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Volumn 193, Issue 8, 2014, Pages 3966-3977

Immunophilins control T lymphocyte adhesion and migration by regulating CrkII binding to C3G

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; CRK SH3 DOMAIN BINDING GUANINE NUCLEOTIDE RELEASING FACTOR; CYAN FLUORESCENT PROTEIN; CYCLOPHILIN A; CYCLOSPORIN A; FIBRONECTIN; FK 506 BINDING PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; IMMUNOPHILIN; PROTEIN CRKI; PROTEIN CRKII; STROMAL CELL DERIVED FACTOR 1ALPHA; TACROLIMUS; UNCLASSIFIED DRUG; YELLOW FLUORESCENT PROTEIN; CRK PROTEIN, HUMAN; CYCLOSPORIN; GUANINE NUCLEOTIDE EXCHANGE FACTOR; ONCOPROTEIN; PROTEIN BINDING; STROMAL CELL DERIVED FACTOR 1;

EID: 84907485549     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1303485     Document Type: Article
Times cited : (19)

References (63)
  • 1
    • 77949828806 scopus 로고    scopus 로고
    • Crk and CrkL adaptor proteins: Networks for physiological and pathological signaling
    • Birge, R. B., C. Kalodimos, F. Inagaki, and S. Tanaka. 2009. Crk and CrkL adaptor proteins: networks for physiological and pathological signaling. Cell Commun. Signal. 7: 13.
    • (2009) Cell Commun. Signal. , vol.7 , pp. 13
    • Birge, R.B.1    Kalodimos, C.2    Inagaki, F.3    Tanaka, S.4
  • 2
    • 0035475308 scopus 로고    scopus 로고
    • Crk family adaptors-signalling complex formation and biological roles
    • Feller, S. M. 2001. Crk family adaptors-signalling complex formation and biological roles. Oncogene 20: 6348-6371.
    • (2001) Oncogene , vol.20 , pp. 6348-6371
    • Feller, S.M.1
  • 3
    • 0033618287 scopus 로고    scopus 로고
    • T cell activation stimulates the association of enzymatically active tyrosine-phosphorylated ZAP-70 with the Crk adapter proteins
    • Gelkop, S., and N. Isakov. 1999. T cell activation stimulates the association of enzymatically active tyrosine-phosphorylated ZAP-70 with the Crk adapter proteins. J. Biol. Chem. 274: 21519-21527.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21519-21527
    • Gelkop, S.1    Isakov, N.2
  • 4
    • 29144441366 scopus 로고    scopus 로고
    • T cell activation-induced CrkII binding to the Zap70 protein tyrosine kinase is mediated by Lck-dependent phosphorylation of Zap70 tyrosine 315
    • Gelkop, S., G. D. Gish, Y. Babichev, T. Pawson, and N. Isakov. 2005. T cell activation-induced CrkII binding to the Zap70 protein tyrosine kinase is mediated by Lck-dependent phosphorylation of Zap70 tyrosine 315. J. Immunol. 175: 8123-8132.
    • (2005) J. Immunol. , vol.175 , pp. 8123-8132
    • Gelkop, S.1    Gish, G.D.2    Babichev, Y.3    Pawson, T.4    Isakov, N.5
  • 5
    • 0036928182 scopus 로고    scopus 로고
    • Mechanism of recruitment of WASP to the immunological synapse and of its activation following TCR ligation
    • Sasahara, Y., R. Rachid, M. J. Byrne, M. A. de la Fuente, R. T. Abraham, N. Ramesh, and R. S. Geha. 2002. Mechanism of recruitment of WASP to the immunological synapse and of its activation following TCR ligation. Mol. Cell 10: 1269-1281.
    • (2002) Mol. Cell , vol.10 , pp. 1269-1281
    • Sasahara, Y.1    Rachid, R.2    Byrne, M.J.3    De La Fuente, M.A.4    Abraham, R.T.5    Ramesh, N.6    Geha, R.S.7
  • 6
    • 85047682875 scopus 로고    scopus 로고
    • Protein kinase C(theta) in T cell activation
    • Isakov, N., and A. Altman. 2002. Protein kinase C(theta) in T cell activation. Annu. Rev. Immunol. 20: 761-794.
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 761-794
    • Isakov, N.1    Altman, A.2
  • 7
    • 80054895503 scopus 로고    scopus 로고
    • A motif in the V3 domain of the kinase PKC-u determines its localization in the immunological synapse and functions in T cells via association with CD28
    • Kong, K. F., T. Yokosuka, A. J. Canonigo-Balancio, N. Isakov, T. Saito, and A. Altman. 2011. A motif in the V3 domain of the kinase PKC-u determines its localization in the immunological synapse and functions in T cells via association with CD28. Nat. Immunol. 12: 1105-1112.
    • (2011) Nat. Immunol. , vol.12 , pp. 1105-1112
    • Kong, K.F.1    Yokosuka, T.2    Canonigo-Balancio, A.J.3    Isakov, N.4    Saito, T.5    Altman, A.6
  • 8
    • 0026895954 scopus 로고
    • The product of the cellular crk gene consists primarily of SH2 and SH3 regions
    • Reichman, C. T., B. J. Mayer, S. Keshav, and H. Hanafusa. 1992. The product of the cellular crk gene consists primarily of SH2 and SH3 regions. Cell Growth Differ. 3: 451-460.
    • (1992) Cell Growth Differ. , vol.3 , pp. 451-460
    • Reichman, C.T.1    Mayer, B.J.2    Keshav, S.3    Hanafusa, H.4
  • 9
    • 0026686182 scopus 로고
    • Two species of human CRK cDNA encode proteins with distinct biological activities
    • Matsuda, M., S. Tanaka, S. Nagata, A. Kojima, T. Kurata, and M. Shibuya. 1992. Two species of human CRK cDNA encode proteins with distinct biological activities. Mol. Cell. Biol. 12: 3482-3489.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3482-3489
    • Matsuda, M.1    Tanaka, S.2    Nagata, S.3    Kojima, A.4    Kurata, T.5    Shibuya, M.6
  • 10
    • 0028243505 scopus 로고
    • C-Abl kinase regulates the protein binding activity of c-Crk
    • Feller, S. M., B. Knudsen, and H. Hanafusa. 1994. c-Abl kinase regulates the protein binding activity of c-Crk. EMBO J. 13: 2341-2351.
    • (1994) EMBO J. , vol.13 , pp. 2341-2351
    • Feller, S.M.1    Knudsen, B.2    Hanafusa, H.3
  • 11
    • 0028916892 scopus 로고
    • Direct demonstration of an intramolecular SH2-phosphotyrosine interaction in the Crk protein
    • Rosen, M. K., T. Yamazaki, G. D. Gish, C. M. Kay, T. Pawson, and L. E. Kay. 1995. Direct demonstration of an intramolecular SH2-phosphotyrosine interaction in the Crk protein. Nature 374: 477-479.
    • (1995) Nature , vol.374 , pp. 477-479
    • Rosen, M.K.1    Yamazaki, T.2    Gish, G.D.3    Kay, C.M.4    Pawson, T.5    Kay, E.L.6
  • 13
    • 33846688095 scopus 로고    scopus 로고
    • Proline cis-trans isomerization controls autoinhibition of a signaling protein
    • Sarkar, P., C. Reichman, T. Saleh, R. B. Birge, and C. G. Kalodimos. 2007. Proline cis-trans isomerization controls autoinhibition of a signaling protein. Mol. Cell 25: 413-426.
    • (2007) Mol. Cell , vol.25 , pp. 413-426
    • Sarkar, P.1    Reichman, C.2    Saleh, T.3    Birge, R.B.4    Kalodimos, C.G.5
  • 14
    • 78650486391 scopus 로고    scopus 로고
    • Structural basis for regulation of the Crk signaling protein by a proline switch
    • Sarkar, P., T. Saleh, S. R. Tzeng, R. B. Birge, and C. G. Kalodimos. 2011. Structural basis for regulation of the Crk signaling protein by a proline switch. Nat. Chem. Biol. 7: 51-57.
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 51-57
    • Sarkar, P.1    Saleh, T.2    Tzeng, S.R.3    Birge, R.B.4    Kalodimos, C.G.5
  • 15
    • 47749132965 scopus 로고    scopus 로고
    • A new twist to adaptor proteins contributes to regulation of lymphocyte cell signaling
    • Isakov, N. 2008. A new twist to adaptor proteins contributes to regulation of lymphocyte cell signaling. Trends Immunol. 29: 388-396.
    • (2008) Trends Immunol. , vol.29 , pp. 388-396
    • Isakov, N.1
  • 16
    • 78650447046 scopus 로고    scopus 로고
    • Structural biology: The twist in Crk signaling revealed
    • Nicholson, L. K., and S. De. 2011. Structural biology: the twist in Crk signaling revealed. Nat. Chem. Biol. 7: 5-6.
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 5-6
    • Nicholson, L.K.1    De, S.2
  • 18
    • 0035903217 scopus 로고    scopus 로고
    • A pair of fluorescent resonance energy transfer-based probes for tyrosine phosphorylation of the CrkII adaptor protein in vivo
    • Kurokawa, K., N. Mochizuki, Y. Ohba, H. Mizuno, A. Miyawaki, and M. Matsuda. 2001. A pair of fluorescent resonance energy transfer-based probes for tyrosine phosphorylation of the CrkII adaptor protein in vivo. J. Biol. Chem. 276: 31305-31310.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31305-31310
    • Kurokawa, K.1    Mochizuki, N.2    Ohba, Y.3    Mizuno, H.4    Miyawaki, A.5    Matsuda, M.6
  • 20
    • 0025868143 scopus 로고
    • Determination of kinetic constants for peptidyl prolyl cis-trans isomerases by an improved spectrophotometric assay
    • Kofron, J. L., P. Kuzmic, V. Kishore, E. Colón-Bonilla, and D. H. Rich. 1991. Determination of kinetic constants for peptidyl prolyl cis-trans isomerases by an improved spectrophotometric assay. Biochemistry 30: 6127-6134.
    • (1991) Biochemistry , vol.30 , pp. 6127-6134
    • Kofron, J.L.1    Kuzmic, P.2    Kishore, V.3    Colón-Bonilla, E.4    Rich, D.H.5
  • 21
    • 0346874407 scopus 로고    scopus 로고
    • A flow cytometric method to detect protein-protein interaction in living cells by directly visualizing donor fluorophore quenching during CFP-.YFP fluorescence resonance energy transfer (FRET)
    • He, L., D. P. Olson, X. Wu, T. S. Karpova, J. G. McNally, and P. E. Lipsky. 2003. A flow cytometric method to detect protein-protein interaction in living cells by directly visualizing donor fluorophore quenching during CFP-.YFP fluorescence resonance energy transfer (FRET). Cytometry A 55: 71-85.
    • (2003) Cytometry A , vol.55 , pp. 71-85
    • He, L.1    Olson, D.P.2    Wu, X.3    Karpova, T.S.4    McNally, J.G.5    Lipsky, P.E.6
  • 22
    • 33644506455 scopus 로고    scopus 로고
    • Recruitment and activation of PLCgamma1 in T cells: A new insight into old domains
    • Braiman, A., M. Barda-Saad, C. L. Sommers, and L. E. Samelson. 2006. Recruitment and activation of PLCgamma1 in T cells: a new insight into old domains. EMBO J. 25: 774-784.
    • (2006) EMBO J. , vol.25 , pp. 774-784
    • Braiman, A.1    Barda-Saad, M.2    Sommers, C.L.3    Samelson, L.E.4
  • 23
    • 84861731097 scopus 로고    scopus 로고
    • Vav1 oncogenic mutation inhibits T cell receptor-induced calcium mobilization through inhibition of phospholipase Cg1 activation
    • Knyazhitsky, M., E. Moas, E. Shaginov, A. Luria, and A. Braiman. 2012. Vav1 oncogenic mutation inhibits T cell receptor-induced calcium mobilization through inhibition of phospholipase Cg1 activation. J. Biol. Chem. 287: 19725-19735.
    • (2012) J. Biol. Chem. , vol.287 , pp. 19725-19735
    • Knyazhitsky, M.1    Moas, E.2    Shaginov, E.3    Luria, A.4    Braiman, A.5
  • 25
    • 21244444702 scopus 로고    scopus 로고
    • Cyclophilin A binds to linear peptide motifs containing a consensus that is present in many human proteins
    • Piotukh, K., W. Gu, M. Kofler, D. Labudde, V. Helms, and C. Freund. 2005. Cyclophilin A binds to linear peptide motifs containing a consensus that is present in many human proteins. J. Biol. Chem. 280: 23668-23674.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23668-23674
    • Piotukh, K.1    Gu, W.2    Kofler, M.3    Labudde, D.4    Helms, V.5    Freund, C.6
  • 26
    • 0027207885 scopus 로고
    • Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B
    • Luban, J., K. L. Bossolt, E. K. Franke, G. V. Kalpana, and S. P. Goff. 1993. Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B. Cell 73: 1067-1078.
    • (1993) Cell , vol.73 , pp. 1067-1078
    • Luban, J.1    Bossolt, K.L.2    Franke, E.K.3    Kalpana, G.V.4    Goff, S.P.5
  • 28
    • 0028335709 scopus 로고
    • The C-terminal SH3 domain of the mouse c-Crk protein negatively regulates tyrosine-phosphorylation of Crk associated p130 in rat 3Y1 cells
    • Ogawa, S., H. Toyoshima, H. Kozutsumi, K. Hagiwara, R. Sakai, T. Tanaka, N. Hirano, H. Mano, Y. Yazaki, and H. Hirai. 1994. The C-terminal SH3 domain of the mouse c-Crk protein negatively regulates tyrosine-phosphorylation of Crk associated p130 in rat 3Y1 cells. Oncogene 9: 1669-1678.
    • (1994) Oncogene , vol.9 , pp. 1669-1678
    • Ogawa, S.1    Toyoshima, H.2    Kozutsumi, H.3    Hagiwara, K.4    Sakai, R.5    Tanaka, T.6    Hirano, N.7    Mano, H.8    Yazaki, Y.9    Hirai, H.10
  • 29
    • 0035931912 scopus 로고    scopus 로고
    • Activation of the focal adhesion kinase signaling pathway by structural alterations in the carboxyl-terminal region of c-Crk II
    • Zvara, A., J. E. Fajardo, M. Escalante, G. Cotton, T. Muir, K. H. Kirsch, and R. B. Birge. 2001. Activation of the focal adhesion kinase signaling pathway by structural alterations in the carboxyl-terminal region of c-Crk II. Oncogene 20: 951-961.
    • (2001) Oncogene , vol.20 , pp. 951-961
    • Zvara, A.1    Fajardo, J.E.2    Escalante, M.3    Cotton, G.4    Muir, T.5    Kirsch, K.H.6    Birge, R.B.7
  • 31
    • 28744435281 scopus 로고    scopus 로고
    • Transactivation of Abl by the Crk II adapter protein requires a PNAY sequence in the Crk C-terminal SH3 domain
    • Reichman, C., K. Singh, Y. Liu, S. Singh, H. Li, J. E. Fajardo, A. Fiser, and R. B. Birge. 2005. Transactivation of Abl by the Crk II adapter protein requires a PNAY sequence in the Crk C-terminal SH3 domain. Oncogene 24: 8187-8199.
    • (2005) Oncogene , vol.24 , pp. 8187-8199
    • Reichman, C.1    Singh, K.2    Liu, Y.3    Singh, S.4    Li, H.5    Fajardo, J.E.6    Fiser, A.7    Birge, R.B.8
  • 33
    • 0028606468 scopus 로고
    • Four proline-rich sequences of the guanine-nucleotide exchange factor C3G bind with unique specificity to the first Src homology 3 domain of Crk
    • Knudsen, B. S., S. M. Feller, and H. Hanafusa. 1994. Four proline-rich sequences of the guanine-nucleotide exchange factor C3G bind with unique specificity to the first Src homology 3 domain of Crk. J. Biol. Chem. 269: 32781-32787.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32781-32787
    • Knudsen, B.S.1    Feller, S.M.2    Hanafusa, H.3
  • 34
    • 0029066326 scopus 로고
    • Affinity and specificity requirements for the first Src homology 3 domain of the Crk proteins
    • Knudsen, B. S., J. Zheng, S. M. Feller, J. P. Mayer, S. K. Burrell, D. Cowburn, and H. Hanafusa. 1995. Affinity and specificity requirements for the first Src homology 3 domain of the Crk proteins. EMBO J. 14: 2191-2198.
    • (1995) EMBO J. , vol.14 , pp. 2191-2198
    • Knudsen, B.S.1    Zheng, J.2    Feller, S.M.3    Mayer, J.P.4    Burrell, S.K.5    Cowburn, D.6    Hanafusa, H.7
  • 37
    • 80051840811 scopus 로고    scopus 로고
    • TC-PTP dephosphorylates the guanine nucleotide exchange factor C3G (RapGEF1) and negatively regulates differentiation of human neuroblastoma cells
    • Mitra, A., S. Kalayarasan, V. Gupta, and V. Radha. 2011. TC-PTP dephosphorylates the guanine nucleotide exchange factor C3G (RapGEF1) and negatively regulates differentiation of human neuroblastoma cells. PLoS One 6: e23681.
    • (2011) PLoS One , vol.6 , pp. e23681
    • Mitra, A.1    Kalayarasan, S.2    Gupta, V.3    Radha, V.4
  • 38
    • 3042721497 scopus 로고    scopus 로고
    • Amplification, up-regulation and over-expression of C3G (CRK SH3 domain-binding guanine nucleotidereleasing factor) in non-small cell lung cancers
    • Hirata, T., H. Nagai, K. Koizumi, K. Okino, A. Harada, M. Onda, T. Nagahata, I. Mikami, K. Hirai, S. Haraguchi, et al. 2004. Amplification, up-regulation and over-expression of C3G (CRK SH3 domain-binding guanine nucleotidereleasing factor) in non-small cell lung cancers. J. Hum. Genet. 49: 290-295.
    • (2004) J. Hum. Genet. , vol.49 , pp. 290-295
    • Hirata, T.1    Nagai, H.2    Koizumi, K.3    Okino, K.4    Harada, A.5    Onda, M.6    Nagahata, T.7    Mikami, I.8    Hirai, K.9    Haraguchi, S.10
  • 39
    • 33845764296 scopus 로고    scopus 로고
    • A guided tour into subcellular colocalization analysis in light microscopy
    • Bolte, S., and F. P. Cordelières. 2006. A guided tour into subcellular colocalization analysis in light microscopy. J. Microsc. 224: 213-232.
    • (2006) J. Microsc. , vol.224 , pp. 213-232
    • Bolte, S.1    Cordelières, F.P.2
  • 41
    • 0032387687 scopus 로고    scopus 로고
    • Regulation of integrin-mediated adhesion during cell migration
    • Cox, E. A., and A. Huttenlocher. 1998. Regulation of integrin-mediated adhesion during cell migration. Microsc. Res. Tech. 43: 412-419.
    • (1998) Microsc. Res. Tech. , vol.43 , pp. 412-419
    • Cox, E.A.1    Huttenlocher, A.2
  • 44
    • 0032569839 scopus 로고    scopus 로고
    • C3G is tyrosinephosphorylated after integrin-mediated cell adhesion in normal but not in Bcr/Abl expressing cells
    • de Jong, R., A. van Wijk, N. Heisterkamp, and J. Groffen. 1998. C3G is tyrosinephosphorylated after integrin-mediated cell adhesion in normal but not in Bcr/Abl expressing cells. Oncogene 17: 2805-2810.
    • (1998) Oncogene , vol.17 , pp. 2805-2810
    • De Jong, R.1    Van Wijk, A.2    Heisterkamp, N.3    Groffen, J.4
  • 45
    • 0033152359 scopus 로고    scopus 로고
    • CrkL activates integrin-mediated hematopoietic cell adhesion through the guanine nucleotide exchange factor C3G
    • Arai, A., Y. Nosaka, H. Kohsaka, N. Miyasaka, and O. Miura. 1999. CrkL activates integrin-mediated hematopoietic cell adhesion through the guanine nucleotide exchange factor C3G. Blood 93: 3713-3722.
    • (1999) Blood , vol.93 , pp. 3713-3722
    • Arai, A.1    Nosaka, Y.2    Kohsaka, H.3    Miyasaka, N.4    Miura, O.5
  • 47
    • 79960298987 scopus 로고    scopus 로고
    • The non-receptor tyrosine kinase Lyn controls neutrophil adhesion by recruiting the CrkL-C3G complex and activating Rap1 at the leading edge
    • He, Y., A. Kapoor, S. Cook, S. Liu, Y. Xiang, C. V. Rao, P. J. Kenis, and F. Wang. 2011. The non-receptor tyrosine kinase Lyn controls neutrophil adhesion by recruiting the CrkL-C3G complex and activating Rap1 at the leading edge. J. Cell Sci. 124: 2153-2164.
    • (2011) J. Cell Sci. , vol.124 , pp. 2153-2164
    • He, Y.1    Kapoor, A.2    Cook, S.3    Liu, S.4    Xiang, Y.5    Rao, C.V.6    Kenis, P.J.7    Wang, F.8
  • 50
    • 0033621446 scopus 로고    scopus 로고
    • The adapter protein Crkl links Cbl to C3G after integrin ligation and enhances cell migration
    • Uemura, N., and J. D. Griffin. 1999. The adapter protein Crkl links Cbl to C3G after integrin ligation and enhances cell migration. J. Biol. Chem. 274: 37525-37532.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37525-37532
    • Uemura, N.1    Griffin, J.D.2
  • 52
    • 47649084675 scopus 로고    scopus 로고
    • C3G regulates cortical neuron migration, preplate splitting and radial glial cell attachment
    • Voss, A. K., J. M. Britto, M. P. Dixon, B. N. Sheikh, C. Collin, S. S. Tan, and T. Thomas. 2008. C3G regulates cortical neuron migration, preplate splitting and radial glial cell attachment. Development 135: 2139-2149.
    • (2008) Development , vol.135 , pp. 2139-2149
    • Voss, A.K.1    Britto, J.M.2    Dixon, M.P.3    Sheikh, B.N.4    Collin, C.5    Tan, S.S.6    Thomas, T.7
  • 53
    • 0031026475 scopus 로고    scopus 로고
    • The chemokine SDF-1 is a chemoattractant for human CD34+ hematopoietic progenitor cells and provides a new mechanism to explain the mobilization of CD34+ progenitors to peripheral blood
    • Aiuti, A., I. J.Webb, C. Bleul, T. Springer, and J. C. Gutierrez-Ramos. 1997. The chemokine SDF-1 is a chemoattractant for human CD34+ hematopoietic progenitor cells and provides a new mechanism to explain the mobilization of CD34+ progenitors to peripheral blood. J. Exp. Med. 185: 111-120.
    • (1997) J. Exp. Med. , vol.185 , pp. 111-120
    • Aiuti, A.1    Webb, I.J.2    Bleul, C.3    Springer, T.4    Gutierrez-Ramos, J.C.5
  • 54
    • 0034210221 scopus 로고    scopus 로고
    • The chemokine SDF-1 activates the integrins LFA-1, VLA-4, and VLA-5 on immature human CD34(+) cells: Role in transendothelial/stromal migration and engraftment of NOD/SCID mice
    • Peled, A., O. Kollet, T. Ponomaryov, I. Petit, S. Franitza, V. Grabovsky, M. M. Slav, A. Nagler, O. Lider, R. Alon, et al. 2000. The chemokine SDF-1 activates the integrins LFA-1, VLA-4, and VLA-5 on immature human CD34(+) cells: role in transendothelial/stromal migration and engraftment of NOD/SCID mice. Blood 95: 3289-3296.
    • (2000) Blood , vol.95 , pp. 3289-3296
    • Peled, A.1    Kollet, O.2    Ponomaryov, T.3    Petit, I.4    Franitza, S.5    Grabovsky, V.6    Slav, M.M.7    Nagler, A.8    Lider, O.9    Alon, R.10
  • 56
    • 0035965340 scopus 로고    scopus 로고
    • T cell activation induces direct binding of the Crk adapter protein to the regulatory subunit of phosphatidylinositol 3-kinase (p85) via a complex mechanism involving the Cbl protein
    • Gelkop, S., Y. Babichev, and N. Isakov. 2001. T cell activation induces direct binding of the Crk adapter protein to the regulatory subunit of phosphatidylinositol 3-kinase (p85) via a complex mechanism involving the Cbl protein. J. Biol. Chem. 276: 36174-36182.
    • (2001) J. Biol. Chem. , Issue.276 , pp. 36174-36182
    • Gelkop, S.1    Babichev, Y.2    Isakov, N.3
  • 57
    • 0345257729 scopus 로고    scopus 로고
    • Involvement of crk adapter proteins in regulation of lymphoid cell functions
    • Gelkop, S., Y. Babichev, R. Kalifa, A. Tamir, and N. Isakov. 2003. Involvement of crk adapter proteins in regulation of lymphoid cell functions. Immunol. Res. 28: 79-91.
    • (2003) Immunol. Res. , vol.28 , pp. 79-91
    • Gelkop, S.1    Babichev, Y.2    Kalifa, R.3    Tamir, A.4    Isakov, N.5
  • 58
    • 0029990069 scopus 로고    scopus 로고
    • Adhesion through the interaction of lymphocyte function-associated antigen-1 with intracellular adhesion molecule-1 induces tyrosine phosphorylation of p130cas and its association with c-CrkII
    • Petruzzelli, L., M. Takami, and R. Herrera. 1996. Adhesion through the interaction of lymphocyte function-associated antigen-1 with intracellular adhesion molecule-1 induces tyrosine phosphorylation of p130cas and its association with c-CrkII. J. Biol. Chem. 271: 7796-7801.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7796-7801
    • Petruzzelli, L.1    Takami, M.2    Herrera, R.3
  • 59
    • 0029876948 scopus 로고    scopus 로고
    • Stimulation through the T cell receptor induces Cbl association with Crk proteins and the guanine nucleotide exchange protein C3G
    • Reedquist, K. A., T. Fukazawa, G. Panchamoorthy, W. Y. Langdon, S. E. Shoelson, B. J. Druker, and H. Band. 1996. Stimulation through the T cell receptor induces Cbl association with Crk proteins and the guanine nucleotide exchange protein C3G. J. Biol. Chem. 271: 8435-8442.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8435-8442
    • Reedquist, K.A.1    Fukazawa, T.2    Panchamoorthy, G.3    Langdon, W.Y.4    Shoelson, S.E.5    Druker, B.J.6    Band, H.7
  • 60
    • 0032930551 scopus 로고    scopus 로고
    • Interaction of hematopoietic progenitor kinase 1 with adapter proteins Crk and CrkL leads to synergistic activation of c-Jun N-terminal kinase
    • Ling, P., Z. Yao, C. F. Meyer, X. S. Wang, W. Oehrl, S. M. Feller, and T. H. Tan. 1999. Interaction of hematopoietic progenitor kinase 1 with adapter proteins Crk and CrkL leads to synergistic activation of c-Jun N-terminal kinase. Mol. Cell. Biol. 19: 1359-1368.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1359-1368
    • Ling, P.1    Yao, Z.2    Meyer, C.F.3    Wang, X.S.4    Oehrl, W.5    Feller, S.M.6    Tan, T.H.7
  • 61
    • 0037592093 scopus 로고    scopus 로고
    • Negative regulation of T cell antigen receptor-mediated Crk-L-C3G signaling and cell adhesion by Cbl-b
    • Zhang, W., Y. Shao, D. Fang, J. Huang, M. S. Jeon, and Y. C. Liu. 2003. Negative regulation of T cell antigen receptor-mediated Crk-L-C3G signaling and cell adhesion by Cbl-b. J. Biol. Chem. 278: 23978-23983.
    • (2003) J. Biol. Chem. , vol.278 , pp. 23978-23983
    • Zhang, W.1    Shao, Y.2    Fang, D.3    Huang, J.4    Jeon, M.S.5    Liu, Y.C.6
  • 62
    • 0026575932 scopus 로고
    • The mechanism of action of cyclosporin A and FK506
    • Schreiber, S. L., and G. R. Crabtree. 1992. The mechanism of action of cyclosporin A and FK506. Immunol. Today 13: 136-142.
    • (1992) Immunol. Today , vol.13 , pp. 136-142
    • Schreiber, S.L.1    Crabtree, G.R.2


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