaling
    • Pendergast, A. M. (2002) The Abl family kinases: mechanisms of regulation and signaling. Adv. Cancer Res. 85, 51-100.
    • (2002) Adv. Cancer Res. , vol.85 , pp. 51-100
    • Pendergast, A.M.1
  • 9
    • 0038445642 scopus 로고    scopus 로고
    • Regulation of F-actindependent processes by the Abl family of tyrosine kinases
    • Woodring, P. J., Hunter, T., Wang, J. Y. (2003) Regulation of F-actindependent processes by the Abl family of tyrosine kinases. J. Cell Sci. 116, 2613-2626.
    • (2003) J. Cell Sci. , vol.116 , pp. 2613-2626
    • Woodring, P.J.1    Hunter, T.2    Wang, J.Y.3
  • 11
    • 34948892837 scopus 로고    scopus 로고
    • Abl tyrosine kinase promotes dorsal ruffles but restrains lamellipodia extension during cell spreading on fibronectin
    • Jin, H., Wang, J. Y. (2007) Abl tyrosine kinase promotes dorsal ruffles but restrains lamellipodia extension during cell spreading on fibronectin. Mol. Biol. Cell 18, 4143-4154.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 4143-4154
    • Jin, H.1    Wang, J.Y.2
  • 12
    • 34548825949 scopus 로고    scopus 로고
    • c-Abl-mediated phosphorylation of WAVE3 is required for lamellipodia formation and cell migration
    • Sossey-Alaoui, K., Li, X. R., Cowell, J. K. (2007) c-Abl-mediated phosphorylation of WAVE3 is required for lamellipodia formation and cell migration. J. Biol. Chem. 282, 26257-26265.
    • (2007) J. Biol. Chem. , vol.282 , pp. 26257-26265
    • Sossey-Alaoui, K.1    Li, X.R.2    Cowell, J.K.3
  • 13
    • 33845986367 scopus 로고    scopus 로고
    • c-Abl interacts with the WAVE2 signaling complex to induce membrane ruffling and cell spreading
    • Stuart, J. R., Gonzalez, F. H., Kawai, H., Yuan, Z. M. (2006) c-Abl interacts with the WAVE2 signaling complex to induce membrane ruffling and cell spreading. J. Biol. Chem. 281, 31290-31297.
    • (2006) J. Biol. Chem. , vol.281 , pp. 31290-31297
    • Stuart, J.R.1    Gonzalez, F.H.2    Kawai, H.3    Yuan, Z.M.4
  • 15
    • 84867219246 scopus 로고    scopus 로고
    • The tyrosine kinase Abl is a component of macrophage podosomes and is required for podosome formation and function
    • Baruzzi, A., Berton, G. (2012) The tyrosine kinase Abl is a component of macrophage podosomes and is required for podosome formation and function. Eur. J. Immunol. 42, 2720-2726.
    • (2012) Eur. J. Immunol. , vol.42 , pp. 2720-2726
    • Baruzzi, A.1    Berton, G.2
  • 16
    • 79952352658 scopus 로고    scopus 로고
    • Dynamics of the Rho-family small GTPases in actin regulation and motility
    • Spiering, D., Hodgson, L. (2011) Dynamics of the Rho-family small GTPases in actin regulation and motility. Cell. Adh. Migr. 5, 170-180.
    • (2011) Cell. Adh. Migr. , vol.5 , pp. 170-180
    • Spiering, D.1    Hodgson, L.2
  • 17
    • 18844449626 scopus 로고    scopus 로고
    • Vav-family proteins in T-cell signalling
    • Tybulewicz, V. L. (2005) Vav-family proteins in T-cell signalling. Curr. Opin. Immunol. 17, 267-274.
    • (2005) Curr. Opin. Immunol. , vol.17 , pp. 267-274
    • Tybulewicz, V.L.1
  • 20
    • 70350427908 scopus 로고    scopus 로고
    • Vav GEFs regulate macrophage morphology and adhesion-induced Rac and Rho activation
    • Bhavsar, P. J., Vigorito, E., Turner, M., Ridley, A. J. (2009) Vav GEFs regulate macrophage morphology and adhesion-induced Rac and Rho activation. Exp. Cell. Res. 315, 3345-3358.
    • (2009) Exp. Cell. Res. , vol.315 , pp. 3345-3358
    • Bhavsar, P.J.1    Vigorito, E.2    Turner, M.3    Ridley, A.J.4
  • 21
    • 0242384071 scopus 로고    scopus 로고
    • Vav proteins, masters of the world of cytoskeleton organization
    • Hornstein, I., Alcover, A., Katzav, S. (2004) Vav proteins, masters of the world of cytoskeleton organization. Cell. Signal. 16, 1-11.
    • (2004) Cell. Signal. , vol.16 , pp. 1-11
    • Hornstein, I.1    Alcover, A.2    Katzav, S.3
  • 23
    • 45549089809 scopus 로고    scopus 로고
    • Isolation of human neutrophils from venous blood
    • Nauseef, W. M. (2007) Isolation of human neutrophils from venous blood. Methods Mol. Biol. 412, 15-20.
    • (2007) Methods Mol. Biol. , vol.412 , pp. 15-20
    • Nauseef, W.M.1
  • 24
    • 33846858648 scopus 로고    scopus 로고
    • Rho GTPase Rac1 is critical for neutrophil migration into the lung
    • Filippi, M. D., Szczur, K., Harris, C. E., Berclaz, P. Y. (2007) Rho GTPase Rac1 is critical for neutrophil migration into the lung. Blood 109, 1257-1264.
    • (2007) Blood , vol.109 , pp. 1257-1264
    • Filippi, M.D.1    Szczur, K.2    Harris, C.E.3    Berclaz, P.Y.4
  • 25
    • 0036223113 scopus 로고    scopus 로고
    • Differentiated HL-60 cells are a valid model system for the analysis of human neutrophil migration and chemotaxis
    • Hauert, A. B., Martinelli, S., Marone, C., Niggli, V. (2002) Differentiated HL-60 cells are a valid model system for the analysis of human neutrophil migration and chemotaxis. Int. J. Biochem. Cell Biol. 34, 838-854.
    • (2002) Int. J. Biochem. Cell Biol. , vol.34 , pp. 838-854
    • Hauert, A.B.1    Martinelli, S.2    Marone, C.3    Niggli, V.4
  • 26
    • 77957018140 scopus 로고    scopus 로고
    • Integrin-induced PIP5K1C kinase polarization regulates neutrophil polarization, directionality, and in vivo infiltration
    • Xu, W., Wang, P., Petri, B., Zhang, Y., Tang, W., Sun, L., Kress, H., Mann, T., Shi, Y., Kubes, P., Wu, D. (2010) Integrin-induced PIP5K1C kinase polarization regulates neutrophil polarization, directionality, and in vivo infiltration. Immunity 33, 340-350.
    • (2010) Immunity , vol.33 , pp. 340-350
    • Xu, W.1    Wang, P.2    Petri, B.3    Zhang, Y.4    Tang, W.5    Sun, L.6    Kress, H.7    Mann, T.8    Shi, Y.9    Kubes, P.10    Wu, D.11
  • 27
    • 7744224229 scopus 로고    scopus 로고
    • Model driven quantification of individual and collective cell migration
    • Rosello, C., Ballet, P., Planus, E., Tracqui, P. (2004) Model driven quantification of individual and collective cell migration. Acta Biotheor. 52, 343-363.
    • (2004) Acta Biotheor. , vol.52 , pp. 343-363
    • Rosello, C.1    Ballet, P.2    Planus, E.3    Tracqui, P.4
  • 28
    • 0030756973 scopus 로고    scopus 로고
    • Role of actin polymerization and adhesion to extracellular matrix in Rac-and Rho-induced cytoskeletal reorganization
    • Machesky, L. M., Hall, A. (1997) Role of actin polymerization and adhesion to extracellular matrix in Rac-and Rho-induced cytoskeletal reorganization. J. Cell Biol. 138, 913-926.
    • (1997) J. Cell Biol. , vol.138 , pp. 913-926
    • Machesky, L.M.1    Hall, A.2
  • 29
    • 33846888273 scopus 로고    scopus 로고
    • Vav family proteins are required for optimal regulation of PLCα 2 by integrin γIIb γ3
    • Pearce, A. C., McCarty, O. J., Calaminus, S. D., Vigorito, E., Turner, M., Watson, S. P. (2007) Vav family proteins are required for optimal regulation of PLCα 2 by integrin γIIb γ3. Biochem. J. 401, 753-761.
    • (2007) Biochem. J. , vol.401 , pp. 753-761
    • Pearce, A.C.1    McCarty, O.J.2    Calaminus, S.D.3    Vigorito, E.4    Turner, M.5    Watson, S.P.6
  • 30
    • 0033531955 scopus 로고    scopus 로고
    • Characterization of Rac and Cdc42 activation in chemoattractant-stimulated human neutrophils using a novel assay for active GTPases
    • Benard, V., Bohl, B. P., Bokoch, G. M. (1999) Characterization of Rac and Cdc42 activation in chemoattractant-stimulated human neutrophils using a novel assay for active GTPases. J. Biol. Chem. 274, 13198-13204.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13198-13204
    • Benard, V.1    Bohl, B.P.2    Bokoch, G.M.3
  • 31
    • 57049151271 scopus 로고    scopus 로고
    • Fluctuations of intracellular forces during cell protrusion
    • Ji, L., Lim, J., Danuser, G. (2008) Fluctuations of intracellular forces during cell protrusion. Nat. Cell Biol. 10, 1393-1400.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1393-1400
    • Ji, L.1    Lim, J.2    Danuser, G.3
  • 32
    • 70350379633 scopus 로고    scopus 로고
    • Regulation of cell migration and morphogenesis by Abl-family kinases: Emerging mechanisms and physiological contexts
    • Bradley, W. D., Koleske, A. J. (2009) Regulation of cell migration and morphogenesis by Abl-family kinases: emerging mechanisms and physiological contexts. J. Cell Sci. 122, 3441-3454.
    • (2009) J. Cell Sci. , vol.122 , pp. 3441-3454
    • Bradley, W.D.1    Koleske, A.J.2
  • 33
    • 33947198166 scopus 로고    scopus 로고
    • The Src family kinases Hck and Fgr regulate neutrophil responses to N-formyl-methionyl-leucyl-phenylalanine
    • Fumagalli, L., Zhang, H., Baruzzi, A., Lowell, C. A., Berton, G. (2007) The Src family kinases Hck and Fgr regulate neutrophil responses to N-formyl-methionyl-leucyl-phenylalanine. J. Immunol. 178, 3874-3885.
    • (2007) J. Immunol. , vol.178 , pp. 3874-3885
    • Fumagalli, L.1    Zhang, H.2    Baruzzi, A.3    Lowell, C.A.4    Berton, G.5
  • 34
    • 33745313872 scopus 로고    scopus 로고
    • The Src family kinases Hck and Fgr are dispensable for inside-out, chemoattractant-induced signaling regulating γ2 integrin affinity and valency in neutrophils, but are required for γ2 integrin-mediated outside-in signaling involved in sustained adhesion
    • Giagulli, C., Ottoboni, L., Caveggion, E., Rossi, B., Lowell, C., Constantin, G., Laudanna, C., Berton, G. (2006) The Src family kinases Hck and Fgr are dispensable for inside-out, chemoattractant-induced signaling regulating γ2 integrin affinity and valency in neutrophils, but are required for γ2 integrin-mediated outside-in signaling involved in sustained adhesion. J. Immunol. 177, 604-611.
    • (2006) J. Immunol. , vol.177 , pp. 604-611
    • Giagulli, C.1    Ottoboni, L.2    Caveggion, E.3    Rossi, B.4    Lowell, C.5    Constantin, G.6    Laudanna, C.7    Berton, G.8
  • 36
    • 0042622251 scopus 로고    scopus 로고
    • Scansite 2.0: Proteomewide prediction of cell signaling interactions using short sequence motifs
    • Obenauer, J. C., Cantley, L. C., Yaffe, M. B. (2003) Scansite 2.0: proteomewide prediction of cell signaling interactions using short sequence motifs. Nucleic Acids Res. 31, 35-41.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 35-41
    • Obenauer, J.C.1    Cantley, L.C.2    Yaffe, M.B.3
  • 37
    • 0032860424 scopus 로고    scopus 로고
    • Regulation of the cytoskeleton and cell adhesion by the Rho family GTPases in mammalian cells
    • Kaibuchi, K., Kuroda, S., Amano, M. (1999) Regulation of the cytoskeleton and cell adhesion by the Rho family GTPases in mammalian cells. Annu. Rev. Biochem. 68, 459-486.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 459-486
    • Kaibuchi, K.1    Kuroda, S.2    Amano, M.3
  • 38
    • 47249127287 scopus 로고    scopus 로고
    • The c-Abl tyrosine kinase regulates actin remodeling at the immune synapse
    • Huang, Y., Comiskey, E. O., Dupree, R. S., Li, S., Koleske, A. J., Burkhardt, J. K. (2008) The c-Abl tyrosine kinase regulates actin remodeling at the immune synapse. Blood 112, 111-119.
    • (2008) Blood , vol.112 , pp. 111-119
    • Huang, Y.1    Comiskey, E.O.2    Dupree, R.S.3    Li, S.4    Koleske, A.J.5    Burkhardt, J.K.6
  • 39
    • 0037018155 scopus 로고    scopus 로고
    • Modulation of the F-actin cytoskeleton by c-Abl tyrosine kinase in cell spreading and neurite extension
    • Woodring, P. J., Litwack, E. D., O'Leary, D. D., Lucero, G. R., Wang, J. Y., Hunter, T. (2002) Modulation of the F-actin cytoskeleton by c-Abl tyrosine kinase in cell spreading and neurite extension. J. Cell Biol. 156, 879-892.
    • (2002) J. Cell Biol. , vol.156 , pp. 879-892
    • Woodring, P.J.1    Litwack, E.D.2    O'Leary, D.D.3    Lucero, G.R.4    Wang, J.Y.5    Hunter, T.6
  • 40
    • 0033974061 scopus 로고    scopus 로고
    • Regulatory and signaling properties of the Vav family
    • Bustelo, X. R. (2000) Regulatory and signaling properties of the Vav family. Mol. Cell. Biol. 20, 1461-1477.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1461-1477
    • Bustelo, X.R.1
  • 41
    • 64849109776 scopus 로고    scopus 로고
    • c-Abl kinase is required for α 2 integrin-mediated neutrophil adhesion
    • Cui, L., Chen, C., Xu, T., Zhang, J., Shang, X., Luo, J., Chen, L., Ba, X., Zeng, X. (2009) c-Abl kinase is required for α 2 integrin-mediated neutrophil adhesion. J. Immunol. 182, 3233-3242.
    • (2009) J. Immunol. , vol.182 , pp. 3233-3242
    • Cui, L.1    Chen, C.2    Xu, T.3    Zhang, J.4    Shang, X.5    Luo, J.6    Chen, L.7    Ba, X.8    Zeng, X.9
  • 43
    • 77954934945 scopus 로고    scopus 로고
    • Tyrosine residues at the carboxyl terminus of Vav1 play an important role in regulation of its biological activity
    • Lazer, G., Pe'er, L., Farago, M., Machida, K., Mayer, B. J., Katzav, S. (2010) Tyrosine residues at the carboxyl terminus of Vav1 play an important role in regulation of its biological activity. J. Biol. Chem. 285, 23075-23085.
    • (2010) J. Biol. Chem. , vol.285 , pp. 23075-23085
    • Lazer, G.1    Pe'er, L.2    Farago, M.3    Machida, K.4    Mayer, B.J.5    Katzav, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.