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Volumn 84, Issue 4, 2008, Pages 1192-1201

Critical role of Lck in L-selectin signaling induced by sulfatides engagement

Author keywords

c Abl kinase; siRNA; ZAP 70 kinase

Indexed keywords

ABELSON KINASE; CD3 ANTIGEN; L SELECTIN; PROTEIN KINASE LCK; PROTEIN KINASE ZAP 70; PROTEIN SH2; PROTEIN SH3; SMALL INTERFERING RNA; SULFATIDE; T LYMPHOCYTE RECEPTOR;

EID: 54249161523     PISSN: 07415400     EISSN: None     Source Type: Journal    
DOI: 10.1189/jlb.0208084     Document Type: Article
Times cited : (12)

References (55)
  • 1
    • 0026342111 scopus 로고
    • Leukocyte-endothelial cell recognition: Three (or more) steps to specificity and diversity
    • Butcher, E. C. (1991) Leukocyte-endothelial cell recognition: three (or more) steps to specificity and diversity. Cell 67, 1033-1036.
    • (1991) Cell , vol.67 , pp. 1033-1036
    • Butcher, E.C.1
  • 2
    • 0027982876 scopus 로고
    • Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm
    • Springer, T. A. (1994) Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm. Cell 76, 301-314.
    • (1994) Cell , vol.76 , pp. 301-314
    • Springer, T.A.1
  • 3
    • 0032904627 scopus 로고    scopus 로고
    • Mechanisms that regulate the function of the selectins and their ligands
    • Blanks, J. E., Vestweber, D. (1999) Mechanisms that regulate the function of the selectins and their ligands. Physiol. Rev. 79, 181-213.
    • (1999) Physiol. Rev , vol.79 , pp. 181-213
    • Blanks, J.E.1    Vestweber, D.2
  • 5
    • 0036775765 scopus 로고    scopus 로고
    • Selectins: Lectins that initiate cell adhesion under flow
    • McEver, R. P. (2002) Selectins: lectins that initiate cell adhesion under flow. Curr. Opin. Cell Biol. 14, 581-586.
    • (2002) Curr. Opin. Cell Biol , vol.14 , pp. 581-586
    • McEver, R.P.1
  • 6
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes, R. O. (2002) Integrins: bidirectional, allosteric signaling machines. Cell 110, 673-687.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 7
    • 0025996029 scopus 로고
    • Leukocyte adhesion molecule-1 (LAM-1, L-selectin) interacts with an inducible endothelial cell ligand to support leukocyte adhesion
    • Spertini, O., Luscinskas, F. W., Kansas, G. S., Munro, J. M., Griffin, J. D., Gimbrone Jr., M. A., Tedder, T. F. (1991) Leukocyte adhesion molecule-1 (LAM-1, L-selectin) interacts with an inducible endothelial cell ligand to support leukocyte adhesion. J. Immunol. 147, 2565-2573.
    • (1991) J. Immunol , vol.147 , pp. 2565-2573
    • Spertini, O.1    Luscinskas, F.W.2    Kansas, G.S.3    Munro, J.M.4    Griffin, J.D.5    Gimbrone Jr., M.A.6    Tedder, T.F.7
  • 9
    • 0027178702 scopus 로고
    • L-selectin can mediate leukocyte rolling in untreated mesenteric venules in vivo independent of E- or P-selectin
    • Ley, K., Tedder, T. F., Kansas, G. S. (1993) L-selectin can mediate leukocyte rolling in untreated mesenteric venules in vivo independent of E- or P-selectin. Blood 82, 1632-1638.
    • (1993) Blood , vol.82 , pp. 1632-1638
    • Ley, K.1    Tedder, T.F.2    Kansas, G.S.3
  • 10
    • 0029042710 scopus 로고
    • L-selectin-deficient mice have impaired leukocyte recruitment into inflammatory sites
    • Tedder, T. F., Steeber, D. A., Pizcueta, P. (1995) L-selectin-deficient mice have impaired leukocyte recruitment into inflammatory sites. J. Exp. Med. 181, 2259-2264.
    • (1995) J. Exp. Med , vol.181 , pp. 2259-2264
    • Tedder, T.F.1    Steeber, D.A.2    Pizcueta, P.3
  • 11
    • 0030884913 scopus 로고    scopus 로고
    • The kinetics of L-selectin tethers and the mechanics of selectin-mediated rolling
    • Alon, R., Chen, S., Puri, K. D., Finger, E. B., Springer, T. A. (1997) The kinetics of L-selectin tethers and the mechanics of selectin-mediated rolling. J. Cell Biol. 138, 1169-1180.
    • (1997) J. Cell Biol , vol.138 , pp. 1169-1180
    • Alon, R.1    Chen, S.2    Puri, K.D.3    Finger, E.B.4    Springer, T.A.5
  • 12
    • 0031279203 scopus 로고    scopus 로고
    • Synergy between L-selectin signaling and chemotactic activation during neutrophil adhesion and transmigration
    • Tsang, Y. T., Neelamegham, S., Hu, Y., Berg, E. L., Burns, A. R., Smith, C. W., Simon, S. I. (1997) Synergy between L-selectin signaling and chemotactic activation during neutrophil adhesion and transmigration. J. Immunol. 159, 4566-4577.
    • (1997) J. Immunol , vol.159 , pp. 4566-4577
    • Tsang, Y.T.1    Neelamegham, S.2    Hu, Y.3    Berg, E.L.4    Burns, A.R.5    Smith, C.W.6    Simon, S.I.7
  • 13
    • 0027933127 scopus 로고
    • Sulfatides trigger increase of cytosolic free calcium and enhanced expression of tumor necrosis factor-α and interleukin-8 mRNA in human neutrophils. Evidence for a role of L-selectin as a signaling molecule
    • Laudanna, C., Constantin, G., Baron, P., Scarpini, E., Scarlato, G., Cabrini, G., Dechecchi, C., Rossi, F., Cassatella, M. A., Berton, G. (1994) Sulfatides trigger increase of cytosolic free calcium and enhanced expression of tumor necrosis factor-α and interleukin-8 mRNA in human neutrophils. Evidence for a role of L-selectin as a signaling molecule. J. Biol. Chem. 269, 4021-4026.
    • (1994) J. Biol. Chem , vol.269 , pp. 4021-4026
    • Laudanna, C.1    Constantin, G.2    Baron, P.3    Scarpini, E.4    Scarlato, G.5    Cabrini, G.6    Dechecchi, C.7    Rossi, F.8    Cassatella, M.A.9    Berton, G.10
  • 14
    • 0028065619 scopus 로고
    • Potentiation of the oxidative burst of human neutrophils. A signaling role for L-selectin
    • Waddell, T. K., Fialkow, L., Chan, C. K., Kishimoto, T. K., Downey, G. P. (1994) Potentiation of the oxidative burst of human neutrophils. A signaling role for L-selectin. J. Biol. Chem. 269, 18485-18491.
    • (1994) J. Biol. Chem , vol.269 , pp. 18485-18491
    • Waddell, T.K.1    Fialkow, L.2    Chan, C.K.3    Kishimoto, T.K.4    Downey, G.P.5
  • 15
    • 0036295875 scopus 로고    scopus 로고
    • Mechanisms of L-selectin-induced activation of the nuclear factor of activated T lymphocytes (NFAT)
    • Brenner, B. C., Kadel, S., Grigorovich, S., Linderkamp, O. (2002) Mechanisms of L-selectin-induced activation of the nuclear factor of activated T lymphocytes (NFAT). Biochem. Biophys. Res. Commun. 291, 237-244.
    • (2002) Biochem. Biophys. Res. Commun , vol.291 , pp. 237-244
    • Brenner, B.C.1    Kadel, S.2    Grigorovich, S.3    Linderkamp, O.4
  • 16
    • 0037432137 scopus 로고    scopus 로고
    • Activation of NF-κ B transcription factor in human neutrophils by sulphatides and L-selectin cross-linking
    • Turutin, D. V., Kubareva, E. A., Pushkareva, M. A., Ullrich, V., Sud'ina, G. F. (2003) Activation of NF-κ B transcription factor in human neutrophils by sulphatides and L-selectin cross-linking. FEBS Lett. 536, 241-245.
    • (2003) FEBS Lett , vol.536 , pp. 241-245
    • Turutin, D.V.1    Kubareva, E.A.2    Pushkareva, M.A.3    Ullrich, V.4    Sud'ina, G.F.5
  • 17
    • 0029075155 scopus 로고
    • Signaling functions of L-selectin. Enhancement of tyrosine phosphorylation and activation of MAP kinase
    • Waddell, T. K., Fialkow, L., Chan, C. K., Kishimoto, T. K., Downey, G. P. (1995) Signaling functions of L-selectin. Enhancement of tyrosine phosphorylation and activation of MAP kinase. J. Biol. Chem. 270, 15403-15411.
    • (1995) J. Biol. Chem , vol.270 , pp. 15403-15411
    • Waddell, T.K.1    Fialkow, L.2    Chan, C.K.3    Kishimoto, T.K.4    Downey, G.P.5
  • 19
    • 0029074732 scopus 로고
    • The cytoplasmic domain of L-selectin interacts with cytoskeletal proteins via α-actinin: Receptor positioning in microvilli does not require interaction with α-actinin
    • Pavalko, F. M., Walker, D. M., Graham, L., Goheen, M., Doerschuk, C. M., Kansas, G. S. (1995) The cytoplasmic domain of L-selectin interacts with cytoskeletal proteins via α-actinin: receptor positioning in microvilli does not require interaction with α-actinin. J. Cell Biol. 129, 1155-1164.
    • (1995) J. Cell Biol , vol.129 , pp. 1155-1164
    • Pavalko, F.M.1    Walker, D.M.2    Graham, L.3    Goheen, M.4    Doerschuk, C.M.5    Kansas, G.S.6
  • 21
    • 0033197965 scopus 로고    scopus 로고
    • Signaling functions of L-selectin in neutrophils: Alterations in the cytoskeleton and colocalization with CD18
    • Simon, S. I., Cherapanov, V., Nadra, I., Waddell, T. K., Seo, S. M., Wang, Q., Doerschuk, C. M., Downey, G. P. (1999) Signaling functions of L-selectin in neutrophils: alterations in the cytoskeleton and colocalization with CD18. J. Immunol. 163, 2891-2901.
    • (1999) J. Immunol , vol.163 , pp. 2891-2901
    • Simon, S.I.1    Cherapanov, V.2    Nadra, I.3    Waddell, T.K.4    Seo, S.M.5    Wang, Q.6    Doerschuk, C.M.7    Downey, G.P.8
  • 22
    • 0028014460 scopus 로고
    • Signal transduction by lymphocyte antigen receptors
    • Weiss, A., Littman, D. R. (1994) Signal transduction by lymphocyte antigen receptors. Cell 76, 263-274.
    • (1994) Cell , vol.76 , pp. 263-274
    • Weiss, A.1    Littman, D.R.2
  • 23
    • 16144364951 scopus 로고    scopus 로고
    • Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation
    • Yamaguchi, H., Hendrickson, W. A. (1996) Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation. Nature 384, 484-489.
    • (1996) Nature , vol.384 , pp. 484-489
    • Yamaguchi, H.1    Hendrickson, W.A.2
  • 24
    • 0031452274 scopus 로고    scopus 로고
    • Structures of Src-family tyrosine kinases
    • Sicheri, F., Kuriyan, J. (1997) Structures of Src-family tyrosine kinases. Curr. Opin. Struct. Biol. 7, 777-785.
    • (1997) Curr. Opin. Struct. Biol , vol.7 , pp. 777-785
    • Sicheri, F.1    Kuriyan, J.2
  • 25
    • 0031439247 scopus 로고    scopus 로고
    • Cellular functions regulated by Src family kinases
    • Thomas, S. M., Brugge, J. S. (1997) Cellular functions regulated by Src family kinases. Annu. Rev. Cell Dev. Biol. 13, 513-609.
    • (1997) Annu. Rev. Cell Dev. Biol , vol.13 , pp. 513-609
    • Thomas, S.M.1    Brugge, J.S.2
  • 26
    • 0026080883 scopus 로고
    • Enhancement of T-cell responsiveness by the lymphocyte-specific tyrosine protein kinase p56lck
    • Abraham, N., Miceli, M. C., Parnes, J. R., Veillette, A. (1991) Enhancement of T-cell responsiveness by the lymphocyte-specific tyrosine protein kinase p56lck. Nature 350, 62-66.
    • (1991) Nature , vol.350 , pp. 62-66
    • Abraham, N.1    Miceli, M.C.2    Parnes, J.R.3    Veillette, A.4
  • 27
    • 0026705903 scopus 로고
    • Genetic evidence for the involvement of the Lck tyrosine kinase in signal transduction through the T cell antigen receptor
    • Straus, D. B., Weiss, A. (1992) Genetic evidence for the involvement of the Lck tyrosine kinase in signal transduction through the T cell antigen receptor. Cell 70, 585-593.
    • (1992) Cell , vol.70 , pp. 585-593
    • Straus, D.B.1    Weiss, A.2
  • 28
    • 0026483786 scopus 로고
    • ZAP-70: A 70 kd protein-tyrosine kinase that associates with the TCR ζ chain
    • Chan, A. C., Iwashima, M., Turck, C. W., Weiss, A. (1992) ZAP-70: a 70 kd protein-tyrosine kinase that associates with the TCR ζ chain. Cell 71, 649-662.
    • (1992) Cell , vol.71 , pp. 649-662
    • Chan, A.C.1    Iwashima, M.2    Turck, C.W.3    Weiss, A.4
  • 29
    • 0036143017 scopus 로고    scopus 로고
    • Reciprocal regulation of lymphocyte activation by tyrosine kinases and phosphatases
    • Hermiston, M. L., Xu, Z., Majeti, R., Weiss, A. (2002) Reciprocal regulation of lymphocyte activation by tyrosine kinases and phosphatases. J. Clin. Invest. 109, 9-14.
    • (2002) J. Clin. Invest , vol.109 , pp. 9-14
    • Hermiston, M.L.1    Xu, Z.2    Majeti, R.3    Weiss, A.4
  • 30
    • 33750986199 scopus 로고    scopus 로고
    • Lck regulates the threshold of activation in primary T cells, while both Lck and Fyn contribute to the magnitude of the extracellular signal-related kinase response
    • Lovatt, M., Filby, A., Parravicini, V., Werlen, G., Palmer, E., Zamoyska, R. (2006) Lck regulates the threshold of activation in primary T cells, while both Lck and Fyn contribute to the magnitude of the extracellular signal-related kinase response. Mol. Cell. Biol. 26, 8655-8665.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 8655-8665
    • Lovatt, M.1    Filby, A.2    Parravicini, V.3    Werlen, G.4    Palmer, E.5    Zamoyska, R.6
  • 32
    • 0027467796 scopus 로고
    • A dominant-negative transgene defines a role for p56lck in thymopoiesis
    • Levin, S. D., Anderson, S. J., Forbush, K. A., Perlmutter, R. M. (1993) A dominant-negative transgene defines a role for p56lck in thymopoiesis. EMBO J. 12, 1671-1680.
    • (1993) EMBO J , vol.12 , pp. 1671-1680
    • Levin, S.D.1    Anderson, S.J.2    Forbush, K.A.3    Perlmutter, R.M.4
  • 33
    • 36248982104 scopus 로고    scopus 로고
    • c-Abl is required for the signaling transduction induced by L-selectin ligation
    • Chen, C., Shang, X., Xu, T., Cui, L. L., Luo, J. X., Ba, X. Q., Hao, S., Zeng, X. L. (2007) c-Abl is required for the signaling transduction induced by L-selectin ligation. Eur. J. Immunol. 37, 3246-3258.
    • (2007) Eur. J. Immunol , vol.37 , pp. 3246-3258
    • Chen, C.1    Shang, X.2    Xu, T.3    Cui, L.L.4    Luo, J.X.5    Ba, X.Q.6    Hao, S.7    Zeng, X.L.8
  • 34
    • 0025791955 scopus 로고
    • Separation of leukocytes: Improved cell purity by fine adjustments of gradient medium density and osmolality
    • Boyum, A., Lovbaug, D., Tresland, L., Nordlie, E. M. (1991) Separation of leukocytes: improved cell purity by fine adjustments of gradient medium density and osmolality. Scand. J. Immunol. 34, 697-712.
    • (1991) Scand. J. Immunol , vol.34 , pp. 697-712
    • Boyum, A.1    Lovbaug, D.2    Tresland, L.3    Nordlie, E.M.4
  • 35
    • 0015822275 scopus 로고
    • Culture of human endothelial cells derived from umbilical veins. Identification by morphologic and immunologic criteria
    • Jaffe, E. A., Nachman, R. L., Becker, C. G., Minick, C. R. (1973) Culture of human endothelial cells derived from umbilical veins. Identification by morphologic and immunologic criteria. J. Clin. Invest. 52, 2745-2764.
    • (1973) J. Clin. Invest , vol.52 , pp. 2745-2764
    • Jaffe, E.A.1    Nachman, R.L.2    Becker, C.G.3    Minick, C.R.4
  • 36
    • 28244434854 scopus 로고    scopus 로고
    • Short-interfering RNA-mediated Lck knockdown results in augmented downstream T cell responses
    • Methi, T., Ngai, J., Mahic, M., Amarzguioui, M., Vang, T., Tasken, K. (2005) Short-interfering RNA-mediated Lck knockdown results in augmented downstream T cell responses. J. Immunol. 175, 7398-7406.
    • (2005) J. Immunol , vol.175 , pp. 7398-7406
    • Methi, T.1    Ngai, J.2    Mahic, M.3    Amarzguioui, M.4    Vang, T.5    Tasken, K.6
  • 38
    • 0032549712 scopus 로고    scopus 로고
    • Calmodulin regulates L-selectin adhesion molecule expression and function through a protease-dependent mechanism
    • Kahn, J., Walcheck, B., Migaki, G. I., Jutila, M. A., Kishimoto, T. K. (1998) Calmodulin regulates L-selectin adhesion molecule expression and function through a protease-dependent mechanism. Cell 92, 809-818.
    • (1998) Cell , vol.92 , pp. 809-818
    • Kahn, J.1    Walcheck, B.2    Migaki, G.I.3    Jutila, M.A.4    Kishimoto, T.K.5
  • 39
    • 0037127291 scopus 로고    scopus 로고
    • The cytoplasmic tail of L-selectin interacts with members of the ezrin-radixinmoesin (ERM) family of proteins: Cell activation-dependent binding of moesin but not ezrin
    • Ivetic, A., Deka, J., Ridley, A., Ager, A. (2002) The cytoplasmic tail of L-selectin interacts with members of the ezrin-radixinmoesin (ERM) family of proteins: cell activation-dependent binding of moesin but not ezrin. J. Biol. Chem. 277, 2321-2329.
    • (2002) J. Biol. Chem , vol.277 , pp. 2321-2329
    • Ivetic, A.1    Deka, J.2    Ridley, A.3    Ager, A.4
  • 40
    • 4043079958 scopus 로고    scopus 로고
    • Mutagenesis of the ezrin-radixin-moesin binding domain of L-selectin tail affects shedding, microvillar positioning, and leukocyte tethering
    • Ivetic, A., Florey, O., Deka, J., Haskard, D. O., Ager, A., Ridley, A. J. (2004) Mutagenesis of the ezrin-radixin-moesin binding domain of L-selectin tail affects shedding, microvillar positioning, and leukocyte tethering. J. Biol. Chem. 279, 33263-33272.
    • (2004) J. Biol. Chem , vol.279 , pp. 33263-33272
    • Ivetic, A.1    Florey, O.2    Deka, J.3    Haskard, D.O.4    Ager, A.5    Ridley, A.J.6
  • 41
    • 0031034050 scopus 로고    scopus 로고
    • Han, J., Das, B., Wei, W., Aelst, L. V., Mosterller, R. D., Khosravi-far, R., Westwick, J. K., Der, C. J., Broek, D. (1997) Lck regulates Vav activation of members of the Rho family of GTPases. Mol. Cell. Biol. 17, 1346-1353.
    • Han, J., Das, B., Wei, W., Aelst, L. V., Mosterller, R. D., Khosravi-far, R., Westwick, J. K., Der, C. J., Broek, D. (1997) Lck regulates Vav activation of members of the Rho family of GTPases. Mol. Cell. Biol. 17, 1346-1353.
  • 42
    • 0038363406 scopus 로고    scopus 로고
    • Selective interaction of LAT (linker of activated T cells) with the open-active form of Lck in lipid rafts reveals a new mechanism for the regulation of Lck in T cells
    • Kabouridis, P. S. (2003) Selective interaction of LAT (linker of activated T cells) with the open-active form of Lck in lipid rafts reveals a new mechanism for the regulation of Lck in T cells. Biochem. J. 371, 907-915.
    • (2003) Biochem. J , vol.371 , pp. 907-915
    • Kabouridis, P.S.1
  • 43
    • 0030459950 scopus 로고    scopus 로고
    • Integrin regulation of c-Abl tyrosine kinase activity and cytoplasmic-nuclear transport
    • Lewis, J. M., Baskaran, R., Taagepera, S., Schwartz, M., Wang, J. (1996) Integrin regulation of c-Abl tyrosine kinase activity and cytoplasmic-nuclear transport. Proc. Natl. Acad. Sci. USA 93, 15174-15179.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 15174-15179
    • Lewis, J.M.1    Baskaran, R.2    Taagepera, S.3    Schwartz, M.4    Wang, J.5
  • 45
    • 0027185152 scopus 로고
    • T cell activation by clustered tyrosine kinases
    • Kolanus, W., Romeo, C., Seed, B. (1993) T cell activation by clustered tyrosine kinases. Cell 74, 171-183.
    • (1993) Cell , vol.74 , pp. 171-183
    • Kolanus, W.1    Romeo, C.2    Seed, B.3
  • 46
    • 0027315182 scopus 로고
    • T cell antigen receptor signal transduction: A tale of tails and cytoplasmic protein-tyrosine kinases
    • Weiss, A. (1993) T cell antigen receptor signal transduction: a tale of tails and cytoplasmic protein-tyrosine kinases. Cell 73, 209-212.
    • (1993) Cell , vol.73 , pp. 209-212
    • Weiss, A.1
  • 47
    • 0035367576 scopus 로고    scopus 로고
    • Proximal protein tyrosine kinases in immunoreceptor signaling
    • Latour, S., Veillette, A. (2001) Proximal protein tyrosine kinases in immunoreceptor signaling. Curr. Opin. Immunol. 13, 299-306.
    • (2001) Curr. Opin. Immunol , vol.13 , pp. 299-306
    • Latour, S.1    Veillette, A.2
  • 48
    • 0029743318 scopus 로고    scopus 로고
    • Role of the Lck Src homology 2 and 3 domains in protein tyrosine phosphorylation
    • Lee-Fruman, K. K., Collins, T. L., Burakoff, S. J. (1996) Role of the Lck Src homology 2 and 3 domains in protein tyrosine phosphorylation. J. Biol. Chem. 271, 25003-25010.
    • (1996) J. Biol. Chem , vol.271 , pp. 25003-25010
    • Lee-Fruman, K.K.1    Collins, T.L.2    Burakoff, S.J.3
  • 49
    • 0029838105 scopus 로고    scopus 로고
    • Identification of the site in the Syk protein tyrosine kinase that binds the SH2 domain of Lck
    • Couture, C., Deckert, M., Williams, S., Russo, F. O., Altman, A., Mustelin, T. (1996) Identification of the site in the Syk protein tyrosine kinase that binds the SH2 domain of Lck. J. Biol. Chem. 271, 24294-24299.
    • (1996) J. Biol. Chem , vol.271 , pp. 24294-24299
    • Couture, C.1    Deckert, M.2    Williams, S.3    Russo, F.O.4    Altman, A.5    Mustelin, T.6
  • 50
    • 0028177590 scopus 로고
    • p56Lck inteacts via its src homology 2 domain with the ZAP-70 kinase
    • Duplay, P., Thome, M., Herve, F., Acuto, O. (1994) p56Lck inteacts via its src homology 2 domain with the ZAP-70 kinase. J. Exp. Med. 179, 1163-1172.
    • (1994) J. Exp. Med , vol.179 , pp. 1163-1172
    • Duplay, P.1    Thome, M.2    Herve, F.3    Acuto, O.4
  • 51
    • 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., Gish, G. O., Babichev, Y., Pawson, T., Isakov, N. (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.O.2    Babichev, Y.3    Pawson, T.4    Isakov, N.5
  • 52
    • 0027436140 scopus 로고
    • Phosphatidylinositol (PI) 3-kinase and PI 4-kinase binding to the CD4-p56lck complex: The p56lck SH3 domain binds to PI 3-kinase but not PI 4-kinase
    • Prasad, K. V., Kapeller, R., Janssen, O., Repke, H., Duke-Cohan, J. S., Cantley, L. C., Rudd, C. E. (1993) Phosphatidylinositol (PI) 3-kinase and PI 4-kinase binding to the CD4-p56lck complex: the p56lck SH3 domain binds to PI 3-kinase but not PI 4-kinase. Mol. Cell. Biol. 13, 7708-7717.
    • (1993) Mol. Cell. Biol , vol.13 , pp. 7708-7717
    • Prasad, K.V.1    Kapeller, R.2    Janssen, O.3    Repke, H.4    Duke-Cohan, J.S.5    Cantley, L.C.6    Rudd, C.E.7
  • 53
    • 0028918408 scopus 로고
    • Ras-dependent induction of cellular responses by constitutively active phosphatidylinositol-3 kinase
    • Hu, Q., Klippel, A., Muslin, A. J., Fantl, W. J., Williams, L. T. (1995) Ras-dependent induction of cellular responses by constitutively active phosphatidylinositol-3 kinase. Science 268, 100-102.
    • (1995) Science , vol.268 , pp. 100-102
    • Hu, Q.1    Klippel, A.2    Muslin, A.J.3    Fantl, W.J.4    Williams, L.T.5
  • 54
    • 0037085436 scopus 로고    scopus 로고
    • The Lck SH3 domain negatively regulates localization to lipid rafts through an interaction with c-Cbl
    • Hawash, I. Y., Kesavan, K. P., Magee, A. I., Geahlen, R. L., Harrison, M. L. (2002) The Lck SH3 domain negatively regulates localization to lipid rafts through an interaction with c-Cbl. J. Biol. Chem. 277, 5683-5691.
    • (2002) J. Biol. Chem , vol.277 , pp. 5683-5691
    • Hawash, I.Y.1    Kesavan, K.P.2    Magee, A.I.3    Geahlen, R.L.4    Harrison, M.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.