메뉴 건너뛰기




Volumn 23, Issue 7, 2009, Pages 1065-1076

Adapter protein SH2B1β cross-links actin filaments and regulates actin cytoskeleton

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; AMINO ACID DERIVATIVE; GREEN FLUORESCENT PROTEIN; PROTEIN SH2B1BETA; UNCLASSIFIED DRUG; VASODILATOR STIMULATED PHOSPHOPROTEIN; ACTIN; ACTIN BINDING PROTEIN; CELL ADHESION MOLECULE; ISOPROTEIN; JANUS KINASE 2; MUTANT PROTEIN; PHOSPHOPROTEIN; SH2B1 PROTEIN, HUMAN; SIGNAL TRANSDUCING ADAPTOR PROTEIN; VASODILATOR-STIMULATED PHOSPHOPROTEIN;

EID: 67649573981     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/me.2008-0428     Document Type: Article
Times cited : (26)

References (77)
  • 3
    • 0031919849 scopus 로고    scopus 로고
    • Jaks and STATs: Biological implications
    • DOI 10.1146/annurev.immunol.16.1.293
    • Leonard WJ, O'Shea JJ 1998 Jaks and STATs: biological implications. Annu Rev Immunol 16:293-322 (Pubitemid 28183367)
    • (1998) Annual Review of Immunology , vol.16 , pp. 293-322
    • Leonard, W.J.1    O'Shea, J.J.2
  • 5
    • 0028234529 scopus 로고
    • Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins
    • Darnell Jr JE, Kerr IM, Stark GR 1994 Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins. Science 264:1415-1421 (Pubitemid 24217131)
    • (1994) Science , vol.264 , Issue.5164 , pp. 1415-1421
    • Darnell Jr., J.E.1    Kerr, I.M.2    Stark, G.R.3
  • 6
    • 30944454334 scopus 로고    scopus 로고
    • Cross-regulation of JAK and Src kinases
    • DOI 10.1080/08977190500368031, PII L0265877266
    • Ingley E, Klinken SP 2006 Cross-regulation of JAK and Src kinases. Growth Factors 24:89-95 (Pubitemid 43108779)
    • (2006) Growth Factors , vol.24 , Issue.1 , pp. 89-95
    • Ingley, E.1    Klinken, S.P.2
  • 7
    • 0030613545 scopus 로고    scopus 로고
    • Identification of SH2-Bβ as a substrate of the tyrosine kinase JAK2 involved in growth hormone signaling
    • Rui L, Mathews LS, Hotta K, Gustafson TA, Carter-Su C 1997 Identification of SH2-Bβ as a substrate of the tyrosine kinase JAK2 involved in growth hormone signaling. Mol Cell Biol 17:6633-6644 (Pubitemid 27451210)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.11 , pp. 6633-6644
    • Rui, L.1    Mathews, L.S.2    Hotta, I.3    Gustafson, T.A.4    Carter-Su, C.5
  • 8
    • 33845663497 scopus 로고    scopus 로고
    • SH2B1 (SH2-B) and JAK2: A multifunctional adaptor protein and kinase made for each other
    • DOI 10.1016/j.tem.2006.11.007, PII S104327600600244X
    • Maures TJ, Kurzer JH, Carter-Su C 2007 SH2B1 (SH2-B) and JAK2: a multifunctional adaptor protein and kinase made for each other. Trends Endocrinol Metab 18:38-45 (Pubitemid 44960015)
    • (2007) Trends in Endocrinology and Metabolism , vol.18 , Issue.1 , pp. 38-45
    • Maures, T.J.1    Kurzer, J.H.2    Carter-Su, C.3
  • 9
    • 0035798534 scopus 로고    scopus 로고
    • Four PSM/SH2-B Alternative Splice Variants and Their Differential Roles in Mitogenesis
    • DOI 10.1074/jbc.M104191200
    • Yousaf N, Deng Y, Kang Y, Riedel H 2001 Four PSM/SH2-B alternative splice variants and their differential roles in mitogenesis. J Biol Chem 276:40940-40948 (Pubitemid 37373243)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.44 , pp. 40940-40948
    • Yousaf, N.1    Deng, Y.2    Kang, Y.3    Riedel, H.4
  • 10
    • 0032726331 scopus 로고    scopus 로고
    • Alternative splicing, gene localization, and binding of SH2-B to the insulin receptor kinase domain
    • Nelms K, O'Neill TJ, Li S, Hubbard SR, Gustafson TA, Paul WE 1999 Alternative splicing, gene localization, and binding of SH2-B to the insulin receptor kinase domain. Mamm Genome 10:1160-1167
    • (1999) Mamm Genome , vol.10 , pp. 1160-1167
    • Nelms, K.1    O'Neill, T.J.2    Li, S.3    Hubbard, S.R.4    Gustafson, T.A.5    Paul, W.E.6
  • 13
    • 34548370733 scopus 로고    scopus 로고
    • 813 phosphorylation-dependent and -independent mechanisms
    • DOI 10.1210/me.2007-0111
    • Li Z, Zhou Y, Carter-Su C, Myers Jr MG, Rui L 2007 SH2B1 enhances leptin signaling by both Janus kinase 2 Tyr813 phosphorylation-dependent and -independent mechanisms. Mol Endocrinol 21:2270-2281 (Pubitemid 47347387)
    • (2007) Molecular Endocrinology , vol.21 , Issue.9 , pp. 2270-2281
    • Li, Z.1    Zhou, Y.2    Carter-Su, C.3    Myers Jr., M.G.4    Rui, L.5
  • 14
    • 0032516879 scopus 로고    scopus 로고
    • Platelet-derived growth factor (PDGF) stimulates the association of SH2- Bβ with PDGF receptor and phosphorylation of SH2-Bβ
    • DOI 10.1074/jbc.273.33.21239
    • Rui L, Carter-Su C 1998 Platelet-derived growth factor (PDGF) stimulates the association of SH2-Bβ with PDGF receptor and phosphorylation of SH2-Bβ. J Biol Chem 273:21239-21245 (Pubitemid 28385415)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.33 , pp. 21239-21245
    • Rui, L.1    Carter-Su, C.2
  • 15
    • 0034610745 scopus 로고    scopus 로고
    • PSM, a mediator of PDGF-BB-, IGF-I-, and insulin-stimulated mitogenesis
    • Riedel H, Yousaf N, Zhao Y, Dai H, Deng Y, Wang J 2000 PSM, a mediator of PDGF-BB-, IGF-I-, and insulin-stimulated mitogenesis. Oncogene 19:39-50 (Pubitemid 30066349)
    • (2000) Oncogene , vol.19 , Issue.1 , pp. 39-50
    • Riedel, H.1    Yousaf, N.2    Zhao, Y.3    Dai, H.4    Deng, Y.5    Wang, J.6
  • 16
    • 0032488916 scopus 로고    scopus 로고
    • Insulin-like growth factor-I receptor and insulin receptor association with a Src homology-2 domain-containing putative adapter
    • DOI 10.1074/jbc.273.6.3136
    • Wang J, Riedel H 1998 Insulin-like growth factor-I receptor and insulin receptor association with a Src homology-2 domain-containing putative adapter. J Biol Chem 273:3136-3139 (Pubitemid 28109718)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.6 , pp. 3136-3139
    • Wang, J.1    Riedel, H.2
  • 17
    • 0033537971 scopus 로고    scopus 로고
    • SH2-B is required for nerve growth factor-induced neuronal differentiation
    • Rui L, Herrington J, Carter-Su C 1999 SH2-B is required for nerve growth factor-induced neuronal differentiation. J Biol Chem 274:10590-10594 (Pubitemid 129518359)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.15 , pp. 10590-10594
    • Rui, L.1    Herrington, J.2    Carter-Su, C.3
  • 18
    • 0032418850 scopus 로고    scopus 로고
    • Identification and characterization of novel substrates of Trk receptors in developing neurons
    • DOI 10.1016/S0896-6273(00)80620-0
    • Qian X, Riccio A, Zhang Y, Ginty DD 1998 Identification and characterization of novel substrates of Trk receptors in developing neurons. Neuron 21:1017-1029 (Pubitemid 29018072)
    • (1998) Neuron , vol.21 , Issue.5 , pp. 1017-1029
    • Qian, X.1    Riccio, A.2    Zhang, Y.3    Ginty, D.D.4
  • 19
    • 0032189383 scopus 로고    scopus 로고
    • SH2-Bα is an insulin-receptor adapter protein and substrate that interacts with the activation loop of the insulin-receptor kinase
    • Kotani K, Wilden P, Pillay TS 1998 SH2-Bα is an insulin-receptor adapter protein and substrate that interacts with the activation loop of the insulin-receptor kinase. Biochem J 335(Pt 1):103-109 (Pubitemid 28477055)
    • (1998) Biochemical Journal , vol.335 , Issue.1 , pp. 103-109
    • Kotani, K.1    Wilden, P.2    Pillay, T.S.3
  • 20
    • 0037013284 scopus 로고    scopus 로고
    • Interaction of fibroblast growth factor receptor 3 and the adapter protein SH2-B. a role in Stat5 activation
    • DOI 10.1074/jbc.M102777200
    • Kong M, Wang CS, Donoghue DJ 2002 Interaction of fibroblast growth factor receptor 3 and the adapter protein SH2-B. A role in STAT5 activation. J Biol Chem 277:15962-15970 (Pubitemid 34967878)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.18 , pp. 15962-15970
    • Kong, M.1    Wang, C.S.2    Donoghue, D.J.3
  • 22
    • 4344581405 scopus 로고    scopus 로고
    • Disruption of the SH2-B gene causes age-dependent insulin resistance and glucose intolerance
    • DOI 10.1128/MCB.24.17.7435-7443.2004
    • Duan C, Yang H, White MF, Rui L 2004 Disruption of the SH2-B gene causes age-dependent insulin resistance and glucose intolerance. Mol Cell Biol 24:7435-7443 (Pubitemid 39121472)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.17 , pp. 7435-7443
    • Duan, C.1    Yang, H.2    White, M.F.3    Rui, L.4
  • 23
    • 25144523930 scopus 로고    scopus 로고
    • Identification of SH2-B as a key regulator of leptin sensitivity, energy balance, and body weight in mice
    • Ren D, Li M, Duan C, Rui L 2005 Identification of SH2-B as a key regulator of leptin sensitivity, energy balance, and body weight in mice. Cell Metab 2:95-104
    • (2005) Cell Metab , vol.2 , pp. 95-104
    • Ren, D.1    Li, M.2    Duan, C.3    Rui, L.4
  • 26
    • 34447286254 scopus 로고    scopus 로고
    • Adapter protein SH2-Bβ stimulates actin-based motility of Listeria monocytogenes in a vasodilator-stimulated phosphoprotein (VASP)-dependent fashion
    • Diakonova M, Helfer E, Seveau S, Swanson JA, Kocks C, Rui L, Carlier MF, Carter-Su C 2007 Adapter protein SH2-Bβ stimulates actin-based motility of Listeria monocytogenes in a vasodilator-stimulated phosphoprotein (VASP)-dependent fashion. Infect Immun 75:3581-3593
    • (2007) Infect Immun , vol.75 , pp. 3581-3593
    • Diakonova, M.1    Helfer, E.2    Seveau, S.3    Swanson, J.A.4    Kocks, C.5    Rui, L.6    Carlier, M.F.7    Carter-Su, C.8
  • 27
    • 0034521857 scopus 로고    scopus 로고
    • Identification of actin binding protein, ABP-280, as a binding partner of human Lnk adaptor protein
    • DOI 10.1016/S0161-5890(00)00070-5, PII S0161589000000705
    • He X, Li Y, Schembri-King J, Jakes S, Hayashi J 2000 Identification of actin binding protein, ABP-280, as a binding partner of human Lnk adaptor protein. Mol Immunol 37:603-612 (Pubitemid 32052529)
    • (2000) Molecular Immunology , vol.37 , Issue.10 , pp. 603-612
    • He, X.1    Li, Y.2    Schembri-King, J.3    Jakes, S.4    Hayashi, J.5
  • 28
    • 0842307897 scopus 로고    scopus 로고
    • Increased Numbers of B-1 Cells and Enhanced Responses against TI-2 Antigen in Mice Lacking APS, an Adaptor Molecule Containing PH and SH2 Domains
    • DOI 10.1128/MCB.24.6.2243-2250.2004
    • Iseki M, Kubo C, Kwon SM, Yamaguchi A, Kataoka Y, Yoshida N, Takatsu K, Takaki S 2004 Increased numbers of B-1 cells and enhanced responses against TI-2 antigen in mice lacking APS, an adaptor molecule containing PH and SH2 domains. Mol Cell Biol 24:2243-2250 (Pubitemid 38325981)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.6 , pp. 2243-2250
    • Iseki, M.1    Kubo, C.2    Kwon, S.-M.3    Yamaguchi, A.4    Kataoka, Y.5    Yoshida, N.6    Takatsu, K.7    Takaki, S.8
  • 29
    • 0842267299 scopus 로고    scopus 로고
    • Roles of a conserved family of adaptor proteins, Lnk, SH2-B, and APS, for mast cell development, growth, and functions: APS-deficiency causes augmented degranulation and reduced actin assembly
    • DOI 10.1016/j.bbrc.2004.01.060
    • Kubo-Akashi C, Iseki M, Kwon SM, Takizawa H, Takatsu K, Takaki S 2004 Roles of a conserved family of adaptor proteins, Lnk, SH2-B, and APS, for mast cell development, growth, and functions: APS-deficiency causes augmented degranulation and reduced actin assembly. Biochem Biophys Res Commun 315:356-362 (Pubitemid 38183114)
    • (2004) Biochemical and Biophysical Research Communications , vol.315 , Issue.2 , pp. 356-362
    • Kubo-Akashi, C.1    Iseki, M.2    Kwon, S.-M.3    Takizawa, H.4    Takatsu, K.5    Takaki, S.6
  • 30
    • 0037206949 scopus 로고    scopus 로고
    • 2-terminal autoinhibitory domain of guanine nucleotide exchange factor Vav3 and augments its activity
    • DOI 10.1038/sj.onc.1205927
    • Yabana N, Shibuya M 2002 Adaptor protein APS binds the NH2-terminal autoinhibitory domain of guanine nucleotide exchange factor Vav3 and augments its activity. Oncogene 21:7720-7729 (Pubitemid 35402117)
    • (2002) Oncogene , vol.21 , Issue.50 , pp. 7720-7729
    • Yabana, N.1    Shibuya, M.2
  • 31
    • 24944515497 scopus 로고    scopus 로고
    • The interaction between the adaptor protein APS and Enigma is involved in actin organisation
    • DOI 10.1016/j.yexcr.2005.05.008, PII S0014482705002193
    • Barrès R, Gonzalez T, Le Marchand-Brustel Y, Tanti JF 2005 The interaction between the adaptor protein APS and Enigma is involved in actin organisation. Exp Cell Res 308:334-344 (Pubitemid 43300527)
    • (2005) Experimental Cell Research , vol.308 , Issue.2 , pp. 334-344
    • Barres, R.1    Gonzalez, T.2    Marchand-Brustel, Y.L.3    Tanti, J.-F.4
  • 32
    • 33751520655 scopus 로고    scopus 로고
    • Enigma interacts with adaptor protein with PH and SH2 domains to control insulin-induced actin cytoskeleton remodeling and glucose transporter 4 translocation
    • DOI 10.1210/me.2005-0455
    • Barrès R, Grémeaux T, Gual P, Gonzalez T, Gugenheim J, Tran A, Le Marchand-Brustel Y, Tanti JF 2006 Enigma interacts with adaptor protein with PH and SH2 domains to control insulin-induced actin cytoskeleton remodeling and glucose transporter 4 translocation. Mol Endocrinol 20:2864-2875 (Pubitemid 44833541)
    • (2006) Molecular Endocrinology , vol.20 , Issue.11 , pp. 2864-2875
    • Barres, R.1    Gremeaux, T.2    Gual, P.3    Gonzalez, T.4    Gugenheim, J.5    Tran, A.6    Le Marchand-Brustel, Y.7    Tanti, J.-F.8
  • 33
    • 33646867122 scopus 로고    scopus 로고
    • Mechanistic differences in actin bundling activity of two mammalian formins, FRL1 and mDia2
    • DOI 10.1074/jbc.M510923200
    • Harris ES, Rouiller I, Hanein D, Higgs HN 2006 Mechanistic differences in actin bundling activity of two mammalian formins, FRL1 and mDia2. J Biol Chem 281:14383-14392 (Pubitemid 43848368)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.20 , pp. 14383-14392
    • Harris, E.S.1    Rouiller, I.2    Hanein, D.3    Higgs, H.N.4
  • 34
    • 0037107132 scopus 로고    scopus 로고
    • Three functionally distinct adhesions in filopodia: Shaft adhesions control lamellar extension
    • Steketee MB, Tosney KW 2002 Three functionally distinct adhesions in filopodia: shaft adhesions control lamellar extension. J Neurosci 22:8071-8083 (Pubitemid 35379113)
    • (2002) Journal of Neuroscience , vol.22 , Issue.18 , pp. 8071-8083
    • Steketee, M.B.1    Tosney, K.W.2
  • 36
    • 0036538658 scopus 로고    scopus 로고
    • Filopodia are conduits for melanosome transfer to keratinocytes
    • Scott G, Leopardi S, Printup S, Madden BC 2002 Filopodia are conduits for melanosome transfer to keratinocytes. J Cell Sci 115:1441-1451 (Pubitemid 34428702)
    • (2002) Journal of Cell Science , vol.115 , Issue.7 , pp. 1441-1451
    • Scott, G.1    Leopardi, S.2    Printup, S.3    Madden, B.C.4
  • 37
    • 0032211079 scopus 로고    scopus 로고
    • Synaptogenesis via dendritic filopodia in developing hippocampal area CA1
    • Fiala JC, Feinberg M, Popov V, Harris KM 1998 Synaptogenesis via dendritic filopodia in developing hippocampal area CA1. J Neurosci 18:8900-8911 (Pubitemid 28491754)
    • (1998) Journal of Neuroscience , vol.18 , Issue.21 , pp. 8900-8911
    • Fiala, J.C.1    Feinberg, M.2    Popov, V.3    Harris, K.M.4
  • 42
    • 0036320467 scopus 로고    scopus 로고
    • Contribution of Ena/VASP proteins to intracellular motility of Listeria requires phosphorylation and proline-rich core but not F-actin binding or multimerization
    • DOI 10.1091/mbc.E02-01-0058
    • Geese M, Loureiro JJ, Bear JE, Wehland J, Gertler FB, Sechi AS 2002 Contribution of Ena/VASP proteins to intracellular motility of listeria requires phosphorylation and proline-rich core but not F-actin binding or multimerization. Mol Biol Cell 13:2383-2396 (Pubitemid 34831342)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.7 , pp. 2383-2396
    • Geese, M.1    Loureiro, J.J.2    Bear, J.E.3    Wehland, J.4    Gertler, F.B.5    Sechi, A.S.6
  • 43
    • 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
    • DOI 10.1091/mbc.E01-10-0102
    • Loureiro JJ, Rubinson DA, Bear JE, Baltus GA, Kwiatkowski AV, Gertler FB 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 (Pubitemid 34831353)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.7 , 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
  • 44
    • 0033303548 scopus 로고    scopus 로고
    • Prolactin as a chemoattractant for human breast carcinoma
    • Maus MV, Reilly SC, Clevenger CV 1999 Prolactin as a chemoattractant for human breast carcinoma. Endocrinology 140:5447-5450 (Pubitemid 30687159)
    • (1999) Endocrinology , vol.140 , Issue.11 , pp. 5447-5450
    • Maus, M.V.1    Reilly, S.C.2    Clevenger, C.V.3
  • 46
    • 0028174290 scopus 로고
    • Prolactin-induced proliferation of Nb2 cells involves tyrosine phosphorylation of the prolactin receptor and its associated tyrosine kinase JAK2
    • Lebrun JJ, Ali S, Sofer L, Ullrich A, Kelly PA 1994 Prolactin-induced proliferation of Nb2 cells involves tyrosine phosphorylation of the prolactin receptor and its associated tyrosine kinase JAK2. J Biol Chem 269:14021-14026 (Pubitemid 2081885)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.19 , pp. 14021-14026
    • Lebrun, J.J.1    Ali, S.2    Sofer, L.3    Ullrich, A.4    Kelly, P.A.5
  • 47
    • 0027965825 scopus 로고
    • JAK2 activation and cell proliferation induced by antibody-mediated prolactin receptor dimerization
    • DOI 10.1210/en.135.4.1299
    • Rui H, Lebrun JJ, Kirken RA, Kelly PA, Farrar WL 1994 JAK2 activation and cell proliferation induced by antibody-mediated prolactin receptor dimerization. Endocrinology 135:1299-1306 (Pubitemid 24307502)
    • (1994) Endocrinology , vol.135 , Issue.4 , pp. 1299-1306
    • Rui, H.1    Lebrun, J.-J.2    Kirken, R.A.3    Kelly, P.A.4    Farrar, W.L.5
  • 48
    • 6344243617 scopus 로고    scopus 로고
    • SH2-B promotes insulin receptor substrate 1 (IRS1)- And IRS2-mediated activation of the phosphatidylinositol 3-kinase pathway in response to leptin
    • DOI 10.1074/jbc.M408495200
    • Duan C, Li M, Rui L 2004 SH2-B promotes insulin receptor substrate 1 (IRS1)- and IRS2-mediated activation of the phosphatidylinositol 3-kinase pathway in response to leptin. J Biol Chem 279:43684-43691 (Pubitemid 39390672)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.42 , pp. 43684-43691
    • Duan, C.1    Li, M.2    Rui, L.3
  • 49
    • 0027328678 scopus 로고
    • Stimulation of monocyte chemotaxis by human growth hormone and its deactivation by somatostatin
    • Wiedermann CJ, Reinisch N, Braunsteiner H 1993 Stimulation of monocyte chemotaxis by human growth hormone and its deactivation by somatostatin. Blood 82:954-960 (Pubitemid 23221681)
    • (1993) Blood , vol.82 , Issue.3 , pp. 954-960
    • Wiedermann, C.J.1    Reinisch, N.2    Braunsteiner, H.3
  • 50
    • 0030795552 scopus 로고    scopus 로고
    • Growth hormone-induced reorganization of the actin cytoskeleton is not required for STAT5 (signal transducer and activator of transcription-5)- Mediated transcription
    • DOI 10.1210/en.138.8.3207
    • Goh EL, Pircher TJ, Wood TJ, Norstedt G, Graichen R, Lobie PE 1997 Growth hormone-induced reorganization of the actin cytoskeleton is not required for STAT5 (signal transducer and activator of transcription-5)-mediated transcription. Endocrinology 138:3207-3215 (Pubitemid 27345670)
    • (1997) Endocrinology , vol.138 , Issue.8 , pp. 3207-3215
    • Goh, E.L.K.1    Pircher, T.J.2    Wood, T.J.J.3    Norstedt, G.4    Graichen, R.5    Lobie, P.E.6
  • 53
    • 44349179335 scopus 로고    scopus 로고
    • Filopodia: Molecular architecture and cellular functions
    • DOI 10.1038/nrm2406, PII NRM2406
    • Mattila PK, Lappalainen P 2008 Filopodia: molecular architecture and cellular functions. Nat Rev Mol Cell Biol 9:446-454 (Pubitemid 351733400)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.6 , pp. 446-454
    • Mattila, P.K.1    Lappalainen, P.2
  • 54
    • 36749024118 scopus 로고    scopus 로고
    • Filopodia: The fingers that do the walking
    • Gupton SL, Gertler FB 2007 Filopodia: the fingers that do the walking. Sci STKE 2007:re5
    • (2007) Sci STKE , vol.2007
    • Gupton, S.L.1    Gertler, F.B.2
  • 55
    • 12544253725 scopus 로고    scopus 로고
    • The Rho family GTPase Rif induces filopodia through mDia2
    • Pellegrin S, Mellor H 2005 The Rho family GTPase Rif induces filopodia through mDia2. Curr Biol 15:129-133
    • (2005) Curr Biol , vol.15 , pp. 129-133
    • Pellegrin, S.1    Mellor, H.2
  • 56
    • 0036122307 scopus 로고    scopus 로고
    • Myosin-X is an unconventional myosin that undergoes intrafilopodial motility
    • DOI 10.1038/ncb762
    • Berg JS, Cheney RE 2002 Myosin-X is an unconventional myosin that undergoes intrafilopodial motility. Nat Cell Biol 4:246-250 (Pubitemid 34218199)
    • (2002) Nature Cell Biology , vol.4 , Issue.3 , pp. 246-250
    • Berg, J.S.1    Cheney, R.E.2
  • 57
    • 20444426470 scopus 로고    scopus 로고
    • The Diaphanous-related formin dDia2 is required for the formation and maintenance of filopodia
    • DOI 10.1038/ncb1266
    • Schirenbeck A, Bretschneider T, Arasada R, Schleicher M, Faix J 2005 The Diaphanous-related formin dDia2 is required for the formation and maintenance of filopodia. Nat Cell Biol 7:619-625 (Pubitemid 40796985)
    • (2005) Nature Cell Biology , vol.7 , Issue.6 , pp. 619-625
    • Schirenbeck, A.1    Bretschneider, T.2    Arasada, R.3    Schleicher, M.4    Faix, J.5
  • 58
    • 37249003725 scopus 로고    scopus 로고
    • Novel roles of formin mDia2 in lamellipodia and filopodia formation in motile cells
    • DOI 10.1371/journal.pbio.0050317
    • Yang C, Czech L, Gerboth S, Kojima S, Scita G, Svitkina T 2007 Novel roles of formin mDia2 in lamellipodia and filopodia formation in motile cells. PLoS Biol 5:e317 (Pubitemid 350276935)
    • (2007) PLoS Biology , vol.5 , Issue.11 , pp. 2624-2645
    • Yang, C.1    Czech, L.2    Gerboth, S.3    Kojima, S.-I.4    Scita, G.5    Svitkina, T.6
  • 59
    • 0036498546 scopus 로고    scopus 로고
    • The lamellipodium: Where motility begins
    • DOI 10.1016/S0962-8924(01)02237-1, PII S0962892401022371
    • Small JV, Stradal T, Vignal E, Rottner K 2002 The lamellipodium: where motility begins. Trends Cell Biol 12:112-120 (Pubitemid 34164650)
    • (2002) Trends in Cell Biology , vol.12 , Issue.3 , pp. 112-120
    • Small, J.V.1    Stradal, T.2    Vignal, E.3    Rottner, K.4
  • 60
    • 0030864520 scopus 로고    scopus 로고
    • A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family
    • Niebuhr K, Ebel F, Frank R, Reinhard M, Domann E, Carl UD, Walter U, Gertler FB, Wehland J, Chakraborty T 1997 A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family. EMBO J 16:5433-5444
    • (1997) EMBO J , vol.16 , pp. 5433-5444
    • Niebuhr, K.1    Ebel, F.2    Frank, R.3    Reinhard, M.4    Domann, E.5    Carl, U.D.6    Walter, U.7    Gertler, F.B.8    Wehland, J.9    Chakraborty, T.10
  • 61
    • 0029807736 scopus 로고    scopus 로고
    • The tandem repeat domain in the Listeria monocytogenes ActA protein controls the rate of actin-based motility, the percentage of moving bacteria, and the localization of vasodilator-stimulated phosphoprotein and profilin
    • Smith GA, Theriot JA, Portnoy DA 1996 The tandem repeat domain in the Listeria monocytogenes ActA protein controls the rate of actin-based motility, the percentage of moving bacteria, and the localization of vasodilator- stimulated phosphoprotein and profilin. J Cell Biol 135:647-660
    • (1996) J Cell Biol , vol.135 , pp. 647-660
    • Smith, G.A.1    Theriot, J.A.2    Portnoy, D.A.3
  • 62
    • 0035955727 scopus 로고    scopus 로고
    • ActA from Listeria monocytogenes can interact with up to four Ena/VASP homology 1 domains simultaneously
    • Machner MP, Urbanke C, Barzik M, Otten S, Sechi AS, Wehland J, Heinz DW 2001 ActA from Listeria monocytogenes can interact with up to four Ena/VASP homology 1 domains simultaneously. J Biol Chem 276:40096-40103
    • (2001) J Biol Chem , vol.276 , pp. 40096-40103
    • Machner, M.P.1    Urbanke, C.2    Barzik, M.3    Otten, S.4    Sechi, A.S.5    Wehland, J.6    Heinz, D.W.7
  • 64
    • 12044259376 scopus 로고
    • Membrane ruffling and signal transduction
    • Ridley AJ 1994 Membrane ruffling and signal transduction. Bioessays 16:321-327 (Pubitemid 2084281)
    • (1994) BioEssays , vol.16 , Issue.5 , pp. 321-327
    • Ridley, A.J.1
  • 65
    • 8344250882 scopus 로고    scopus 로고
    • Membrane ruffles in cell migration: Indicators of inefficient lamellipodia adhesion and compartments of actin filament reorganization
    • DOI 10.1016/j.yexcr.2004.08.034, PII S0014482704005142
    • Borm B, Requardt RP, Herzog V, Kirfel G 2005 Membrane ruffles in cell migration: indicators of inefficient lamellipodia adhesion and compartments of actin filament reorganization. Exp Cell Res 302:83-95 (Pubitemid 39482370)
    • (2005) Experimental Cell Research , vol.302 , Issue.1 , pp. 83-95
    • Borm, B.1    Requardt, R.P.2    Herzog, V.3    Kirfel, G.4
  • 66
    • 0038146905 scopus 로고    scopus 로고
    • YXXL motifs in SH2-Bβ are phosphorylated by JAK2, JAK1, and platelet-derived growth factor receptor and are required for membrane ruffling
    • DOI 10.1074/jbc.M210765200
    • O'Brien KB, Argetsinger LS, Diakonova M, Carter-Su C 2003 YXXL motifs in SH2-Bβ are phosphorylated by JAK2, JAK1, and platelet-derived growth factor receptor and are required for membrane ruffling. J Biol Chem 278:11970-11978 (Pubitemid 36800171)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.14 , pp. 11970-11978
    • O'Brien, K.B.1    Argetsinger, L.S.2    Diakonova, M.3    Carter-Su, C.4
  • 67
    • 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, Halbrügge M, Scheer U, Wiegand C, Jockusch BM, 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    Halbrügge, M.2    Scheer, U.3    Wiegand, C.4    Jockusch, B.M.5    Walter, U.6
  • 68
    • 0027170920 scopus 로고
    • SH3 domains direct cellular localization of signaling molecules
    • DOI 10.1016/0092-8674(93)90296-3
    • Bar-Sagi D, Rotin D, Batzer A, Mandiyan V, Schlessinger J 1993 SH3 domains direct cellular localization of signaling molecules. Cell 74:83-91 (Pubitemid 23219880)
    • (1993) Cell , vol.74 , Issue.1 , pp. 83-91
    • Bar-Sagi, D.1    Rotin, D.2    Batzer, A.3    Mandiyan, V.4    Schlessinger, J.5
  • 69
    • 0024542907 scopus 로고
    • Rapid phosphorylation and reorganization of ezrin and spectrin accompany morphological changes induced in A-431 cells by epidermal growth factor
    • DOI 10.1083/jcb.108.3.921
    • Bretscher A 1989 Rapid phosphorylation and reorganization of ezrin and spectrin accompany morphological changes induced in A-431 cells by epidermal growth factor. J Cell Biol 108:921-930 (Pubitemid 19083743)
    • (1989) Journal of Cell Biology , vol.108 , Issue.3 , pp. 921-930
    • Bretscher, A.1
  • 70
  • 71
    • 0027222202 scopus 로고
    • Binding of the α-fodrin SH3 domain to the leading lamellae of locomoting chicken fibroblasts
    • Merilainen J, Palovuori R, Sormunen R, Wasenius VM, Lehto VP 1993 Binding of the α-fodrin SH3 domain to the leading lamellae of locomoting chicken fibroblasts. J Cell Sci 105(Pt 3):647-654 (Pubitemid 23243197)
    • (1993) Journal of Cell Science , vol.105 , Issue.3 , pp. 647-654
    • Merilainen, J.1    Palovuori, R.2    Sormunen, R.3    Wasenius, V.-M.4    Lehto, V.-P.5
  • 72
    • 0027419589 scopus 로고
    • Cortactin, an 80/85-kilodalton pp60(src) substrate, is a filamentous actin-binding protein enriched in the cell cortex
    • Wu H, Parsons JT 1993 Cortactin, an 80/85-kilodalton pp60src substrate, is a filamentous actin-binding protein enriched in the cell cortex. J Cell Biol 120:1417-1426 (Pubitemid 23081688)
    • (1993) Journal of Cell Biology , vol.120 , Issue.6 , pp. 1417-1426
    • Wu, H.1    Parsons, J.T.2
  • 73
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: A physically integrated molecular process
    • DOI 10.1016/S0092-8674(00)81280-5
    • Lauffenburger DA, Horwitz AF 1996 Cell migration: a physically integrated molecular process. Cell 84:359-369 (Pubitemid 26058561)
    • (1996) Cell , vol.84 , Issue.3 , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 74
    • 0036899655 scopus 로고    scopus 로고
    • The JAK/STAT pathway in model organisms: Emerging roles in cell movement
    • DOI 10.1016/S1534-5807(02)00376-3
    • Hou SX, Zheng Z, Chen X, Perrimon N 2002 The Jak/STAT pathway in model organisms: emerging roles in cell movement. Dev Cell 3:765-778 (Pubitemid 35460778)
    • (2002) Developmental Cell , vol.3 , Issue.6 , pp. 765-778
    • Hou, S.X.1    Zheng, Z.2    Chen, X.3    Perrimon, N.4
  • 75
    • 0034004130 scopus 로고    scopus 로고
    • Differential binding to and regulation of JAK2 by the SH2 domain and N- Terminal region of SH2-Bβ
    • DOI 10.1128/MCB.20.9.3168-3177.2000
    • Rui L, Gunter DR, Herrington J, Carter-Su C 2000 Differential binding to and regulation of JAK2 by the SH2 domain and N-terminal region of SH2-Bβ. Mol Cell Biol 20:3168-3177 (Pubitemid 30215029)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.9 , pp. 3168-3177
    • Rui, L.1    Gunter, D.R.2    Herrington, J.3    Carter-Su, C.4
  • 77
    • 0017687926 scopus 로고
    • The phagokinetic tracks of 3T3 cells
    • Albrecht-Buehler G 1977 The phagokinetic tracks of 3T3 cells. Cell 11:395-404 (Pubitemid 8139150)
    • (1977) Cell , vol.11 , Issue.2 , pp. 395-404
    • Albrecht Buehler, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.