메뉴 건너뛰기




Volumn 101, Issue 7, 2003, Pages 2804-2809

Felic (CIP4b), a novel binding partner with the Src kinase Lyn and Cdc42, localizes to the phagocytic cup

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSKELETON PROTEIN; EZRIN; FELIC PROTEIN; GUANOSINE TRIPHOSPHATASE; INSULIN; MATRIGEL; PROTEIN; PROTEIN CDC42; PROTEIN CIP 4B; PROTEIN TYROSINE KINASE; SRC KINASE LYN; TYROSINE; UNCLASSIFIED DRUG; ISOPROTEIN; LYN PROTEIN-TYROSINE KINASE; MICROTUBULE ASSOCIATED PROTEIN; PROTEIN KINASE LYN; TRIP10 PROTEIN, HUMAN;

EID: 0038446676     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood-2002-03-0851     Document Type: Article
Times cited : (32)

References (38)
  • 1
    • 0030933277 scopus 로고    scopus 로고
    • Oncoprotein networks
    • Hunter T. Oncoprotein networks. Cell. 1997;88:333-346.
    • (1997) Cell , vol.88 , pp. 333-346
    • Hunter, T.1
  • 2
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • Pawson T, Scott JD. Signaling through scaffold, anchoring, and adaptor proteins. Science. 1997;278:2075-2080.
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 3
    • 0031439247 scopus 로고    scopus 로고
    • Cellular functions regulated by Src family kinases
    • Thomas SM, Brugge JS. Cellular functions regulated by Src family kinases. Annu Rev Cell Dev Biol. 1997;13:513-609.
    • (1997) Annu Rev Cell Dev Biol , vol.13 , pp. 513-609
    • Thomas, S.M.1    Brugge, J.S.2
  • 4
    • 0026767469 scopus 로고
    • Shc proteins are phosphorylated and regulated by the v-Src and v-Fps protein-tyrosine kinases
    • McGlade J, Cheng A, Pelicci PG, Pawson T. Shc proteins are phosphorylated and regulated by the v-Src and v-Fps protein-tyrosine kinases. Proc Natl Acad Sci U S A. 1992;89:8869-8873.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 8869-8873
    • McGlade, J.1    Cheng, A.2    Pelicci, P.G.3    Pawson, T.4
  • 5
    • 0028984311 scopus 로고
    • Transformation and pp60v-src autophosphorylation correlate with SHC-GRB2 complex formation in rat and chicken cells expressing host-range and kinase-active, transformation-defective alleles of v-src
    • Verderame MF, Guan JL, Woods Ignatoski KM. Transformation and pp60v-src autophosphorylation correlate with SHC-GRB2 complex formation in rat and chicken cells expressing host-range and kinase-active, transformation-defective alleles of v-src. Mol Biol Cell. 1995;6:953-966.
    • (1995) Mol Biol Cell , vol.6 , pp. 953-966
    • Verderame, M.F.1    Guan, J.L.2    Woods Ignatoski, K.M.3
  • 6
    • 0035825121 scopus 로고    scopus 로고
    • Cbl associates with Pyk2 and Src to regulate Src kinase activity, alpha(v)beta(3) integrin-mediated signaling, cell adhesion, and osteoclast motility
    • Sanjay A, Houghton A, Neff L, et al. Cbl associates with Pyk2 and Src to regulate Src kinase activity, alpha(v)beta(3) integrin-mediated signaling, cell adhesion, and osteoclast motility. J Cell Biol. 2001;152:181-195.
    • (2001) J Cell Biol , vol.152 , pp. 181-195
    • Sanjay, A.1    Houghton, A.2    Neff, L.3
  • 7
    • 0034610546 scopus 로고    scopus 로고
    • Involvement of Shc and Cbl-PI 3-kinase in Lyn-dependent proliferative signaling pathways for G-CSF
    • Grishin A, Sinha S, Roginskaya V, et al. Involvement of Shc and Cbl-PI 3-kinase in Lyn-dependent proliferative signaling pathways for G-CSF. Oncogene. 2000;19:97-105.
    • (2000) Oncogene , vol.19 , pp. 97-105
    • Grishin, A.1    Sinha, S.2    Roginskaya, V.3
  • 8
    • 0031011280 scopus 로고    scopus 로고
    • Yeast two-hybrid in vivo association of the Src kinase Lyn with the proto-oncogene product Cbl but not with the p85 subunit of PI 3-kinase
    • Dombrosky-Ferlan PM, Corey SJ. Yeast two-hybrid in vivo association of the Src kinase Lyn with the proto-oncogene product Cbl but not with the p85 subunit of PI 3-kinase. Oncogene. 1997;14:2019-2024.
    • (1997) Oncogene , vol.14 , pp. 2019-2024
    • Dombrosky-Ferlan, P.M.1    Corey, S.J.2
  • 9
    • 0032531732 scopus 로고    scopus 로고
    • Pyk2 and Src-family protein-tyrosine kinases compensate for the loss of FAK in fibronectin-stimulated signaling events but Pyk2 does not fully function to enhance FAK-cell migration
    • Sieg DJ, Ilic D, Jones KC, Damsky CH, Hunter T, Schlaepfer DD. Pyk2 and Src-family protein-tyrosine kinases compensate for the loss of FAK in fibronectin-stimulated signaling events but Pyk2 does not fully function to enhance FAK-cell migration. Embo J. 1998;17:5933-5947.
    • (1998) Embo J , vol.17 , pp. 5933-5947
    • Sieg, D.J.1    Ilic, D.2    Jones, K.C.3    Damsky, C.H.4    Hunter, T.5    Schlaepfer, D.D.6
  • 10
    • 0028577724 scopus 로고
    • Binding of Vav to Grb2 through dimerization of Src homology 3 domains
    • Ye ZS, Baltimore D. Binding of Vav to Grb2 through dimerization of Src homology 3 domains. Proc Natl Acad Sci U S A. 1994;91:12629-12633.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 12629-12633
    • Ye, Z.S.1    Baltimore, D.2
  • 11
    • 0031034050 scopus 로고    scopus 로고
    • Lck regulates Vav activation of members of the Rho family of GT-Pases
    • Han J, Das B, Wei W, et al. Lck regulates Vav activation of members of the Rho family of GT-Pases. Mol Cell Biol. 1997;17:1346-1353.
    • (1997) Mol Cell Biol , vol.17 , pp. 1346-1353
    • Han, J.1    Das, B.2    Wei, W.3
  • 12
    • 0027207287 scopus 로고
    • Tyrosine kinase-stimulated guanine nucleotide exchange activity of Vav in T cell activation
    • Gulbins E, Coggeshall KM, Baier G, Katzav S, Burn P, Altman A. Tyrosine kinase-stimulated guanine nucleotide exchange activity of Vav in T cell activation. Science. 1993;260:822-825.
    • (1993) Science , vol.260 , pp. 822-825
    • Gulbins, E.1    Coggeshall, K.M.2    Baier, G.3    Katzav, S.4    Burn, P.5    Altman, A.6
  • 13
    • 0033755863 scopus 로고    scopus 로고
    • Src kinase-mediated signaling in leukocytes
    • Korade-Mirnics Z, Corey SJ. Src kinase-mediated signaling in leukocytes. J Leukoc Biol. 2000;68:603-613.
    • (2000) J Leukoc Biol , vol.68 , pp. 603-613
    • Korade-Mirnics, Z.1    Corey, S.J.2
  • 14
    • 0028806216 scopus 로고
    • Impaired proliferation of peripheral B cells and indication of autoimmune disease in lyn-deficient mice
    • Nishizumi H, Taniuchi I, Yamanashi Y, et al. Impaired proliferation of peripheral B cells and indication of autoimmune disease in lyn-deficient mice. Immunity. 1995;3:549-560.
    • (1995) Immunity , vol.3 , pp. 549-560
    • Nishizumi, H.1    Taniuchi, I.2    Yamanashi, Y.3
  • 15
    • 0028784215 scopus 로고
    • Multiple defects in the immune system of Lyn-deficient mice, culminating in autoimmune disease
    • Hibbs ML, Tadinton DM, Armes J, et al. Multiple defects in the immune system of Lyn-deficient mice, culminating in autoimmune disease. Cell. 1995;83:301-311.
    • (1995) Cell , vol.83 , pp. 301-311
    • Hibbs, M.L.1    Tadinton, D.M.2    Armes, J.3
  • 16
    • 0029670779 scopus 로고    scopus 로고
    • Physical and functional association of the cbl protooncogen product with an src-family protein tyrosine kinase, p53/56lyn, in the B cell antigen receptor-mediated signaling
    • Tezuka T, Umemori H, Fusaki N, et al. Physical and functional association of the cbl protooncogen product with an src-family protein tyrosine kinase, p53/56lyn, in the B cell antigen receptor-mediated signaling. J Exp Med. 1996;183:675-680.
    • (1996) J Exp Med , vol.183 , pp. 675-680
    • Tezuka, T.1    Umemori, H.2    Fusaki, N.3
  • 17
    • 0027469994 scopus 로고
    • Identification of HS1 protein as a major substrate of protein-tyrosine kinase(s) upon B-cell antigen receptor-mediated signaling
    • Yamanashi Y, Okada M, Semba T, et al. Identification of HS1 protein as a major substrate of protein-tyrosine kinase(s) upon B-cell antigen receptor-mediated signaling. Proc Natl Acad Sci U S A. 1993;90:3631-3635.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 3631-3635
    • Yamanashi, Y.1    Okada, M.2    Semba, T.3
  • 19
    • 0032550365 scopus 로고    scopus 로고
    • A double-edged kinase Lyn: A positive and negative regulator for antigen receptor-mediated signals
    • Nishizumi H, Horikawa K, Mlinaric-Rascan I, Yamamoto T. A double-edged kinase Lyn: a positive and negative regulator for antigen receptor-mediated signals. J Exp Med. 1998;187:1343-1348.
    • (1998) J Exp Med , vol.187 , pp. 1343-1348
    • Nishizumi, H.1    Horikawa, K.2    Mlinaric-Rascan, I.3    Yamamoto, T.4
  • 21
    • 0032488908 scopus 로고    scopus 로고
    • Requirement of Src kinase Lyn for induction of DNA synthesis by granulocyte colony-stimulating factor
    • Corey SJ, Dombrosky-Ferlan PM, Zuo S, et al. Requirement of Src kinase Lyn for induction of DNA synthesis by granulocyte colony-stimulating factor. J Biol Chem. 1998;273:3230-3235.
    • (1998) J Biol Chem , vol.273 , pp. 3230-3235
    • Corey, S.J.1    Dombrosky-Ferlan, P.M.2    Zuo, S.3
  • 22
    • 0030684003 scopus 로고    scopus 로고
    • Requirements for both Racl and Cdc42 in membrane ruffling and phagocytosis in leukocytes
    • Cox D, Chang P, Zhang Q, Reddy PG, Bokoch GM, Greenberg S. Requirements for both Racl and Cdc42 in membrane ruffling and phagocytosis in leukocytes. J Exp Med. 1997;186:1487-1494.
    • (1997) J Exp Med , vol.186 , pp. 1487-1494
    • Cox, D.1    Chang, P.2    Zhang, Q.3    Reddy, P.G.4    Bokoch, G.M.5    Greenberg, S.6
  • 23
    • 0032476593 scopus 로고    scopus 로고
    • Fc receptor-mediated phagocytosis requires CDC42 and Rac1
    • Massol P, Montcourrier P, Guillemot JC, Chavrier P. Fc receptor-mediated phagocytosis requires CDC42 and Rac1. Embo J. 1998;17:6219-6229.
    • (1998) Embo J , vol.17 , pp. 6219-6229
    • Massol, P.1    Montcourrier, P.2    Guillemot, J.C.3    Chavrier, P.4
  • 24
    • 0034695748 scopus 로고    scopus 로고
    • Fegamma receptor-mediated phagocytosis in macrophages lacking the Src family tyrosine kinases Hck, Fgr, and Lyn
    • Fitzer-Attas CJ, Lowry M, Crowley MT, et al. Fegamma receptor-mediated phagocytosis in macrophages lacking the Src family tyrosine kinases Hck, Fgr, and Lyn. J Exp Med. 2000;191:669-682.
    • (2000) J Exp Med , vol.191 , pp. 669-682
    • Fitzer-Attas, C.J.1    Lowry, M.2    Crowley, M.T.3
  • 25
    • 0031194076 scopus 로고    scopus 로고
    • A Cdc42 target protein with homology to the non-kinase domain of FER has a potential role in regulating the actin cytoskeleton
    • Aspenstrom P. A Cdc42 target protein with homology to the non-kinase domain of FER has a potential role in regulating the actin cytoskeleton. Curr Biol. 1997;7:479-487.
    • (1997) Curr Biol , vol.7 , pp. 479-487
    • Aspenstrom, P.1
  • 26
    • 0034536206 scopus 로고    scopus 로고
    • Microtubule-dependent formation of podosomal adhesion structures in primary human macrophages
    • Linder S, Hufner K, Wintergerst U, Aepfelbacher M. Microtubule-dependent formation of podosomal adhesion structures in primary human macrophages. J Cell Sci. 2000;113(pt 23):4165-4176.
    • (2000) J Cell Sci , vol.113 , Issue.PART 23 , pp. 4165-4176
    • Linder, S.1    Hufner, K.2    Wintergerst, U.3    Aepfelbacher, M.4
  • 27
    • 0034677932 scopus 로고    scopus 로고
    • Cdc42-interacting protein 4 mediates binding of the Wiskott-Aldrich syndrome protein to microtubules
    • Tian L, Nelson DL, Stewart DM. Cdc42-interacting protein 4 mediates binding of the Wiskott-Aldrich syndrome protein to microtubules. J Biol Chem. 2000;275:7854-7861.
    • (2000) J Biol Chem , vol.275 , pp. 7854-7861
    • Tian, L.1    Nelson, D.L.2    Stewart, D.M.3
  • 28
    • 0032147066 scopus 로고    scopus 로고
    • Positive and negative roles of the tyrosine kinase Lyn in B cell function
    • DeFranco AL, Chan VW, Lowell CA. Positive and negative roles of the tyrosine kinase Lyn in B cell function. Semin Immunol. 1998;10:299-307.
    • (1998) Semin Immunol , vol.10 , pp. 299-307
    • DeFranco, A.L.1    Chan, V.W.2    Lowell, C.A.3
  • 30
    • 0027971687 scopus 로고
    • Identification of Src, Fyn, Lyn, PI3K and Abl SH3 domain ligands using phage display libraries
    • Rickles RJ, Botfield MC, Weng Z, et al. Identification of Src, Fyn, Lyn, PI3K and Abl SH3 domain ligands using phage display libraries. Embo J. 1994;13:5598-5604.
    • (1994) Embo J , vol.13 , pp. 5598-5604
    • Rickles, R.J.1    Botfield, M.C.2    Weng, Z.3
  • 31
    • 0036077064 scopus 로고    scopus 로고
    • Identification and genetic analysis of human and mouse activated Cdc42 interacting protein-4 isoforms
    • Wang L, Rudert WA, Grishin A, et al. Identification and genetic analysis of human and mouse activated Cdc42 interacting protein-4 isoforms. Biochem Biophys Res Commun. 2002;293:1426-1430.
    • (2002) Biochem Biophys Res Commun , vol.293 , pp. 1426-1430
    • Wang, L.1    Rudert, W.A.2    Grishin, A.3
  • 32
    • 0032933797 scopus 로고    scopus 로고
    • c-Src, receptor tyrosine kinases, and human cancer
    • Biscardi JS, Tice DA, Parsons SJ. c-Src, receptor tyrosine kinases, and human cancer. Adv Cancer Res. 1999;76:61-119
    • (1999) Adv Cancer Res , vol.76 , pp. 61-119
    • Biscardi, J.S.1    Tice, D.A.2    Parsons, S.J.3
  • 33
    • 0033575251 scopus 로고    scopus 로고
    • Src-family tyrosine kinases in activation of ERK-1 and p85/p110-phosphatidylinositol 3-kinase by G/CCKB receptors
    • Daulhac L, Kowalski-Chauvel A, Pradayrol L, Vaysse N, Seva C. Src-family tyrosine kinases in activation of ERK-1 and p85/p110-phosphatidylinositol 3-kinase by G/CCKB receptors. J Biol Chem. 1999;274:20657-20663.
    • (1999) J Biol Chem , vol.274 , pp. 20657-20663
    • Daulhac, L.1    Kowalski-Chauvel, A.2    Pradayrol, L.3    Vaysse, N.4    Seva, C.5
  • 34
    • 0027465483 scopus 로고
    • Intestinal crypt cells contain higher levels of cytoskeletal-associated pp60c-src protein tyrosine kinase activity than do differentiated enterocytes
    • Cartwright CA, Mamajiwalla S, Skolnick SA, Eckhart W, Burgess DR. Intestinal crypt cells contain higher levels of cytoskeletal-associated pp60c-src protein tyrosine kinase activity than do differentiated enterocytes. Oncogene. 1993;8:1033-1039.
    • (1993) Oncogene , vol.8 , pp. 1033-1039
    • Cartwright, C.A.1    Mamajiwalla, S.2    Skolnick, S.A.3    Eckhart, W.4    Burgess, D.R.5
  • 35
    • 0032422123 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the Wiskott-Aldrich syndrome protein by Lyn and Btk is regulated by CDC42
    • Guinamard R, Aspenstrom P, Fougereau M, Chavrier P, Guillemot JC. Tyrosine phosphorylation of the Wiskott-Aldrich syndrome protein by Lyn and Btk is regulated by CDC42. FEBS Lett. 1998;434:431-436.
    • (1998) FEBS Lett , vol.434 , pp. 431-436
    • Guinamard, R.1    Aspenstrom, P.2    Fougereau, M.3    Chavrier, P.4    Guillemot, J.C.5
  • 36
    • 0033574722 scopus 로고    scopus 로고
    • The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly
    • Rohatgi R, Ma L, Miki H, et al. The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell. 1999;97:221-231.
    • (1999) Cell , vol.97 , pp. 221-231
    • Rohatgi, R.1    Ma, L.2    Miki, H.3
  • 37
    • 0034683671 scopus 로고    scopus 로고
    • Activation by Cdc42 and PIP(2) of Wiskott-Aldrich syndrome protein (WASp) stimulates actin nucleation by Arp2/3 complex
    • Higgs HN, Pollard TD. Activation by Cdc42 and PIP(2) of Wiskott-Aldrich syndrome protein (WASp) stimulates actin nucleation by Arp2/3 complex. J Cell Biol. 2000;150:1311-1320.
    • (2000) J Cell Biol , vol.150 , pp. 1311-1320
    • Higgs, H.N.1    Pollard, T.D.2
  • 38
    • 0034616165 scopus 로고    scopus 로고
    • Vav2 is an activator of Cdc42, Rac1, and RhoA
    • Abe K, Rossman KL, Liu B, et al. Vav2 is an activator of Cdc42, Rac1, and RhoA. J Biol Chem. 2000;275:10141-10149.
    • (2000) J Biol Chem , vol.275 , pp. 10141-10149
    • Abe, K.1    Rossman, K.L.2    Liu, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.