메뉴 건너뛰기




Volumn 84, Issue 1-2, 1999, Pages 75-82

Identification of BAIAP2 (BAI-associated protein 2), a novel human homologue of hamster IRSp53, whose SH3 domain interacts with the cytoplasmic domain of BAI1

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ANGIOGENESIS INHIBITOR; CELL ADHESION MOLECULE; CELL PROTEIN; COMPLEMENTARY DNA; INSULIN RECEPTOR KINASE;

EID: 0032891376     PISSN: 03010171     EISSN: None     Source Type: Journal    
DOI: 10.1159/000015219     Document Type: Article
Times cited : (74)

References (40)
  • 1
    • 0029938472 scopus 로고    scopus 로고
    • A novel class of murine semaphorins with homology to thrombospondin is differentially expressed during early embryogenesis
    • Adams RH, Betz H, Puschel AW: A novel class of murine semaphorins with homology to thrombospondin is differentially expressed during early embryogenesis. Mech Dev 57:33-45 (1996).
    • (1996) Mech Dev , vol.57 , pp. 33-45
    • Adams, R.H.1    Betz, H.2    Puschel, A.W.3
  • 2
    • 0028800295 scopus 로고
    • Thrombospondin-4, an extracellular matrix protein expressed in the developing and adult nervous system promotes neunte outgrowth
    • Arber S, Caroni P: Thrombospondin-4, an extracellular matrix protein expressed in the developing and adult nervous system promotes neunte outgrowth. J Cell Biol 131:1083-1094 (1995).
    • (1995) J Cell Biol , vol.131 , pp. 1083-1094
    • Arber, S.1    Caroni, P.2
  • 3
    • 0026743906 scopus 로고
    • Identification of a protein that binds to the SH3 region of ab1 and is similar to Bcr and GAP-rho
    • Cicchetti P, Mayer BJ, Thiel G, Baltimore D: Identification of a protein that binds to the SH3 region of Ab1 and is similar to Bcr and GAP-rho. Science 257:803-806 (1992).
    • (1992) Science , vol.257 , pp. 803-806
    • Cicchetti, P.1    Mayer, B.J.2    Thiel, G.3    Baltimore, D.4
  • 4
    • 0026608178 scopus 로고
    • C. elegans cell-signalling gene sem-5 encodes a protein with SH2 and SH3 domains
    • Clark SG, Stern MJ, Horvitz HR: C. elegans cell-signalling gene sem-5 encodes a protein with SH2 and SH3 domains. Nature 356:340-344 (1992).
    • (1992) Nature , vol.356 , pp. 340-344
    • Clark, S.G.1    Stern, M.J.2    Horvitz, H.R.3
  • 5
    • 0028895654 scopus 로고
    • Modular binding domains in signal transduction proteins
    • Cohen GB, Ren R, Baltimore D: Modular binding domains in signal transduction proteins. Cell 80:237-48 (1995)
    • (1995) Cell , vol.80 , pp. 237-248
    • Cohen, G.B.1    Ren, R.2    Baltimore, D.3
  • 6
    • 0025814801 scopus 로고
    • Arginyl-glycyl-spartic acid (RGD): A cell adhesion motif
    • D'Souza SE, Ginsberg MH, Plow EF: Arginyl-glycyl-spartic acid (RGD): a cell adhesion motif. Trends Biochem Sci 16:246-250 (1991).
    • (1991) Trends Biochem Sci , vol.16 , pp. 246-250
    • D'Souza, S.E.1    Ginsberg, M.H.2    Plow, E.F.3
  • 8
    • 0027962645 scopus 로고
    • Two binding orientations for peptides to the Src SH3 domain: Development of a general model for SH3-ligand interactions
    • Feng S, Chen JK, Yu H, Simon JA, Schreiber SL: Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions. Science 266:1241-1247 (1994).
    • (1994) Science , vol.266 , pp. 1241-1247
    • Feng, S.1    Chen, J.K.2    Yu, H.3    Simon, J.A.4    Schreiber, S.L.5
  • 9
    • 0030318850 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and protrusive structures of the growth cone
    • Goldberg DJ, Wu DY: Tyrosine phosphorylation and protrusive structures of the growth cone. Perspect Dev Neurobiol 4:183-192 (1996).
    • (1996) Perspect Dev Neurobiol , vol.4 , pp. 183-192
    • Goldberg, D.J.1    Wu, D.Y.2
  • 10
    • 0028142840 scopus 로고
    • Integrin-ligand interactions: A year in review
    • Haas TA, Plow EF: Integrin-ligand interactions: a year in review. Curr Opin Cell Biol 6:656-662 (1994).
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 656-662
    • Haas, T.A.1    Plow, E.F.2
  • 11
    • 0029906430 scopus 로고    scopus 로고
    • A role for the FGF receptor in the axonal growth response stimulated by cell adhesion molecules?
    • Hall H, Walsh FS, Doherty P: A role for the FGF receptor in the axonal growth response stimulated by cell adhesion molecules? Cell Adhes Commun 3:441-450 (1996).
    • (1996) Cell Adhes Commun , vol.3 , pp. 441-450
    • Hall, H.1    Walsh, F.S.2    Doherty, P.3
  • 12
    • 0027209470 scopus 로고
    • High-resolution cytogenetic mapping of 342 new cosmid markers including 43 RFLP markers on human chromosome 17 by fluorescence in situ hybridization
    • Inazawa J, Saito H, Ariyama T, Abe T, Nakamura Y: High-resolution cytogenetic mapping of 342 new cosmid markers including 43 RFLP markers on human chromosome 17 by fluorescence in situ hybridization. Genomics 17:153-162 (1993).
    • (1993) Genomics , vol.17 , pp. 153-162
    • Inazawa, J.1    Saito, H.2    Ariyama, T.3    Abe, T.4    Nakamura, Y.5
  • 13
    • 0028882810 scopus 로고
    • Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases
    • Kim E, Niethammer M, Rothschild A, Jan YN, Sheng M: Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases. Nature 378:85-88 (1995).
    • (1995) Nature , vol.378 , pp. 85-88
    • Kim, E.1    Niethammer, M.2    Rothschild, A.3    Jan, Y.N.4    Sheng, M.5
  • 14
    • 0026770381 scopus 로고
    • F-spondin: A gene expressed at high levels in the floor plate encodes a secreted protein that promotes neural cell adhesion and neunte extension
    • Klar A, Baldassare M, Jessell TM: F-spondin: a gene expressed at high levels in the floor plate encodes a secreted protein that promotes neural cell adhesion and neunte extension. Cell 69:95-110 (1992).
    • (1992) Cell , vol.69 , pp. 95-110
    • Klar, A.1    Baldassare, M.2    Jessell, T.M.3
  • 15
    • 0030296445 scopus 로고    scopus 로고
    • Growth cones and the cues that repel them
    • Kolodkin AL: Growth cones and the cues that repel them. Trends Neurosci 19:507-513 (1996).
    • (1996) Trends Neurosci , vol.19 , pp. 507-513
    • Kolodkin, A.L.1
  • 16
    • 0029098659 scopus 로고
    • Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95
    • Kornau HC, Schenker LT, Kennedy MB, Seeburg PH: Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95. Science 269:1737-1740 (1995).
    • (1995) Science , vol.269 , pp. 1737-1740
    • Kornau, H.C.1    Schenker, L.T.2    Kennedy, M.B.3    Seeburg, P.H.4
  • 17
    • 0026753387 scopus 로고
    • UNC-5, a transmembrane protein with immunoglobulin and thrombospondin type 1 domains, guides cell and pioneer axon migrations in C. elegans
    • Leung-Hagesteijn C, Spence AM, Stern BD, Zhou Y, Su MW, Hedgecock EM, Culotti JG: UNC-5, a transmembrane protein with immunoglobulin and thrombospondin type 1 domains, guides cell and pioneer axon migrations in C. elegans. Cell 71:289-299 (1992).
    • (1992) Cell , vol.71 , pp. 289-299
    • Leung-Hagesteijn, C.1    Spence, A.M.2    Stern, B.D.3    Zhou, Y.4    Su, M.W.5    Hedgecock, E.M.6    Culotti, J.G.7
  • 18
    • 0030319532 scopus 로고    scopus 로고
    • Selective neural cell adhesion molecule signaling by Src family tyrosine kinases and tyrosine phosphatases
    • Maness PF, Beggs HE, Klinz SG, Morse WR: Selective neural cell adhesion molecule signaling by Src family tyrosine kinases and tyrosine phosphatases. Perspect Dev Neurobiol 4:169-181 (1996).
    • (1996) Perspect Dev Neurobiol , vol.4 , pp. 169-181
    • Maness, P.F.1    Beggs, H.E.2    Klinz, S.G.3    Morse, W.R.4
  • 19
    • 0027507115 scopus 로고
    • Signaling through SH2 and SH3 domains
    • Mayer B, Baltimore D: Signaling through SH2 and SH3 domains. Trends Cell Biol 3:8-13 (1993).
    • (1993) Trends Cell Biol , vol.3 , pp. 8-13
    • Mayer, B.1    Baltimore, D.2
  • 20
    • 0024234650 scopus 로고
    • Complete amino acid sequence of the neuron-specific gamma isozyme of enolase (NSE) from human brain and comparison with the non-neuronal alpha form (NNE)
    • McAleese SM, Dunbar B, Fothergill JE, Hinks LJ, Day IN: Complete amino acid sequence of the neuron-specific gamma isozyme of enolase (NSE) from human brain and comparison with the non-neuronal alpha form (NNE). Eur J Biochem 178:413-417 (1988).
    • (1988) Eur J Biochem , vol.178 , pp. 413-417
    • McAleese, S.M.1    Dunbar, B.2    Fothergill, J.E.3    Hinks, L.J.4    Day, I.N.5
  • 21
    • 0011060784 scopus 로고
    • Growth-associated protein, GAP-43, a polypeptide that is induced when neurons extend axons, is a component of growth cones and corresponds to pp46, a major polypeptide of a subcellular fraction enriched in growth cones
    • Meiri KF, Pfenninger KH, Willard MB: Growth-associated protein, GAP-43, a polypeptide that is induced when neurons extend axons, is a component of growth cones and corresponds to pp46, a major polypeptide of a subcellular fraction enriched in growth cones. Proc natl Acad Sci, USA 83:3537-3541 (1986).
    • (1986) Proc Natl Acad Sci, USA , vol.83 , pp. 3537-3541
    • Meiri, K.F.1    Pfenninger, K.H.2    Willard, M.B.3
  • 22
    • 0026749753 scopus 로고
    • SH3 -an abundant protein domain in search of a function
    • Musacchio A, Gibson T, Lehto VP, Saraste M: SH3 -an abundant protein domain in search of a function. FEBS Lett 307:55-61 (1992).
    • (1992) FEBS Lett , vol.307 , pp. 55-61
    • Musacchio, A.1    Gibson, T.2    Lehto, V.P.3    Saraste, M.4
  • 24
    • 0026505764 scopus 로고
    • Thrombospondin promotes process outgrowth in neurons from the peripheral and central nervous systems
    • Osterhout DJ, Frazier WA, Higgins D: Thrombospondin promotes process outgrowth in neurons from the peripheral and central nervous systems. Dev Biol 150:256-265 (1992).
    • (1992) Dev Biol , vol.150 , pp. 256-265
    • Osterhout, D.J.1    Frazier, W.A.2    Higgins, D.3
  • 25
    • 0028859279 scopus 로고
    • Protein modules and signaling networks
    • Pawson T: Protein modules and signaling networks. Nature 373:573-80 (1995).
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 26
    • 0021089398 scopus 로고
    • Nerve growth cones isolated from fetal rat brain: Subcellular fractionation and characterization
    • Pfenninger KH, Ellis L, Johnson MP, Friedman LB, Somlo S: Nerve growth cones isolated from fetal rat brain: subcellular fractionation and characterization. Cell 35:573-584 (1983).
    • (1983) Cell , vol.35 , pp. 573-584
    • Pfenninger, K.H.1    Ellis, L.2    Johnson, M.P.3    Friedman, L.B.4    Somlo, S.5
  • 27
    • 0024328787 scopus 로고
    • Molecular cloning and primary structure of human glial fibrillary acidic protein
    • Reeves SA, Helman LJ, Allison A, Israel MA: Molecular cloning and primary structure of human glial fibrillary acidic protein. Proc natl Acad Sci, USA 86:5178-5182 (1989).
    • (1989) Proc Natl Acad Sci, USA , vol.86 , pp. 5178-5182
    • Reeves, S.A.1    Helman, L.J.2    Allison, A.3    Israel, M.A.4
  • 28
    • 0027408247 scopus 로고
    • Identification of a ten-amino acid proline-rich SH3 binding site
    • Ren R, Mayer BJ, Cicchetti P, Baltimore D: Identification of a ten-amino acid proline-rich SH3 binding site. Science 259:1157-1161 (1993).
    • (1993) Science , vol.259 , pp. 1157-1161
    • Ren, R.1    Mayer, B.J.2    Cicchetti, P.3    Baltimore, D.4
  • 29
    • 0030739938 scopus 로고    scopus 로고
    • The SH3p4/ Sh3p8/SH3p13 protein family: Binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain
    • Ringstad N, Nemoto Y, De Camilli P: The SH3p4/ Sh3p8/SH3p13 protein family: binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain. Proc natl Acad Sci, USA 94:8569-8574 (1997).
    • (1997) Proc Natl Acad Sci, USA , vol.94 , pp. 8569-8574
    • Ringstad, N.1    Nemoto, Y.2    De Camilli, P.3
  • 30
    • 0032577870 scopus 로고    scopus 로고
    • Cloning and characterization of BAP1 (BAI-associated protein 1): A PDZ domain-containing protein that interacts with BAI1
    • Shiratsuchi T, Futamura M, Oda K, Nishimori H, Nakamura Y, Tokino T: Cloning and characterization of BAP1 (BAI-associated protein 1): a PDZ domain-containing protein that interacts with BAI1. Biochem biophys Res Commun 247:597-604 (1998).
    • (1998) Biochem Biophys Res Commun , vol.247 , pp. 597-604
    • Shiratsuchi, T.1    Futamura, M.2    Oda, K.3    Nishimori, H.4    Nakamura, Y.5    Tokino, T.6
  • 32
    • 0031967521 scopus 로고    scopus 로고
    • An emerging link between cytoskeletal dynamics and cell adhesion molecules in growth cone guidance
    • Suter DM, Forscher P: An emerging link between cytoskeletal dynamics and cell adhesion molecules in growth cone guidance. Curr Opin Neurobiol 8:106-116 (1998).
    • (1998) Curr Opin Neurobiol , vol.8 , pp. 106-116
    • Suter, D.M.1    Forscher, P.2
  • 33
    • 0028863477 scopus 로고
    • Making the connection: Cytoskeletal rearrangements during growth cone guidance
    • Tanaka E, Sabry J: Making the connection: cytoskeletal rearrangements during growth cone guidance. Cell 83:171-176 (1995).
    • (1995) Cell , vol.83 , pp. 171-176
    • Tanaka, E.1    Sabry, J.2
  • 36
    • 12644286553 scopus 로고    scopus 로고
    • Cell signaling and CAM-mediated neurite outgrowth
    • Walsh FS, Meiri K, Doherty P: Cell signaling and CAM-mediated neurite outgrowth. Soc Gen Physiol Ser 52:221-226 (1997).
    • (1997) Soc Gen Physiol Ser , vol.52 , pp. 221-226
    • Walsh, F.S.1    Meiri, K.2    Doherty, P.3
  • 37
    • 0031553972 scopus 로고    scopus 로고
    • Examining the specificity of Src homology 3 domain-ligand interactions with alkaline phosphatase fusion proteins
    • Yamabhai M, Kay BK: Examining the specificity of Src homology 3 domain-ligand interactions with alkaline phosphatase fusion proteins. Anal Biochem 247:143-151 (1997).
    • (1997) Anal Biochem , vol.247 , pp. 143-151
    • Yamabhai, M.1    Kay, B.K.2
  • 38
    • 0031964941 scopus 로고    scopus 로고
    • Disruption of a putative SH3 domain and the proline-rich motifs in the 53-kDa substrate of the insulin receptor kinase does not alter its subcellular localization or ability to serve as a substrate
    • Yeh TC, Li W, Keller GA, Roth RA: Disruption of a putative SH3 domain and the proline-rich motifs in the 53-kDa substrate of the insulin receptor kinase does not alter its subcellular localization or ability to serve as a substrate. J cell Biochem 68:139-150 (1998).
    • (1998) J Cell Biochem , vol.68 , pp. 139-150
    • Yeh, T.C.1    Li, W.2    Keller, G.A.3    Roth, R.A.4
  • 39
    • 0030020789 scopus 로고    scopus 로고
    • Characterization and cloning of a 58/53-kDa substrate of the insulin receptor tyrosine kinase
    • Yeh TC, Ogawa W, Danielsen AG, Roth RA: Characterization and cloning of a 58/53-kDa substrate of the insulin receptor tyrosine kinase. J biol Chem 271:2921-2928 (1996).
    • (1996) J Biol Chem , vol.271 , pp. 2921-2928
    • Yeh, T.C.1    Ogawa, W.2    Danielsen, A.G.3    Roth, R.A.4
  • 40
    • 0013484134 scopus 로고
    • Structural basis for the binding of proline-rich peptides to SH3 domains
    • Yu H, Chen JK, Feng S, Dalgamo DC, Brauer AW, Schreiber SL: Structural basis for the binding of proline-rich peptides to SH3 domains. Cell 76:933-945 (1994).
    • (1994) Cell , vol.76 , pp. 933-945
    • Yu, H.1    Chen, J.K.2    Feng, S.3    Dalgamo, D.C.4    Brauer, A.W.5    Schreiber, S.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.