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Volumn 178, Issue 4, 2007, Pages 675-686

Src kinase activity and SH2 domain regulate the dynamics of Src association with lipid and protein targets

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINO 7 TERT BUTYL 5 (4 METHYLPHENYL)PYRAZOLO[3,4 D]PYRIMIDINE; GREEN FLUORESCENT PROTEIN; PAXILLIN; PROTEIN SH2; PROTEIN TYROSINE KINASE; STEROID RECEPTOR COACTIVATOR 1;

EID: 34547932452     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.200701133     Document Type: Article
Times cited : (52)

References (60)
  • 1
    • 0034627767 scopus 로고    scopus 로고
    • Src family tyrosine kinases and growth factor signaling
    • Abram, C.L., and S.A. Courtneidge. 2000. Src family tyrosine kinases and growth factor signaling. Exp. Cell Res. 254:1-13.
    • (2000) Exp. Cell Res , vol.254 , pp. 1-13
    • Abram, C.L.1    Courtneidge, S.A.2
  • 2
    • 0028818769 scopus 로고
    • Characterization of two activated mutants of human pp60c-src that escape c-Src kinase regulation by distinct mechanisms
    • Bjorge, J.D., C. Bellagamba, H.C. Cheng, A. Tanaka, J.H. Wang, and D.J. Fujita. 1995. Characterization of two activated mutants of human pp60c-src that escape c-Src kinase regulation by distinct mechanisms. J. Biol. Chem. 270:24222-24228.
    • (1995) J. Biol. Chem , vol.270 , pp. 24222-24228
    • Bjorge, J.D.1    Bellagamba, C.2    Cheng, H.C.3    Tanaka, A.4    Wang, J.H.5    Fujita, D.J.6
  • 3
    • 0034693806 scopus 로고    scopus 로고
    • Selected glimpses into the activation and function of Src kinase
    • Bjorge, J.D., A. Jakymiw, and D.J. Fujita. 2000. Selected glimpses into the activation and function of Src kinase. Oncogene. 19:5620-5635.
    • (2000) Oncogene , vol.19 , pp. 5620-5635
    • Bjorge, J.D.1    Jakymiw, A.2    Fujita, D.J.3
  • 4
    • 0029904262 scopus 로고    scopus 로고
    • Requirement for c-Src catalytic activity and the SH3 domain in platelet-derived growth factor BB and epidermal growth factor mitogenic signaling
    • Broome, M.A., and T. Hunter. 1996. Requirement for c-Src catalytic activity and the SH3 domain in platelet-derived growth factor BB and epidermal growth factor mitogenic signaling. J. Biol. Chem. 271:16798-16806.
    • (1996) J. Biol. Chem , vol.271 , pp. 16798-16806
    • Broome, M.A.1    Hunter, T.2
  • 5
    • 0022504694 scopus 로고
    • The absence of myristic acid decreases membrane binding of p60src but does not affect tyrosine protein kinase activity
    • Buss, J.E., M.P. Kamps, K. Gould, and B.M. Sefton. 1986. The absence of myristic acid decreases membrane binding of p60src but does not affect tyrosine protein kinase activity. J. Virol. 58:468-474.
    • (1986) J. Virol , vol.58 , pp. 468-474
    • Buss, J.E.1    Kamps, M.P.2    Gould, K.3    Sefton, B.M.4
  • 6
    • 0036205320 scopus 로고    scopus 로고
    • Src catalytic but not scaffolding function is needed for integrin-regulated tyrosine phosphorylation, cell migration, and cell spreading
    • Cary, L.A., R.A. Klinghoffer, C. Sachsenmaier, and J.A. Cooper. 2002. Src catalytic but not scaffolding function is needed for integrin-regulated tyrosine phosphorylation, cell migration, and cell spreading. Mol. Cell. Biol. 22:2427-2440.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 2427-2440
    • Cary, L.A.1    Klinghoffer, R.A.2    Sachsenmaier, C.3    Cooper, J.A.4
  • 7
    • 33749544508 scopus 로고    scopus 로고
    • Transient anchorage of cross-linked glycosyl-phosphatidylinositol-anchored proteins depends on cholesterol, Src family kinases, caveolin, and phosphoinositides
    • Chen, Y., Y.R. Thelin, B. Yang, S.L. Milgram, and K. Jacobson. 2006. Transient anchorage of cross-linked glycosyl-phosphatidylinositol-anchored proteins depends on cholesterol, Src family kinases, caveolin, and phosphoinositides. J. Cell Biol. 175:169-178.
    • (2006) J. Cell Biol , vol.175 , pp. 169-178
    • Chen, Y.1    Thelin, Y.R.2    Yang, B.3    Milgram, S.L.4    Jacobson, K.5
  • 8
    • 29144452123 scopus 로고    scopus 로고
    • Endogenous and synthetic inhibitors of the Src-family protein tyrosine kinases
    • Chong, Y.P., K.K. Ia, T.D. Mulhern, and H.C. Cheng. 2005. Endogenous and synthetic inhibitors of the Src-family protein tyrosine kinases. Biochim. Biophys. Acta. 1754:210-220.
    • (2005) Biochim. Biophys. Acta , vol.1754 , pp. 210-220
    • Chong, Y.P.1    Ia, K.K.2    Mulhern, T.D.3    Cheng, H.C.4
  • 9
    • 0036547763 scopus 로고    scopus 로고
    • Role of Src in signal transduction pathways
    • Courtneidge, S.A. 2002. Role of Src in signal transduction pathways. Biochem. Soc. Trans. 30:11-17.
    • (2002) Biochem. Soc. Trans , vol.30 , pp. 11-17
    • Courtneidge, S.A.1
  • 10
  • 11
    • 0034630157 scopus 로고    scopus 로고
    • Crk-associated substrate p130(Cas) interacts with nephrocystin and both proteins localize to cell-cell contacts of polarized epithelial cells
    • Donaldson, J.C., P.J. Dempsey, S. Reddy, A.H. Bouton, R.J. Coffey, and S.K. Hanks. 2000. Crk-associated substrate p130(Cas) interacts with nephrocystin and both proteins localize to cell-cell contacts of polarized epithelial cells. Exp. Cell Res. 256:168-178.
    • (2000) Exp. Cell Res , vol.256 , pp. 168-178
    • Donaldson, J.C.1    Dempsey, P.J.2    Reddy, S.3    Bouton, A.H.4    Coffey, R.J.5    Hanks, S.K.6
  • 12
    • 0007443841 scopus 로고
    • Translational diffusion of membrane proteins
    • P. Yeagle, editor. CRC Press, Boca Raton, FL
    • Edidin, M. 1992. Translational diffusion of membrane proteins. In The structure of biological membranes. P. Yeagle, editor. CRC Press, Boca Raton, FL. 539-572.
    • (1992) The structure of biological membranes , pp. 539-572
    • Edidin, M.1
  • 13
    • 0028941630 scopus 로고
    • Mutational analysis of the Src SH3 domain: The same residues of the ligand binding surface are important for intra- and intermolecular interactions
    • Erpel, T., G. Superti-Furga, and S.A. Courtneidge. 1995. Mutational analysis of the Src SH3 domain: the same residues of the ligand binding surface are important for intra- and intermolecular interactions. EMBO J. 14:963-975.
    • (1995) EMBO J , vol.14 , pp. 963-975
    • Erpel, T.1    Superti-Furga, G.2    Courtneidge, S.A.3
  • 14
    • 0027411585 scopus 로고    scopus 로고
    • Felder, S., M. Zhou, P. Hu, J. Urena, A. Ullrich, M. Chaudhuri, M. White, S.E. Shoelson, and J. Schlessinger. 1993. SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange. Mol. Cell. Biol. 13:1449-1455.
    • Felder, S., M. Zhou, P. Hu, J. Urena, A. Ullrich, M. Chaudhuri, M. White, S.E. Shoelson, and J. Schlessinger. 1993. SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange. Mol. Cell. Biol. 13:1449-1455.
  • 15
    • 1842584776 scopus 로고    scopus 로고
    • Newest findings on the oldest oncogene; how activated src does it
    • Frame, M.C. 2004. Newest findings on the oldest oncogene; how activated src does it. J. Cell Sci. 117:989-998.
    • (2004) J. Cell Sci , vol.117 , pp. 989-998
    • Frame, M.C.1
  • 16
    • 0025977037 scopus 로고
    • Eukaryotic proteins expressed in Escherichia coli: An improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase
    • Guan, K.L., and J.E. Dixon. 1991. Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase. Anal. Biochem. 192:262-267.
    • (1991) Anal. Biochem , vol.192 , pp. 262-267
    • Guan, K.L.1    Dixon, J.E.2
  • 18
    • 22144479017 scopus 로고    scopus 로고
    • Ras plasma membrane signalling platforms
    • Hancock, J.F., and R.G. Parton. 2005. Ras plasma membrane signalling platforms. Biochem. J. 389:1-11.
    • (2005) Biochem. J , vol.389 , pp. 1-11
    • Hancock, J.F.1    Parton, R.G.2
  • 19
    • 33748981090 scopus 로고    scopus 로고
    • FRAP beam-size analysis to measure palmitoylation-dependent membrane association dynamics and micro-domain partitioning of Ras proteins
    • Henis, Y.I., B. Rotblat, and Y. Kloog. 2006. FRAP beam-size analysis to measure palmitoylation-dependent membrane association dynamics and micro-domain partitioning of Ras proteins. Methods. 40:183-190.
    • (2006) Methods , vol.40 , pp. 183-190
    • Henis, Y.I.1    Rotblat, B.2    Kloog, Y.3
  • 21
    • 0029005840 scopus 로고
    • Revisiting the fluid mosaic model of membranes
    • Jacobson, K., E.D. Sheets, and R. Simson. 1995. Revisiting the fluid mosaic model of membranes. Science. 268:1441-1442.
    • (1995) Science , vol.268 , pp. 1441-1442
    • Jacobson, K.1    Sheets, E.D.2    Simson, R.3
  • 22
    • 0033998793 scopus 로고    scopus 로고
    • The role of lipid rafts in T cell antigen receptor (TCR) signalling
    • Janes, P.W., S.C. Ley, A.I. Magee, and P.S. Kabouridis. 2000. The role of lipid rafts in T cell antigen receptor (TCR) signalling. Semin. Immunol. 12:23-34.
    • (2000) Semin. Immunol , vol.12 , pp. 23-34
    • Janes, P.W.1    Ley, S.C.2    Magee, A.I.3    Kabouridis, P.S.4
  • 23
    • 0022654122 scopus 로고
    • Neither arginine nor histidine can carry out the function of lysine-295 in the ATP-binding site of p60src
    • Kamps, M.P., and B.M. Sefton. 1986. Neither arginine nor histidine can carry out the function of lysine-295 in the ATP-binding site of p60src. Mol. Cell. Biol. 6:751-757.
    • (1986) Mol. Cell. Biol , vol.6 , pp. 751-757
    • Kamps, M.P.1    Sefton, B.M.2
  • 24
    • 0021151496 scopus 로고
    • Direct evidence that oncogenic tyrosine kinases and cyclic AMP-dependent protein kinase have homologous ATP-binding sites
    • Kamps, M.P., S.S. Taylor, and B.M. Sefton. 1984. Direct evidence that oncogenic tyrosine kinases and cyclic AMP-dependent protein kinase have homologous ATP-binding sites. Nature. 310:589-592.
    • (1984) Nature , vol.310 , pp. 589-592
    • Kamps, M.P.1    Taylor, S.S.2    Sefton, B.M.3
  • 25
    • 0022398521 scopus 로고
    • Mutation of NH2-terminal glycine of p60src prevents both myristoylation and morphological transformation
    • Kamps, M.P., J.E. Buss, and B.M. Sefton. 1985. Mutation of NH2-terminal glycine of p60src prevents both myristoylation and morphological transformation. Proc. Natl. Acad. Sci. USA. 82:4625-4628.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4625-4628
    • Kamps, M.P.1    Buss, J.E.2    Sefton, B.M.3
  • 26
    • 0025877229 scopus 로고
    • The SH2 and SH3 domains of pp60src direct stable association with tyrosine phosphorylated proteins p130 and p110
    • Kanner, S.B., A.B. Reynolds, H.C. Wang, R.R. Vines, and J.T. Parsons. 1991. The SH2 and SH3 domains of pp60src direct stable association with tyrosine phosphorylated proteins p130 and p110. EMBO J. 10:1689-1698.
    • (1991) EMBO J , vol.10 , pp. 1689-1698
    • Kanner, S.B.1    Reynolds, A.B.2    Wang, H.C.3    Vines, R.R.4    Parsons, J.T.5
  • 27
    • 0028151515 scopus 로고
    • Association of the amino-terminal half of c-Src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527
    • Kaplan, K.B., K.B. Bibbins, J.R. Swedlow, M. Arnaud, D.O. Morgan, and H.E. Varmus. 1994. Association of the amino-terminal half of c-Src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527. EMBO J. 13:4745-4756.
    • (1994) EMBO J , vol.13 , pp. 4745-4756
    • Kaplan, K.B.1    Bibbins, K.B.2    Swedlow, J.R.3    Arnaud, M.4    Morgan, D.O.5    Varmus, H.E.6
  • 28
    • 9644284452 scopus 로고    scopus 로고
    • Single-molecule tracking of membrane molecules: Plasma membrane compartmentalization and dynamic assembly of raft-philic signaling molecules
    • Kusumi, A., H. Ike, C. Nakada, K. Murase, and T. Fujiwara. 2005. Single-molecule tracking of membrane molecules: plasma membrane compartmentalization and dynamic assembly of raft-philic signaling molecules. Semin. Immunol. 17:3-21.
    • (2005) Semin. Immunol , vol.17 , pp. 3-21
    • Kusumi, A.1    Ike, H.2    Nakada, C.3    Murase, K.4    Fujiwara, T.5
  • 30
    • 27744432013 scopus 로고    scopus 로고
    • Temporally resolved interactions between antigen-stimulated IgE receptors and Lyn kinase on living cells
    • Larson, D.R., J.A. Gosse, D.A. Holowka, B.A. Baird, and W.W. Webb. 2005. Temporally resolved interactions between antigen-stimulated IgE receptors and Lyn kinase on living cells. J. Cell Biol. 171:527-536.
    • (2005) J. Cell Biol , vol.171 , pp. 527-536
    • Larson, D.R.1    Gosse, J.A.2    Holowka, D.A.3    Baird, B.A.4    Webb, W.W.5
  • 31
    • 0037072827 scopus 로고    scopus 로고
    • 19) is localized near focal adhesions, remains associated with lipid rafts/caveolae, but no longer forms a high molecular mass hetero-oligomer with caveolin-1
    • 19) is localized near focal adhesions, remains associated with lipid rafts/caveolae, but no longer forms a high molecular mass hetero-oligomer with caveolin-1. J. Biol. Chem. 277:34556-34567.
    • (2002) J. Biol. Chem , vol.277 , pp. 34556-34567
    • Lee, H.1    Park, D.S.2    Wang, X.B.3    Scherer, P.E.4    Schwartz, P.E.5    Lisanti, M.P.6
  • 32
    • 24044540256 scopus 로고    scopus 로고
    • Specificity and versatility of SH3 and other proline-recognition domains: Structural basis and implications for cellular signal transduction
    • Li, S.S. 2005. Specificity and versatility of SH3 and other proline-recognition domains: structural basis and implications for cellular signal transduction. Biochem. J. 390:641-653.
    • (2005) Biochem. J , vol.390 , pp. 641-653
    • Li, S.S.1
  • 33
    • 33745185987 scopus 로고    scopus 로고
    • The human and mouse complement of SH2 domain proteins - establishing the boundaries of phosphotyrosine signaling
    • Liu, B.A., K. Jablonowski, M. Raina, M. Arce, T. Pawson, and P.D. Nash. 2006. The human and mouse complement of SH2 domain proteins - establishing the boundaries of phosphotyrosine signaling. Mol. Cell. 22:851-868.
    • (2006) Mol. Cell , vol.22 , pp. 851-868
    • Liu, B.A.1    Jablonowski, K.2    Raina, M.3    Arce, M.4    Pawson, T.5    Nash, P.D.6
  • 35
    • 0035030510 scopus 로고    scopus 로고
    • SH3 domains: Complexity in moderation
    • Mayer, B.J. 2001. SH3 domains: complexity in moderation. J. Cell Sci. 114:1253-1263.
    • (2001) J. Cell Sci , vol.114 , pp. 1253-1263
    • Mayer, B.J.1
  • 36
    • 0029257493 scopus 로고
    • Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases
    • Mayer, B.J., H. Hirai, and R. Sakai. 1995. Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases. Curr. Biol. 5:296-305.
    • (1995) Curr. Biol , vol.5 , pp. 296-305
    • Mayer, B.J.1    Hirai, H.2    Sakai, R.3
  • 37
    • 0033525077 scopus 로고    scopus 로고
    • Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts. Many raft proteins are acylated, while few are prenylated
    • Melkonian, K.A., A.G. Ostermeyer, J.Z. Chen, M.G. Roth, and D.A. Brown. 1999. Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts. Many raft proteins are acylated, while few are prenylated. J. Biol. Chem. 274:3910-3917.
    • (1999) J. Biol. Chem , vol.274 , pp. 3910-3917
    • Melkonian, K.A.1    Ostermeyer, A.G.2    Chen, J.Z.3    Roth, M.G.4    Brown, D.A.5
  • 38
    • 0142039937 scopus 로고    scopus 로고
    • Lipid-dependent recruitment of neuronal Src to lipid rafts in the brain
    • Mukherjee, A., L. Arnaud, and J.A. Cooper. 2003. Lipid-dependent recruitment of neuronal Src to lipid rafts in the brain. J. Biol. Chem. 278:40806-40814.
    • (2003) J. Biol. Chem , vol.278 , pp. 40806-40814
    • Mukherjee, A.1    Arnaud, L.2    Cooper, J.A.3
  • 39
    • 0028485085 scopus 로고
    • High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides
    • Musacchio, A., M. Saraste, and M. Wilmanns. 1994. High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides. Nat. Struct. Biol. 1:546-551.
    • (1994) Nat. Struct. Biol , vol.1 , pp. 546-551
    • Musacchio, A.1    Saraste, M.2    Wilmanns, M.3
  • 40
    • 0035958959 scopus 로고    scopus 로고
    • Processive phosphorylation of p130Cas by Src depends on SH3-polyproline interactions
    • Pellicena, P., and W.T. Miller. 2001. Processive phosphorylation of p130Cas by Src depends on SH3-polyproline interactions. J. Biol. Chem. 276:28190-28196.
    • (2001) J. Biol. Chem , vol.276 , pp. 28190-28196
    • Pellicena, P.1    Miller, W.T.2
  • 41
    • 0002427909 scopus 로고
    • Measurement of lateral diffusion by fluorescence photobleaching recovery
    • D.M. Weir, L.A. Herzenberg, C.C. Blackwell, and L.A. Herzenberg, editors. Blackwell Scientific Publications, Edinburgh
    • Petersen, N.O., S. Felder, and E.L. Elson. 1986. Measurement of lateral diffusion by fluorescence photobleaching recovery. In Handbook of Experimental Immunology. D.M. Weir, L.A. Herzenberg, C.C. Blackwell, and L.A. Herzenberg, editors. Blackwell Scientific Publications, Edinburgh. 24.21-24.23.
    • (1986) Handbook of Experimental Immunology
    • Petersen, N.O.1    Felder, S.2    Elson, E.L.3
  • 42
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
    • Resh, M.D. 1999. Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim. Biophys. Acta. 1451:1-16.
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 43
    • 0029014901 scopus 로고
    • Myristoylation and differential palmitoylation of the HCK protein-tyrosine kinases govern their attachment to membranes and association with caveolae
    • Robbins, S.M., N.A. Quintrell, and J.M. Bishop. 1995. Myristoylation and differential palmitoylation of the HCK protein-tyrosine kinases govern their attachment to membranes and association with caveolae. Mol. Cell. Biol. 15:3507-3515.
    • (1995) Mol. Cell. Biol , vol.15 , pp. 3507-3515
    • Robbins, S.M.1    Quintrell, N.A.2    Bishop, J.M.3
  • 46
    • 0035475321 scopus 로고    scopus 로고
    • Paxillin: A focal adhesion-associated adaptor protein
    • Schaller, M.D. 2001. Paxillin: a focal adhesion-associated adaptor protein. Oncogene. 20:6459-6472.
    • (2001) Oncogene , vol.20 , pp. 6459-6472
    • Schaller, M.D.1
  • 48
    • 0000820364 scopus 로고
    • Molecular cloning of the CD2 antigen, the T-cell erythrocyte receptor, by a rapid immunoselection procedure
    • Seed, B., and A. Aruffo. 1987. Molecular cloning of the CD2 antigen, the T-cell erythrocyte receptor, by a rapid immunoselection procedure. Proc. Natl. Acad. Sci. USA. 84:3365-3369.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3365-3369
    • Seed, B.1    Aruffo, A.2
  • 49
    • 0026572318 scopus 로고
    • Effects of SH2 and SH3 deletions on the functional activities of wild-type and transforming variants of c-Src
    • Seidel-Dugan, C., B.E. Meyer, S.M. Thomas, and J.S. Brugge. 1992. Effects of SH2 and SH3 deletions on the functional activities of wild-type and transforming variants of c-Src. Mol. Cell. Biol. 12:1835-1845.
    • (1992) Mol. Cell. Biol , vol.12 , pp. 1835-1845
    • Seidel-Dugan, C.1    Meyer, B.E.2    Thomas, S.M.3    Brugge, J.S.4
  • 50
    • 0030887842 scopus 로고    scopus 로고
    • Engineering unnatural nucleotide specificity for Rous sarcoma virus tyrosine kinase to uniquely label its direct substrates
    • Shah, K., Y. Liu, C. Deirmengian, and K.M. Shokat. 1997. Engineering unnatural nucleotide specificity for Rous sarcoma virus tyrosine kinase to uniquely label its direct substrates. Proc. Natl. Acad. Sci. USA. 94:3565-3570.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3565-3570
    • Shah, K.1    Liu, Y.2    Deirmengian, C.3    Shokat, K.M.4
  • 51
    • 0028175989 scopus 로고
    • Cysteine3 of Src family protein tyrosine kinase determines palmitoylation and localization in caveolae
    • Shenoy-Scaria, A.M., D.J. Dietzen, J. Kwong, D.C. Link, and D.M. Lublin. 1994. Cysteine3 of Src family protein tyrosine kinase determines palmitoylation and localization in caveolae. J. Cell Biol. 126:353-363.
    • (1994) J. Cell Biol , vol.126 , pp. 353-363
    • Shenoy-Scaria, A.M.1    Dietzen, D.J.2    Kwong, J.3    Link, D.C.4    Lublin, D.M.5
  • 52
    • 0345599000 scopus 로고    scopus 로고
    • Differently-anchored influenza hemagglutinin mutants display distinct interaction dynamics with mutual rafts
    • Shvartsman, D.E., M. Kotler, R.D. Tall, M.G. Roth, and Y.I. Henis. 2003. Differently-anchored influenza hemagglutinin mutants display distinct interaction dynamics with mutual rafts. J. Cell Biol. 163:879-888.
    • (2003) J. Cell Biol , vol.163 , pp. 879-888
    • Shvartsman, D.E.1    Kotler, M.2    Tall, R.D.3    Roth, M.G.4    Henis, Y.I.5
  • 53
    • 0031171392 scopus 로고    scopus 로고
    • A crystal milestone: The structure of regulated Src
    • Superti-Furga, G., and S. Gonfloni. 1997. A crystal milestone: the structure of regulated Src. Bioessays. 19:447-450.
    • (1997) Bioessays , vol.19 , pp. 447-450
    • Superti-Furga, G.1    Gonfloni, S.2
  • 54
    • 0033625038 scopus 로고    scopus 로고
    • GFRα-mediated localization of RET to lipid rafts is required for effective downstream signaling, differentiation, and neuronal survival
    • Tansey, M.G., R.H. Baloh, J. Milbrandt, and E.M. Johnson Jr. 2000. GFRα-mediated localization of RET to lipid rafts is required for effective downstream signaling, differentiation, and neuronal survival. Neuron. 25:611-623.
    • (2000) Neuron , vol.25 , pp. 611-623
    • Tansey, M.G.1    Baloh, R.H.2    Milbrandt, J.3    Johnson Jr., E.M.4
  • 55
    • 0030820672 scopus 로고    scopus 로고
    • The role of the Src homology domains in morphological transformation by v-src
    • Tian, M., and G.S. Martin. 1997. The role of the Src homology domains in morphological transformation by v-src. Mol. Biol. Cell. 8:1183-1193.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1183-1193
    • Tian, M.1    Martin, G.S.2
  • 56
    • 0035960717 scopus 로고    scopus 로고
    • Coordination of cell polarization and migration by the Rho family GTPases requires Src tyrosine kinase activity
    • Timpson, P., G.E. Jones, M.C. Frame, and V.G. Brunton. 2001. Coordination of cell polarization and migration by the Rho family GTPases requires Src tyrosine kinase activity. Curr. Biol. 11:1836-1846.
    • (2001) Curr. Biol , vol.11 , pp. 1836-1846
    • Timpson, P.1    Jones, G.E.2    Frame, M.C.3    Brunton, V.G.4
  • 57
    • 33746826012 scopus 로고    scopus 로고
    • Two distinct pools of Src family tyrosine kinases regulate PDGF-induced DNA synthesis and actin dorsal ruffles
    • Veracini, L., M. Franco, A. Boureux, V. Simon, S. Roche, and C. Benistant. 2006. Two distinct pools of Src family tyrosine kinases regulate PDGF-induced DNA synthesis and actin dorsal ruffles. J. Cell Sci. 119:2921-2934.
    • (2006) J. Cell Sci , vol.119 , pp. 2921-2934
    • Veracini, L.1    Franco, M.2    Boureux, A.3    Simon, V.4    Roche, S.5    Benistant, C.6
  • 58
    • 0027409064 scopus 로고
    • Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: Crystal structures of the complexed and peptide-free forms
    • Waksman, G., S.E. Shoelson, N. Pant, D. Cowburn, and J. Kuriyan. 1993. Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms. Cell. 72:779-790.
    • (1993) Cell , vol.72 , pp. 779-790
    • Waksman, G.1    Shoelson, S.E.2    Pant, N.3    Cowburn, D.4    Kuriyan, J.5
  • 60
    • 33846781373 scopus 로고    scopus 로고
    • A paxillin tyrosine phosphorylation switch regulates the assembly and form of cell-matrix adhesions
    • Zaidel-Bar, R., R. Milo, Z. Kam, and B. Geiger. 2007. A paxillin tyrosine phosphorylation switch regulates the assembly and form of cell-matrix adhesions. J. Cell Sci. 120:137-148.
    • (2007) J. Cell Sci , vol.120 , pp. 137-148
    • Zaidel-Bar, R.1    Milo, R.2    Kam, Z.3    Geiger, B.4


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