메뉴 건너뛰기




Volumn 197, Issue 5, 2016, Pages 1945-1956

Pyk2 controls integrin-dependent CTL migration through regulation of de-adhesion

Author keywords

[No Author keywords available]

Indexed keywords

CXCL9 CHEMOKINE; FOCAL ADHESION KINASE 1; INTERCELLULAR ADHESION MOLECULE 1; LYMPHOCYTE FUNCTION ASSOCIATED ANTIGEN 1; SMALL INTERFERING RNA; FOCAL ADHESION KINASE 2; PTK2B PROTEIN, MOUSE;

EID: 84983750690     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1501505     Document Type: Article
Times cited : (14)

References (53)
  • 1
    • 0036595397 scopus 로고    scopus 로고
    • Cytotoxic T lymphocytes: All roads lead to death
    • Barry, M., and R. C. Bleackley. 2002. Cytotoxic T lymphocytes: all roads lead to death. Nat. Rev. Immunol. 2: 401-409.
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 401-409
    • Barry, M.1    Bleackley, R.C.2
  • 2
    • 79957621253 scopus 로고    scopus 로고
    • The insider's guide to leukocyte integrin signalling and function
    • Hogg, N., I. Patzak, and F. Willenbrock. 2011. The insider's guide to leukocyte integrin signalling and function. Nat. Rev. Immunol. 11: 416-426.
    • (2011) Nat. Rev. Immunol. , vol.11 , pp. 416-426
    • Hogg, N.1    Patzak, I.2    Willenbrock, F.3
  • 3
    • 34247891506 scopus 로고    scopus 로고
    • Structural basis of integrin regulation and signaling
    • Luo, B. H., C. V. Carman, and T. A. Springer. 2007. Structural basis of integrin regulation and signaling. Annu. Rev. Immunol. 25: 619-647.
    • (2007) Annu. Rev. Immunol. , vol.25 , pp. 619-647
    • Luo, B.H.1    Carman, C.V.2    Springer, T.A.3
  • 5
    • 67650716492 scopus 로고    scopus 로고
    • The ins and outs of leukocyte integrin signaling
    • Abram, C. L., and C. A. Lowell. 2009. The ins and outs of leukocyte integrin signaling. Annu. Rev. Immunol. 27: 339-362.
    • (2009) Annu. Rev. Immunol. , vol.27 , pp. 339-362
    • Abram, C.L.1    Lowell, C.A.2
  • 6
    • 22244438250 scopus 로고    scopus 로고
    • A talin-dependent LFA-1 focal zone is formed by rapidly migrating T lymphocytes
    • Smith, A., Y. R. Carrasco, P. Stanley, N. Kieffer, F. D. Batista, and N. Hogg. 2005. A talin-dependent LFA-1 focal zone is formed by rapidly migrating T lymphocytes. J. Cell Biol. 170: 141-151.
    • (2005) J. Cell Biol. , vol.170 , pp. 141-151
    • Smith, A.1    Carrasco, Y.R.2    Stanley, P.3    Kieffer, N.4    Batista, F.D.5    Hogg, N.6
  • 8
    • 18244368702 scopus 로고    scopus 로고
    • Focal adhesion kinase-related protein tyrosine kinase Pyk2 in T-cell activation and function
    • Ostergaard, H. L., and T. L. Lysechko. 2005. Focal adhesion kinase-related protein tyrosine kinase Pyk2 in T-cell activation and function. Immunol. Res. 31: 267-282.
    • (2005) Immunol. Res. , vol.31 , pp. 267-282
    • Ostergaard, H.L.1    Lysechko, T.L.2
  • 9
    • 0031571195 scopus 로고    scopus 로고
    • T cell receptor engagement induces tyrosine phosphorylation of FAK and Pyk2 and their association with Lck
    • Berg, N. N., and H. L. Ostergaard. 1997. T cell receptor engagement induces tyrosine phosphorylation of FAK and Pyk2 and their association with Lck. J. Immunol. 159: 1753-1757.
    • (1997) J. Immunol. , vol.159 , pp. 1753-1757
    • Berg, N.N.1    Ostergaard, H.L.2
  • 10
    • 0030992148 scopus 로고    scopus 로고
    • RAFTK, a novel member of the focal adhesion kinase family, is phosphorylated and associates with signaling molecules upon activation of mature T lymphocytes
    • Ganju, R. K., W. C. Hatch, H. Avraham, M. A. Ona, B. Druker, S. Avraham, and J. E. Groopman. 1997. RAFTK, a novel member of the focal adhesion kinase family, is phosphorylated and associates with signaling molecules upon activation of mature T lymphocytes. J. Exp. Med. 185: 1055-1063.
    • (1997) J. Exp. Med. , vol.185 , pp. 1055-1063
    • Ganju, R.K.1    Hatch, W.C.2    Avraham, H.3    Ona, M.A.4    Druker, B.5    Avraham, S.6    Groopman, J.E.7
  • 11
    • 0030902281 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Pyk2 is selectively regulated by Fyn during TCR signaling
    • Qian, D., S. Lev, N. S. van Oers, I. Dikic, J. Schlessinger, and A. Weiss. 1997. Tyrosine phosphorylation of Pyk2 is selectively regulated by Fyn during TCR signaling. J. Exp. Med. 185: 1253-1259.
    • (1997) J. Exp. Med. , vol.185 , pp. 1253-1259
    • Qian, D.1    Lev, S.2    Van Oers, N.S.3    Dikic, I.4    Schlessinger, J.5    Weiss, A.6
  • 12
    • 0031032421 scopus 로고    scopus 로고
    • Cytotoxic T lymphocytes express a beta3 integrin which can induce the phosphorylation of focal adhesion kinase and the related PYK-2
    • Ma, E. A., O. Lou, N. N. Berg, and H. L. Ostergaard. 1997. Cytotoxic T lymphocytes express a beta3 integrin which can induce the phosphorylation of focal adhesion kinase and the related PYK-2. Eur. J. Immunol. 27: 329-335.
    • (1997) Eur. J. Immunol. , vol.27 , pp. 329-335
    • Ma, E.A.1    Lou, O.2    Berg, N.N.3    Ostergaard, H.L.4
  • 14
    • 84905737034 scopus 로고    scopus 로고
    • Functions of the FAK family kinases in T cells: Beyond actin cytoskeletal rearrangement
    • Chapman, N. M., and J. C. Houtman. 2014. Functions of the FAK family kinases in T cells: beyond actin cytoskeletal rearrangement. Immunol. Res. 59: 23-34.
    • (2014) Immunol. Res. , vol.59 , pp. 23-34
    • Chapman, N.M.1    Houtman, J.C.2
  • 16
    • 79251534710 scopus 로고    scopus 로고
    • Pyk2 is required for neutrophil degranulation and host defense responses to bacterial infection
    • Kamen, L. A., J. Schlessinger, and C. A. Lowell. 2011. Pyk2 is required for neutrophil degranulation and host defense responses to bacterial infection. J. Immunol. 186: 1656-1665.
    • (2011) J. Immunol. , vol.186 , pp. 1656-1665
    • Kamen, L.A.1    Schlessinger, J.2    Lowell, C.A.3
  • 17
  • 18
    • 84929207130 scopus 로고    scopus 로고
    • Integrins influence the size and dynamics of signaling microclusters in a Pyk2-dependent manner
    • Steblyanko, M., N. Anikeeva, K. S. Campbell, J. H. Keen, and Y. Sykulev. 2015. Integrins influence the size and dynamics of signaling microclusters in a Pyk2-dependent manner. J. Biol. Chem. 290: 11833-11842.
    • (2015) J. Biol. Chem. , vol.290 , pp. 11833-11842
    • Steblyanko, M.1    Anikeeva, N.2    Campbell, K.S.3    Keen, J.H.4    Sykulev, Y.5
  • 20
    • 84908455770 scopus 로고    scopus 로고
    • A signaling network stimulated by b2 integrin promotes the polarization of lytic granules in cytotoxic cells
    • Zhang, M., M. E. March, W. S. Lane, and E. O. Long. 2014. A signaling network stimulated by b2 integrin promotes the polarization of lytic granules in cytotoxic cells. Sci. Signal. 7: ra96.
    • (2014) Sci. Signal. , vol.7 , pp. ra96
    • Zhang, M.1    March, M.E.2    Lane, W.S.3    Long, E.O.4
  • 21
    • 51249115248 scopus 로고    scopus 로고
    • Proline-rich tyrosine kinase 2 regulates spreading and migration of eosinophils after beta2-integrin adhesion
    • Zhu, X., E. Boetticher, L. Wang, Y. Duan, J. Learoyd, and A. R. Leff. 2008. Proline-rich tyrosine kinase 2 regulates spreading and migration of eosinophils after beta2-integrin adhesion. Am. J. Respir. Cell Mol. Biol. 39: 263-269.
    • (2008) Am. J. Respir. Cell Mol. Biol. , vol.39 , pp. 263-269
    • Zhu, X.1    Boetticher, E.2    Wang, L.3    Duan, Y.4    Learoyd, J.5    Leff, A.R.6
  • 22
    • 69249089318 scopus 로고    scopus 로고
    • B cell receptor-induced phosphorylation of Pyk2 and focal adhesion kinase involves integrins and the rap GTPases and is required for B cell spreading
    • Tse, K. W., M. Dang-Lawson, R. L. Lee, D. Vong, A. Bulic, L. Buckbinder, and M. R. Gold. 2009. B cell receptor-induced phosphorylation of Pyk2 and focal adhesion kinase involves integrins and the rap GTPases and is required for B cell spreading. J. Biol. Chem. 284: 22865-22877.
    • (2009) J. Biol. Chem. , vol.284 , pp. 22865-22877
    • Tse, K.W.1    Dang-Lawson, M.2    Lee, R.L.3    Vong, D.4    Bulic, A.5    Buckbinder, L.6    Gold, M.R.7
  • 23
    • 77952715104 scopus 로고    scopus 로고
    • Hematopoietic Pyk2 regulates migration of differentiated HL-60 cells
    • Wang, L., J. Learoyd, Y. Duan, A. R. Leff, and X. Zhu. 2010. Hematopoietic Pyk2 regulates migration of differentiated HL-60 cells. J. Inflamm. 7: 26.
    • (2010) J. Inflamm. , vol.7 , pp. 26
    • Wang, L.1    Learoyd, J.2    Duan, Y.3    Leff, A.R.4    Zhu, X.5
  • 25
    • 0024365097 scopus 로고
    • Molecular interactions required for triggering alloantigen-specific cytolytic T lymphocytes
    • Kane, K. P., L. A. Sherman, and M. F. Mescher. 1989. Molecular interactions required for triggering alloantigen-specific cytolytic T lymphocytes. J. Immunol. 142: 4153-4160.
    • (1989) J. Immunol. , vol.142 , pp. 4153-4160
    • Kane, K.P.1    Sherman, L.A.2    Mescher, M.F.3
  • 26
    • 0027324758 scopus 로고
    • Activation of CD8-dependent cytotoxic T lymphocyte adhesion and degranulation by peptide class i antigen complexes
    • Kane, K. P., and M. F. Mescher. 1993. Activation of CD8-dependent cytotoxic T lymphocyte adhesion and degranulation by peptide class I antigen complexes. J. Immunol. 150: 4788-4797.
    • (1993) J. Immunol. , vol.150 , pp. 4788-4797
    • Kane, K.P.1    Mescher, M.F.2
  • 27
    • 0032489362 scopus 로고    scopus 로고
    • Paxillin phosphorylation and association with Lck and Pyk2 in anti-CD3-or anti-CD45-stimulated T cells
    • Ostergaard, H. L., O. Lou, C. W. Arendt, and N. N. Berg. 1998. Paxillin phosphorylation and association with Lck and Pyk2 in anti-CD3-or anti-CD45-stimulated T cells. J. Biol. Chem. 273: 5692-5696.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5692-5696
    • Ostergaard, H.L.1    Lou, O.2    Arendt, C.W.3    Berg, N.N.4
  • 28
    • 82755190061 scopus 로고    scopus 로고
    • Paxillin associates with the microtubule cytoskeleton and the immunological synapse of CTL through its leucine-aspartic acid domains and contributes to microtubule organizing center reorientation
    • Robertson, L. K., and H. L. Ostergaard. 2011. Paxillin associates with the microtubule cytoskeleton and the immunological synapse of CTL through its leucine-aspartic acid domains and contributes to microtubule organizing center reorientation. J. Immunol. 187: 5824-5833.
    • (2011) J. Immunol. , vol.187 , pp. 5824-5833
    • Robertson, L.K.1    Ostergaard, H.L.2
  • 29
    • 29144503720 scopus 로고    scopus 로고
    • A role for phosphatidylinositol 3-kinase in TCR-stimulated ERK activation leading to paxillin phosphorylation and CTL degranulation
    • Robertson, L. K., L. R. Mireau, and H. L. Ostergaard. 2005. A role for phosphatidylinositol 3-kinase in TCR-stimulated ERK activation leading to paxillin phosphorylation and CTL degranulation. J. Immunol. 175: 8138-8145.
    • (2005) J. Immunol. , vol.175 , pp. 8138-8145
    • Robertson, L.K.1    Mireau, L.R.2    Ostergaard, H.L.3
  • 30
    • 55549143963 scopus 로고    scopus 로고
    • Trifluoromethylpyrimidine-based inhibitors of proline-rich tyrosine kinase 2 (PYK2): Structure-activity relationships and strategies for the elimination of reactive metabolite formation
    • Walker, D. P., F. C. Bi, A. S. Kalgutkar, J. N. Bauman, S. X. Zhao, J. R. Soglia, G. E. Aspnes, D. W. Kung, J. Klug-McLeod, M. P. Zawistoski, et al. 2008. Trifluoromethylpyrimidine-based inhibitors of proline-rich tyrosine kinase 2 (PYK2): structure-activity relationships and strategies for the elimination of reactive metabolite formation. Bioorg. Med. Chem. Lett. 18: 6071-6077.
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 6071-6077
    • Walker, D.P.1    Bi, F.C.2    Kalgutkar, A.S.3    Bauman, J.N.4    Zhao, S.X.5    Soglia, J.R.6    Aspnes, G.E.7    Kung, D.W.8    Klug-McLeod, J.9    Zawistoski, M.P.10
  • 33
    • 0036521469 scopus 로고    scopus 로고
    • LFA-1 integrin and the microtubular cytoskeleton are involved in the Ca(2)(+)-mediated regulation of the activity of the tyrosine kinase PYK2 in T cells
    • Rodríguez-Fernández, J. L., L. Sánchez-Martín, C. A. de Frutos, D. Sancho, M. Robinson, F. Sánchez-Madrid, and C. Cabañas. 2002. LFA-1 integrin and the microtubular cytoskeleton are involved in the Ca(2)(+)-mediated regulation of the activity of the tyrosine kinase PYK2 in T cells. J. Leukoc. Biol. 71: 520-530.
    • (2002) J. Leukoc. Biol. , vol.71 , pp. 520-530
    • Rodŕguez-Fernández, J.L.1    Sánchez-Martín, L.2    De Frutos, C.A.3    Sancho, D.4    Robinson, M.5    Sánchez-Madrid, F.6    Cabañas, C.7
  • 34
    • 0030944686 scopus 로고    scopus 로고
    • Paxillin is tyrosine-phosphorylated by and preferentially associates with the calcium-dependent tyrosine kinase in rat liver epithelial cells
    • Li, X., and H. S. Earp. 1997. Paxillin is tyrosine-phosphorylated by and preferentially associates with the calcium-dependent tyrosine kinase in rat liver epithelial cells. J. Biol. Chem. 272: 14341-14348.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14341-14348
    • Li, X.1    Earp, H.S.2
  • 36
    • 77957801973 scopus 로고    scopus 로고
    • Regulation of the tyrosine kinase Pyk2 by calcium is through production of reactive oxygen species in cytotoxic T lymphocytes
    • Lysechko, T. L., S. M. Cheung, and H. L. Ostergaard. 2010. Regulation of the tyrosine kinase Pyk2 by calcium is through production of reactive oxygen species in cytotoxic T lymphocytes. J. Biol. Chem. 285: 31174-31184.
    • (2010) J. Biol. Chem. , vol.285 , pp. 31174-31184
    • Lysechko, T.L.1    Cheung, S.M.2    Ostergaard, H.L.3
  • 37
    • 4644328892 scopus 로고    scopus 로고
    • Paxillin: Adapting to change
    • Brown, M. C., and C. E. Turner. 2004. Paxillin: adapting to change. Physiol. Rev. 84: 1315-1339.
    • (2004) Physiol. Rev. , vol.84 , pp. 1315-1339
    • Brown, M.C.1    Turner, C.E.2
  • 38
    • 0030771904 scopus 로고    scopus 로고
    • Differential signaling by the focal adhesion kinase and cell adhesion kinase beta
    • Schaller, M. D., and T. Sasaki. 1997. Differential signaling by the focal adhesion kinase and cell adhesion kinase beta. J. Biol. Chem. 272: 25319-25325.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25319-25325
    • Schaller, M.D.1    Sasaki, T.2
  • 39
    • 0031846188 scopus 로고    scopus 로고
    • Expression and characterization of splice variants of PYK2, a focal adhesion kinase-related protein
    • Xiong, W. C., M. Macklem, and J. T. Parsons. 1998. Expression and characterization of splice variants of PYK2, a focal adhesion kinase-related protein. J. Cell Sci. 111: 1981-1991.
    • (1998) J. Cell Sci. , vol.111 , pp. 1981-1991
    • Xiong, W.C.1    Macklem, M.2    Parsons, J.T.3
  • 40
    • 33845687683 scopus 로고    scopus 로고
    • RAFTK/Pyk2 regulates EGF-induced PC12 cell spreading and movement
    • Park, S. Y., H. Li, and S. Avraham. 2007. RAFTK/Pyk2 regulates EGF-induced PC12 cell spreading and movement. Cell. Signal. 19: 289-300.
    • (2007) Cell. Signal. , vol.19 , pp. 289-300
    • Park, S.Y.1    Li, H.2    Avraham, S.3
  • 42
    • 0032486285 scopus 로고    scopus 로고
    • Identification of a new Pyk2 isoform implicated in chemokine and antigen receptor signaling
    • Dikic, I., I. Dikic, and J. Schlessinger. 1998. Identification of a new Pyk2 isoform implicated in chemokine and antigen receptor signaling. J. Biol. Chem. 273: 14301-14308.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14301-14308
    • Dikic, I.1    Dikic, I.2    Schlessinger, J.3
  • 44
    • 79952091851 scopus 로고    scopus 로고
    • CXCR3 in T cell function
    • Groom, J. R., and A. D. Luster. 2011. CXCR3 in T cell function. Exp. Cell Res. 317: 620-631.
    • (2011) Exp. Cell Res. , vol.317 , pp. 620-631
    • Groom, J.R.1    Luster, A.D.2
  • 45
    • 0031202175 scopus 로고    scopus 로고
    • Microtubule retraction into the uropod and its role in T cell polarization and motility
    • Ratner, S., W. S. Sherrod, and D. Lichlyter. 1997. Microtubule retraction into the uropod and its role in T cell polarization and motility. J. Immunol. 159: 1063-1067.
    • (1997) J. Immunol. , vol.159 , pp. 1063-1067
    • Ratner, S.1    Sherrod, W.S.2    Lichlyter, D.3
  • 46
    • 78649788899 scopus 로고    scopus 로고
    • Calpain 2 controls turnover of LFA-1 adhesions on migrating T lymphocytes
    • Svensson, L., A. McDowall, K. M. Giles, P. Stanley, S. Feske, and N. Hogg. 2010. Calpain 2 controls turnover of LFA-1 adhesions on migrating T lymphocytes. PLoS One 5: e15090.
    • (2010) PLoS One , vol.5 , pp. e15090
    • Svensson, L.1    McDowall, A.2    Giles, K.M.3    Stanley, P.4    Feske, S.5    Hogg, N.6
  • 47
    • 84881164957 scopus 로고    scopus 로고
    • A role for the protein tyrosine phosphatase CD45 in macrophage adhesion through the regulation of paxillin degradation
    • St-Pierre, J., and H. L. Ostergaard. 2013. A role for the protein tyrosine phosphatase CD45 in macrophage adhesion through the regulation of paxillin degradation. PLoS One 8: e71531.
    • (2013) PLoS One , vol.8 , pp. e71531
    • St-Pierre, J.1    Ostergaard, H.L.2
  • 49
    • 26244434596 scopus 로고    scopus 로고
    • Regulating cell migration: Calpains make the cut
    • Franco, S. J., and A. Huttenlocher. 2005. Regulating cell migration: calpains make the cut. J. Cell Sci. 118: 3829-3838.
    • (2005) J. Cell Sci. , vol.118 , pp. 3829-3838
    • Franco, S.J.1    Huttenlocher, A.2
  • 50
    • 0030669961 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Crk-associated substrates by focal adhesion kinase: A putative mechanism for the integrin-mediated tyrosine phosphorylation of Crk-associated substrates
    • Tachibana, K., T. Urano, H. Fujita, Y. Ohashi, K. Kamiguchi, S. Iwata, H. Hirai, and C. Morimoto. 1997. Tyrosine phosphorylation of Crk-associated substrates by focal adhesion kinase: a putative mechanism for the integrin-mediated tyrosine phosphorylation of Crk-associated substrates. J. Biol. Chem. 272: 29083-29090.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29083-29090
    • Tachibana, K.1    Urano, T.2    Fujita, H.3    Ohashi, Y.4    Kamiguchi, K.5    Iwata, S.6    Hirai, H.7    Morimoto, C.8
  • 52
    • 77952321910 scopus 로고    scopus 로고
    • T cell receptor activation leads to two distinct phases of Pyk2 activation and actin cytoskeletal rearrangement in human T cells
    • Collins, M., R. R. Bartelt, and J. C. Houtman. 2010. T cell receptor activation leads to two distinct phases of Pyk2 activation and actin cytoskeletal rearrangement in human T cells. Mol. Immunol. 47: 1665-1674.
    • (2010) Mol. Immunol. , vol.47 , pp. 1665-1674
    • Collins, M.1    Bartelt, R.R.2    Houtman, J.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.