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Volumn 122, Issue 11, 2009, Pages 1882-1894

VASP is a CXCR2-interacting protein that regulates CXCR2-mediated polarization and chemotaxis

Author keywords

Actin; Chemotaxis; CXCR2; Phosphorylation; VASP

Indexed keywords

CHEMOKINE RECEPTOR CXCR2; CYCLIC AMP DEPENDENT PROTEIN KINASE; F ACTIN; INTERLEUKIN 8; PROTEIN KINASE C; SERINE; SHORT HAIRPIN RNA; THREONINE; VASODILATOR STIMULATED PHOSPHOPROTEIN;

EID: 69449104923     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.039057     Document Type: Article
Times cited : (54)

References (48)
  • 2
    • 0039207312 scopus 로고    scopus 로고
    • The vasodilator-stimulated phosphoprotein (VASP) is involved in cGMP- and cAMP-mediated inhibition of agonist-induced platelet aggregation, but is dispensable for smooth muscle function
    • Aszodi, A., Pfeifer, A., Ahmad, M., Glauner, M., Zhou, X. H., Ny, L., Andersson, K. E., Kehrel, B., Offermanns, S. and Fasider, R. (1999). The vasodilator-stimulated phosphoprotein (VASP) is involved in cGMP- and cAMP-mediated inhibition of agonist-induced platelet aggregation, but is dispensable for smooth muscle function. EMBO J. 18, 37-48.
    • (1999) EMBO J , vol.18 , pp. 37-48
    • Aszodi, A.1    Pfeifer, A.2    Ahmad, M.3    Glauner, M.4    Zhou, X.H.5    Ny, L.6    Andersson, K.E.7    Kehrel, B.8    Offermanns, S.9    Fasider, R.10
  • 3
    • 0033551783 scopus 로고    scopus 로고
    • The EVH2 domain of the vasodilator-stimulated phosphoprotein mediates tetramerization, F-actin binding, and actin bundle formation
    • Bachmann, C., Fischer, L., Walter, U. and Reinhard, M. (1999). The EVH2 domain of the vasodilator-stimulated phosphoprotein mediates tetramerization, F-actin binding, and actin bundle formation. J. Biol. Chem. 274, 23549-23557.
    • (1999) J. Biol. Chem , vol.274 , pp. 23549-23557
    • Bachmann, C.1    Fischer, L.2    Walter, U.3    Reinhard, M.4
  • 4
    • 23344442354 scopus 로고    scopus 로고
    • Ena/VASP proteins enhance actin polymerization in the presence of barbed end capping proteins
    • Barzik, M., Kotova, T. I., Higgs, H. N., Hazelwood, L., Hasein, D., Gertler, F. B. and Schafer, D. A. (2005). Ena/VASP proteins enhance actin polymerization in the presence of barbed end capping proteins. J. Biol. Chem. 280, 28653-28662.
    • (2005) J. Biol. Chem , vol.280 , pp. 28653-28662
    • Barzik, M.1    Kotova, T.I.2    Higgs, H.N.3    Hazelwood, L.4    Hasein, D.5    Gertler, F.B.6    Schafer, D.A.7
  • 5
    • 0034705292 scopus 로고    scopus 로고
    • Repulsive axon guidance: Abelson and Enabled play opposing roles downstream of the roundabout receptor
    • Bashaw, G. J., Kidd, T., Murray, D., Pawson, T. and Goodman, C. S. (2000). Repulsive axon guidance: Abelson and Enabled play opposing roles downstream of the roundabout receptor. Cell 101, 703-715.
    • (2000) Cell , vol.101 , pp. 703-715
    • Bashaw, G.J.1    Kidd, T.2    Murray, D.3    Pawson, T.4    Goodman, C.S.5
  • 6
    • 0034705317 scopus 로고    scopus 로고
    • Negative regulation of fibroblast motility by Ena/VASP proteins
    • Bear, J. E., Loureiro, J. J., Libova, I., Fassler, R., Wehland, J. and Gerder, F. B. (2000). Negative regulation of fibroblast motility by Ena/VASP proteins. Cell 101, 717-728.
    • (2000) Cell , vol.101 , pp. 717-728
    • Bear, J.E.1    Loureiro, J.J.2    Libova, I.3    Fassler, R.4    Wehland, J.5    Gerder, F.B.6
  • 9
    • 33947515200 scopus 로고    scopus 로고
    • AMP-activated protein kinase impairs endothelial actin cytoskeleton assembly by phosphorylating vasoditator-stimulated phosphoprotein
    • Blume, C., Benz, P. M., Walter, U., Ha, J., Kemp, B. E. and Renne, T. (2007). AMP-activated protein kinase impairs endothelial actin cytoskeleton assembly by phosphorylating vasoditator-stimulated phosphoprotein. J. Biol. Chem. 282, 4601-4612.
    • (2007) J. Biol. Chem , vol.282 , pp. 4601-4612
    • Blume, C.1    Benz, P.M.2    Walter, U.3    Ha, J.4    Kemp, B.E.5    Renne, T.6
  • 10
    • 0028303913 scopus 로고
    • cAMP- and cGMP-dependent protein kmase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets
    • Butt, E., Abel, K., Krieger, M., Palm, D, Hoppe, V., Hoppe, J. and Walter, U. (1994). cAMP- and cGMP-dependent protein kmase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets. J. Biol. Chem. 269, 14509-14517.
    • (1994) J. Biol. Chem , vol.269 , pp. 14509-14517
    • Butt, E.1    Abel, K.2    Krieger, M.3    Palm, D.4    Hoppe, V.5    Hoppe, J.6    Walter, U.7
  • 11
    • 0346094386 scopus 로고    scopus 로고
    • Vasodilator-stimulated phosphoprotein is a substrate for protein kinase C
    • Chitaley, K., Chen, L., Galler, A., Walter, U., Daum, G. and Clowes, A. W. (2004). Vasodilator-stimulated phosphoprotein is a substrate for protein kinase C. FEBS Lett. 556, 211-215.
    • (2004) FEBS Lett , vol.556 , pp. 211-215
    • Chitaley, K.1    Chen, L.2    Galler, A.3    Walter, U.4    Daum, G.5    Clowes, A.W.6
  • 12
    • 36248961146 scopus 로고    scopus 로고
    • Regulation of VASP serine 157 phosphorylation in human neutrophils after stimulation by a chemoattractant
    • Eckert, R. E. and Jones, S. L. (2007). Regulation of VASP serine 157 phosphorylation in human neutrophils after stimulation by a chemoattractant. J. Leukoc. Biol. 82, 1311-1321.
    • (2007) J. Leukoc. Biol , vol.82 , pp. 1311-1321
    • Eckert, R.E.1    Jones, S.L.2
  • 13
    • 0026546129 scopus 로고
    • Concentration and regulation of cyclic nucleotides, cyclic-nuctootide-dependent protein kinases and one of their major substrates in human platelets: Estimating the rate of cAMP-regulated and cGMP-regulated protein phosphorylation in intact cells
    • Eigenthaler, M., Nolte, C., Halbrugge, M. and Walter, U. (1992). Concentration and regulation of cyclic nucleotides, cyclic-nuctootide-dependent protein kinases and one of their major substrates in human platelets: estimating the rate of cAMP-regulated and cGMP-regulated protein phosphorylation in intact cells. Eur. J. Biochem. 205, 471-481.
    • (1992) Eur. J. Biochem , vol.205 , pp. 471-481
    • Eigenthaler, M.1    Nolte, C.2    Halbrugge, M.3    Walter, U.4
  • 14
    • 0035907361 scopus 로고    scopus 로고
    • Phosphorylation-independent association of CXCR2 with the protein phosphatase 2A core enzyme
    • Fan, G. H., Yang, W., Sai, J. and Richmond, A. (2001a). Phosphorylation-independent association of CXCR2 with the protein phosphatase 2A core enzyme. J. Biol. Chem. 276, 16960-16968.
    • (2001) J. Biol. Chem , vol.276 , pp. 16960-16968
    • Fan, G.H.1    Yang, W.2    Sai, J.3    Richmond, A.4
  • 15
    • 0035936552 scopus 로고    scopus 로고
    • Identification of a motif in the carboxyl terminus of CXCR2 that is involved in adaptin 2 binding and receptor internalization
    • Fan, G. H., Yang, W., Wang, X. J., Qian, Q. and Richmond, A. (2001b). Identification of a motif in the carboxyl terminus of CXCR2 that is involved in adaptin 2 binding and receptor internalization. Biochemistry 40, 791-800.
    • (2001) Biochemistry , vol.40 , pp. 791-800
    • Fan, G.H.1    Yang, W.2    Wang, X.J.3    Qian, Q.4    Richmond, A.5
  • 16
    • 0037155284 scopus 로고    scopus 로고
    • Hsc/Hsp70 interacting protein (hip) associates with CXCR2 and regulates the receptor signaling and trafficking
    • Fan, G. H, Yang, W., Sai, J. and Richmond, A. (2002). Hsc/Hsp70 interacting protein (hip) associates with CXCR2 and regulates the receptor signaling and trafficking. J. Biol. Chem. 277, 6590-6597.
    • (2002) J. Biol. Chem , vol.277 , pp. 6590-6597
    • Fan, G.H.1    Yang, W.2    Sai, J.3    Richmond, A.4
  • 17
    • 35649021883 scopus 로고    scopus 로고
    • Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP
    • Ferron, F., Rebowski, G., Lee, S. H. and Dominguez, R. (2007). Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP. EMBO J. 26, 4597-4606.
    • (2007) EMBO J , vol.26 , pp. 4597-4606
    • Ferron, F.1    Rebowski, G.2    Lee, S.H.3    Dominguez, R.4
  • 18
    • 0037160086 scopus 로고    scopus 로고
    • Increased spreading, Rac/p21-activated kinase (PAK) activity, and compromised cell motility in cells deficient in vasodilatur-stimulated. phosphoprotein (VASP)
    • Garcia Arguinzonis, M. I., Galler, A. B., Walter, U., Reinhard, M. and Simm, A. (2002). Increased spreading, Rac/p21-activated kinase (PAK) activity, and compromised cell motility in cells deficient in vasodilatur-stimulated. phosphoprotein (VASP). J. Biol. Chem. 277, 45604-45610.
    • (2002) J. Biol. Chem , vol.277 , pp. 45604-45610
    • Garcia Arguinzonis, M.I.1    Galler, A.B.2    Walter, U.3    Reinhard, M.4    Simm, A.5
  • 19
    • 0030592559 scopus 로고    scopus 로고
    • Mena, a relative of VASP and Drosophila Enabled, is implicated in the control of microfilament dynamics
    • Gertler, F. B., Niebuhr, K., Reinhard, M., Wehland, J. and Soriano, P. (1996). Mena, a relative of VASP and Drosophila Enabled, is implicated in the control of microfilament dynamics. Cell 87, 227-239.
    • (1996) Cell , vol.87 , pp. 227-239
    • Gertler, F.B.1    Niebuhr, K.2    Reinhard, M.3    Wehland, J.4    Soriano, P.5
  • 20
    • 0025250142 scopus 로고
    • Stoichiometric and reversible phosphorylation of a 46-kDa protein in human platelets in response to cGMP- and cAMP-elevating vasodilators
    • Halbrugge, M., Friedrich, C., Elgenthaler, M., Schanzenbacher, P. and Walter, U. (1990). Stoichiometric and reversible phosphorylation of a 46-kDa protein in human platelets in response to cGMP- and cAMP-elevating vasodilators. J. Biol. Chem. 265, 3088-3093.
    • (1990) J. Biol. Chem , vol.265 , pp. 3088-3093
    • Halbrugge, M.1    Friedrich, C.2    Elgenthaler, M.3    Schanzenbacher, P.4    Walter, U.5
  • 21
    • 0037147305 scopus 로고    scopus 로고
    • Requirement of a vasodilator-stimulated phosphoprotein family member for cell adhesion, the formation of filopodia, and chemotaxis in dictyostelium
    • Hang Y. H., Chung, C. Y., Wessels, D., Stephens, S., Titus, M. A., Soll, D. R. and Firtel, R. A. (2002). Requirement of a vasodilator-stimulated phosphoprotein family member for cell adhesion, the formation of filopodia, and chemotaxis in dictyostelium. J. Biol. Chem. 277, 49977-49887.
    • (2002) J. Biol. Chem , vol.277 , pp. 49977-49887
    • Hang, Y.H.1    Chung, C.Y.2    Wessels, D.3    Stephens, S.4    Titus, M.A.5    Soll, D.R.6    Firtel, R.A.7
  • 22
    • 0034613254 scopus 로고    scopus 로고
    • Phosphorylation of the vasoditator-stimulated phosphoprotein regulates its interaction with actin
    • Harbeck, B., Huttelmaier, S., Schluter, K., Jockusch, B. M. and Menberger, S. (2000). Phosphorylation of the vasoditator-stimulated phosphoprotein regulates its interaction with actin. J. Biol. Chem. 275, 30817-30825.
    • (2000) J. Biol. Chem , vol.275 , pp. 30817-30825
    • Harbeck, B.1    Huttelmaier, S.2    Schluter, K.3    Jockusch, B.M.4    Menberger, S.5
  • 24
    • 0028958812 scopus 로고
    • A comparison of post-receptor signal transduction events in Jurkat cells transfected with either II-8R1 or IL-8R2. Chemokine mediated activation of p42/p44 MAP-kinase (ERK-2)
    • Jones, S. A., Moser, B. and Thelen, M. (1995). A comparison of post-receptor signal transduction events in Jurkat cells transfected with either II-8R1 or IL-8R2. Chemokine mediated activation of p42/p44 MAP-kinase (ERK-2). FEBS Lett. 364, 211-214.
    • (1995) FEBS Lett , vol.364 , pp. 211-214
    • Jones, S.A.1    Moser, B.2    Thelen, M.3
  • 28
    • 0034680938 scopus 로고    scopus 로고
    • cAMP-dependent protein kinase phosphorylation of EVL, a Mena/VASP relative, regulates its interaction with actin and SH3 domains
    • Lambrechts, A., Kwiatkowski, A. V., Lanier, L. M., Bear, J. E., Vandekerckhove, J., Ampe, C. and Gertler, F. B. (2000). cAMP-dependent protein kinase phosphorylation of EVL, a Mena/VASP relative, regulates its interaction with actin and SH3 domains. J. Biol. Chem. 275, 36143-36151.
    • (2000) J. Biol. Chem , vol.275 , pp. 36143-36151
    • Lambrechts, A.1    Kwiatkowski, A.V.2    Lanier, L.M.3    Bear, J.E.4    Vandekerckhove, J.5    Ampe, C.6    Gertler, F.B.7
  • 31
    • 34948857998 scopus 로고    scopus 로고
    • Modulation of lamellipodial structure and dynamics by NO-dependent phosphorylation of VASP Ser239
    • Lindsay, S. L., Ramsey, S., Aitchison, M., Renne, T. and Evans, T. J. (2007). Modulation of lamellipodial structure and dynamics by NO-dependent phosphorylation of VASP Ser239. J. Cell Sci. 120, 3011-3021.
    • (2007) J. Cell Sci , vol.120 , pp. 3011-3021
    • Lindsay, S.L.1    Ramsey, S.2    Aitchison, M.3    Renne, T.4    Evans, T.J.5
  • 32
    • 0036323119 scopus 로고    scopus 로고
    • Critical roles of phosphorylation and actin binding motifs, but not the central proline-rich region, for Ena/vasodilator-stimulated phosphoprotein (VASP) function during cell migration
    • Loureiro, J. J., Rubinson, D. A., Bear, J. E., Baltus, G. A., Kwiatkowski, A. V. and Gertler, F. B. (2002). Critical roles of phosphorylation and actin binding motifs, but not the central proline-rich region, for Ena/vasodilator-stimulated phosphoprotein (VASP) function during cell migration. Mol. Biol. Cell 13, 2533-2546.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2533-2546
    • Loureiro, J.J.1    Rubinson, D.A.2    Bear, J.E.3    Baltus, G.A.4    Kwiatkowski, A.V.5    Gertler, F.B.6
  • 33
    • 0032938716 scopus 로고    scopus 로고
    • Regulation of tyrosine bnase cascades by G-protein-coupled receptors
    • Luttrell, L. M., Daaks, V. and Lefkowitz, R. J. (1999). Regulation of tyrosine bnase cascades by G-protein-coupled receptors. Curr. Opin. Cell Biol. 11, 177-183.
    • (1999) Curr. Opin. Cell Biol , vol.11 , pp. 177-183
    • Luttrell, L.M.1    Daaks, V.2    Lefkowitz, R.J.3
  • 34
    • 4644333836 scopus 로고    scopus 로고
    • Mena and vasodilator-stimulated phosphoprotein are required for multiple actin-dependent processes that shape the vertebrate nervous system
    • Menzies, A. S., Aszodi, A., Williams, S. E., Pfeifer, A., Weliman, A. M., Goh, K. L., Mason, C. A., Fassler, R. and Gertler, F. B. (2004). Mena and vasodilator-stimulated phosphoprotein are required for multiple actin-dependent processes that shape the vertebrate nervous system. J. Neurosci. 24, 8029-8038.
    • (2004) J. Neurosci , vol.24 , pp. 8029-8038
    • Menzies, A.S.1    Aszodi, A.2    Williams, S.E.3    Pfeifer, A.4    Weliman, A.M.5    Goh, K.L.6    Mason, C.A.7    Fassler, R.8    Gertler, F.B.9
  • 35
    • 0027957798 scopus 로고
    • Melanoma growth stimulatory activity enhances the phosphorylation of the class II interleukin-8 receptor in non-hematopoietic cells
    • Mueller, S. G., Schram, W. P. and Richmond, A. (1994). Melanoma growth stimulatory activity enhances the phosphorylation of the class II interleukin-8 receptor in non-hematopoietic cells. J. Biol. Chem. 269, 1973-1980.
    • (1994) J. Biol. Chem , vol.269 , pp. 1973-1980
    • Mueller, S.G.1    Schram, W.P.2    Richmond, A.3
  • 36
    • 34249743266 scopus 로고    scopus 로고
    • RhoB plays an essential role in CXCR2 sorting decisions
    • Neel, N. F., Lapierre, L. A., Goldenring, J. R. and Richmond, A. (2007). RhoB plays an essential role in CXCR2 sorting decisions. J. Cell Sci. 120, 1559-1571.
    • (2007) J. Cell Sci , vol.120 , pp. 1559-1571
    • Neel, N.F.1    Lapierre, L.A.2    Goldenring, J.R.3    Richmond, A.4
  • 37
    • 0033613560 scopus 로고    scopus 로고
    • Galphai is not required for chemotaxis mediated by Gi-coupled receptors
    • Neptune, E. R., Iiri, T. and Bourne, H. R. (1999). Galphai is not required for chemotaxis mediated by Gi-coupled receptors. J. Biol. Chem. 274, 2824-2828.
    • (1999) J. Biol. Chem , vol.274 , pp. 2824-2828
    • Neptune, E.R.1    Iiri, T.2    Bourne, H.R.3
  • 38
    • 44349090393 scopus 로고    scopus 로고
    • Ena/VASP proteins capture actin filament barbed ends
    • Pasic, L., Kotova, T. and Schafer, D. A. (2008). Ena/VASP proteins capture actin filament barbed ends. J. Biol. Chem. 283, 9814-9819.
    • (2008) J. Biol. Chem , vol.283 , pp. 9814-9819
    • Pasic, L.1    Kotova, T.2    Schafer, D.A.3
  • 39
    • 33845512493 scopus 로고    scopus 로고
    • PKCdelta regulates collagen-induced platelet aggregation through inhibition of VASP-mediated filopodia formation
    • Pula, G., Schuh, K., Nakayama, K., Nakayama, K. I, Walter, U. and Poole, A. W. (2006). PKCdelta regulates collagen-induced platelet aggregation through inhibition of VASP-mediated filopodia formation. Blood 108, 4035-4044.
    • (2006) Blood , vol.108 , pp. 4035-4044
    • Pula, G.1    Schuh, K.2    Nakayama, K.3    Nakayama, K.I.4    Walter, U.5    Poole, A.W.6
  • 40
    • 0026563095 scopus 로고
    • The 46/50 kDa phosphoprotein VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts
    • Reinhard, M., Halbrugge, M., Scheer, U., Wiegand, C, Jockusch, B. M. and Walter, U. (1992). The 46/50 kDa phosphoprotein VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts. EMBO J. 11, 2063-2070.
    • (1992) EMBO J , vol.11 , pp. 2063-2070
    • Reinhard, M.1    Halbrugge, M.2    Scheer, U.3    Wiegand, C.4    Jockusch, B.M.5    Walter, U.6
  • 41
    • 0032508720 scopus 로고    scopus 로고
    • Differential cross-regulation of the human chemokine receptors CXCR1 and CXCR2. Evidence for time-dependent signal generation
    • Richardson, R. M., Pridgen, B. C., Haribabu, B., Ali, H. and Sayderman, R. (1998). Differential cross-regulation of the human chemokine receptors CXCR1 and CXCR2. Evidence for time-dependent signal generation. J. Biol. Chem. 273, 23830-23836.
    • (1998) J. Biol. Chem , vol.273 , pp. 23830-23836
    • Richardson, R.M.1    Pridgen, B.C.2    Haribabu, B.3    Ali, H.4    Sayderman, R.5
  • 42
    • 33846002381 scopus 로고    scopus 로고
    • The IL sequence in the LLK1 motifin CXCR2 is required for full lligand-induced activation of Erk, Akt, and chemotaxis in HL-60 cells
    • Sul, J., Walker, G., Wikswo, J. and Richmond, A. (2006). The IL sequence in the LLK1 motifin CXCR2 is required for full lligand-induced activation of Erk, Akt, and chemotaxis in HL-60 cells, J. Biol. Chem. 281, 35931-35941.
    • (2006) J. Biol. Chem , vol.281 , pp. 35931-35941
    • Sul, J.1    Walker, G.2    Wikswo, J.3    Richmond, A.4
  • 43
    • 55549147533 scopus 로고    scopus 로고
    • Parallel P13K-dependent and src-indepeadent pathways lead to CXCL8-mediated Rac2 activation and chemotaxis
    • Sal, J., Raman, D., Liu, Y., Wikswo, J. and Richmond, A. (2008). Parallel P13K-dependent and src-indepeadent pathways lead to CXCL8-mediated Rac2 activation and chemotaxis. J. Biol. Chem. 283, 26538-26547.
    • (2008) J. Biol. Chem , vol.283 , pp. 26538-26547
    • Sal, J.1    Raman, D.2    Liu, Y.3    Wikswo, J.4    Richmond, A.5
  • 44
    • 0032911044 scopus 로고    scopus 로고
    • Dynamics of a chemoattractant receptor in living neutrophils during chemotaxis
    • Servant, G., Weiner, O. D., Neptune, E. R,. Sedat, J. W. and Bourne H. R. (1999). Dynamics of a chemoattractant receptor in living neutrophils during chemotaxis. Mol. Bio. Cell 10, 1163-1178.
    • (1999) Mol. Bio. Cell , vol.10 , pp. 1163-1178
    • Servant, G.1    Weiner, O.D.2    Neptune, E.R.3    Sedat, J.W.4    Bourne, H.R.5
  • 45
    • 0035494440 scopus 로고    scopus 로고
    • Pivotal role of VASP in Arp2/3 complex-mediated actin nucleation, actin branch-formation, and Listeria monocytogenes motility
    • Skoble, J., Auerbach, V., Goley, E. D., Welch, M. D. and Portnoy, D. A. (2001). Pivotal role of VASP in Arp2/3 complex-mediated actin nucleation, actin branch-formation, and Listeria monocytogenes motility. J. Cell Biol. 155, 89-100.
    • (2001) J. Cell Biol , vol.155 , pp. 89-100
    • Skoble, J.1    Auerbach, V.2    Goley, E.D.3    Welch, M.D.4    Portnoy, D.A.5
  • 46
    • 0034618052 scopus 로고    scopus 로고
    • Signal transduction by CXC chemokine receptor 4. Stromal cell-derived factor 1 stimulates prolonged protein kinase B and extracellular signal-regulated kinase 2 activation in T lymphocytes
    • Tilton, B., Ho, L., Oberlin, E., Loetscher, P., Baleux, F., Clark-Lewis, I. and Thelen, M. (2000). Signal transduction by CXC chemokine receptor 4. Stromal cell-derived factor 1 stimulates prolonged protein kinase B and extracellular signal-regulated kinase 2 activation in T lymphocytes. J. Exp. Med. 192, 313-324.
    • (2000) J. Exp. Med , vol.192 , pp. 313-324
    • Tilton, B.1    Ho, L.2    Oberlin, E.3    Loetscher, P.4    Baleux, F.5    Clark-Lewis, I.6    Thelen, M.7
  • 47
    • 0033082439 scopus 로고    scopus 로고
    • The tyrosine kinase Abl and its substrate enabled collaborate with the receptor phosphatase Dlar to control motor axon guidance
    • Wills, Z., Bateman, J., Korey, C. A., Comer, A. and Van Vactor, D. (1999). The tyrosine kinase Abl and its substrate enabled collaborate with the receptor phosphatase Dlar to control motor axon guidance. Neuron 22, 301-312.
    • (1999) Neuron , vol.22 , pp. 301-312
    • Wills, Z.1    Bateman, J.2    Korey, C.A.3    Comer, A.4    Van Vactor, D.5
  • 48
    • 33744951973 scopus 로고    scopus 로고
    • Migfilin interacts with vasodilator-stimulated phosphoprotern (VASP) and regulates VASP localization to cell-matrix adhesions and migration
    • Zhang, Y., Tu, Y., Gkretsi, V. and Wu, C. (2006). Migfilin interacts with vasodilator-stimulated phosphoprotern (VASP) and regulates VASP localization to cell-matrix adhesions and migration. J. Biol. Chem. 281, 12397-12407.
    • (2006) J. Biol. Chem , vol.281 , pp. 12397-12407
    • Zhang, Y.1    Tu, Y.2    Gkretsi, V.3    Wu, C.4


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