메뉴 건너뛰기




Volumn 141, Issue 7, 1998, Pages 1675-1684

The laminin-nidogen complex is a ligand for a specific splice isoform of the transmembrane protein tyrosine phosphatase LAR

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ENTACTIN; FIBRONECTIN; HYBRID PROTEIN; IMMUNOGLOBULIN; LAMININ; LIGAND; PROTEIN; PROTEIN TYROSINE PHOSPHATASE;

EID: 15444357989     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.141.7.1675     Document Type: Article
Times cited : (119)

References (43)
  • 1
    • 0027936858 scopus 로고
    • Induction of tyrosine phosphorylation during ICAM-3 and LFA-1-mediated intercellular adhesion and its regulation by the CD45 tyrosine phosphatase
    • Arroyo, A.G., M.R. Campanero, P. Sánchez-Mateos, J.M. Zapata, M. Ursa, M. Angel del Pozo, and F. Sánchez-Madrid. 1994. Induction of tyrosine phosphorylation during ICAM-3 and LFA-1-mediated intercellular adhesion and its regulation by the CD45 tyrosine phosphatase. J. Cell Biol. 126:1277-1286.
    • (1994) J. Cell Biol. , vol.126 , pp. 1277-1286
    • Arroyo, A.G.1    Campanero, M.R.2    Sánchez-Mateos, P.3    Zapata, J.M.4    Ursa, M.5    Angel Del Pozo, M.6    Sánchez-Madrid, F.7
  • 3
    • 0027279623 scopus 로고
    • Laminin receptors and laminin-binding proteins during tumor invasion and metastasis
    • Castronovo, V. 1993. Laminin receptors and laminin-binding proteins during tumor invasion and metastasis. Invasion Metastasis. 13:1-30.
    • (1993) Invasion Metastasis , vol.13 , pp. 1-30
    • Castronovo, V.1
  • 4
    • 0030968026 scopus 로고    scopus 로고
    • Laminin-induced clustering of dystroglycan on embryonic muscle cells: Comparison with agrin-induced clustering
    • Cohen, M.W., C. Jacobson, P.D. Yurchenco, G.E. Morris, and S. Carbonelto. 1997. Laminin-induced clustering of dystroglycan on embryonic muscle cells: comparison with agrin-induced clustering. J. Cell Biol. 136: 1047-1058.
    • (1997) J. Cell Biol. , vol.136 , pp. 1047-1058
    • Cohen, M.W.1    Jacobson, C.2    Yurchenco, P.D.3    Morris, G.E.4    Carbonelto, S.5
  • 5
    • 0029952315 scopus 로고    scopus 로고
    • The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase, contains a protein kinase domain, and has separate rac-specific and rho-specific guanine nucleotide exchange factor domains
    • Debant, A., C. Serra-Pagès, K. Seipel, S. O'Brien, M. Tang, and S.H. Park. 1996. The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase, contains a protein kinase domain, and has separate rac-specific and rho-specific guanine nucleotide exchange factor domains. Proc. Nat. Natl. Sci. USA. 93:5466-5471.
    • (1996) Proc. Nat. Natl. Sci. USA , vol.93 , pp. 5466-5471
    • Debant, A.1    Serra-Pagès, C.2    Seipel, K.3    O'Brien, S.4    Tang, M.5    Park, S.H.6
  • 6
    • 0028783349 scopus 로고
    • Role of laminin-nidogen complexes in basement membrane formation during embryonic development
    • Dziadek, M. 1995. Role of laminin-nidogen complexes in basement membrane formation during embryonic development. Experientia. 51:901-913.
    • (1995) Experientia , vol.51 , pp. 901-913
    • Dziadek, M.1
  • 7
    • 0026770311 scopus 로고
    • Cell surface β-1,4-galactosyltransferase is associates with the detergent-insoluble cytoskeleton on migrating mesenchymal cells
    • Eckstein, D.J., and B.D. Shur. 1992. Cell surface β-1,4-galactosyltransferase is associates with the detergent-insoluble cytoskeleton on migrating mesenchymal cells. Exp. Cell Res. 201:83-90.
    • (1992) Exp. Cell Res. , vol.201 , pp. 83-90
    • Eckstein, D.J.1    Shur, B.D.2
  • 8
    • 0029757511 scopus 로고    scopus 로고
    • GPI-anchored proteins, glycosphingolipids, and sphingomyelin are sequestered to caveolae only after crosslinking
    • Fujimoto, T. 1996. GPI-anchored proteins, glycosphingolipids, and sphingomyelin are sequestered to caveolae only after crosslinking. J. Histochem. Cytochem. 44:929-941.
    • (1996) J. Histochem. Cytochem. , vol.44 , pp. 929-941
    • Fujimoto, T.1
  • 9
    • 0030318850 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and protrusive structures of the growth cone
    • Goldberg, D.J., and D.Y. Wu. 1996. Tyrosine phosphorylation and protrusive structures of the growth cone. Perspect. Dev. Neurobiol. 4:183-192.
    • (1996) Perspect. Dev. Neurobiol. , vol.4 , pp. 183-192
    • Goldberg, D.J.1    Wu, D.Y.2
  • 11
    • 0029856505 scopus 로고    scopus 로고
    • Signal transduction in cell-matrix interactions
    • Guan, J.-L., and H.-C. Chen. 1996. Signal transduction in cell-matrix interactions. Int. Rev. Cytol. 168:81-121.
    • (1996) Int. Rev. Cytol. , vol.168 , pp. 81-121
    • Guan, J.-L.1    Chen, H.-C.2
  • 12
    • 0028838971 scopus 로고
    • Protein kinases and phosphatases: The yin and yang of protein phosphorylation and signaling
    • Hunter, T. 1995. Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling. Cell. 80:225-236.
    • (1995) Cell , vol.80 , pp. 225-236
    • Hunter, T.1
  • 15
    • 0020360978 scopus 로고
    • Isolation and characterization of type IV procollagen, laminin and heparan sulfate proteoglycan from the EHS sarcoma
    • Kleinman, H.K., M.L. McGarvey, L.A. Liotta, P.G. Robey, K. Tryggvason, and G.R. Martin. 1982. Isolation and characterization of type IV procollagen, laminin and heparan sulfate proteoglycan from the EHS sarcoma. Biochemistry. 21:6188-6193.
    • (1982) Biochemistry , vol.21 , pp. 6188-6193
    • Kleinman, H.K.1    McGarvey, M.L.2    Liotta, L.A.3    Robey, P.G.4    Tryggvason, K.5    Martin, G.R.6
  • 16
    • 0027055575 scopus 로고
    • Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase
    • Kornberg, L., E. Shelton, J.T. Parsons, M. Schaller, and R.L. Juliano. 1992. Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase. J. Biol. Chem. 267:23439-23442.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23439-23442
    • Kornberg, L.1    Shelton, E.2    Parsons, J.T.3    Schaller, M.4    Juliano, R.L.5
  • 17
    • 0030030320 scopus 로고    scopus 로고
    • The transmembrane tyrosine phosphatase DLAR controls motor axon guidance in Drosophila
    • Krueger, N.X., D. Van Vactor, H.I. Wan, W.M. Gelbart, C.S. Goodman, and H. Saito. 1996. The transmembrane tyrosine phosphatase DLAR controls motor axon guidance in Drosophila. Cell. 84:611-622.
    • (1996) Cell , vol.84 , pp. 611-622
    • Krueger, N.X.1    Van Vactor, D.2    Wan, H.I.3    Gelbart, W.M.4    Goodman, C.S.5    Saito, H.6
  • 18
    • 0029797378 scopus 로고    scopus 로고
    • Association between a transmembrane protein tyrosine phosphatase and the cadherin-catenin complex
    • Kypla, R.M., H. Su, and L.F. Reichardt. 1996. Association between a transmembrane protein tyrosine phosphatase and the cadherin-catenin complex. J. Cell Biol. 134:1519-1529.
    • (1996) J. Cell Biol. , vol.134 , pp. 1519-1529
    • Kypla, R.M.1    Su, H.2    Reichardt, L.F.3
  • 20
    • 0026496886 scopus 로고
    • The three-dimensional structure of the tenth type-III module of fibronectin: An insight into RGD-mediated interactions
    • Main, A.L., T.S. Harvey, M. Baron, J. Boyd, and I.D. Campbell. 1992. The three-dimensional structure of the tenth type-III module of fibronectin: an insight into RGD-mediated interactions. Cell. 71:671-678.
    • (1992) Cell , vol.71 , pp. 671-678
    • Main, A.L.1    Harvey, T.S.2    Baron, M.3    Boyd, J.4    Campbell, I.D.5
  • 22
    • 0030753274 scopus 로고    scopus 로고
    • Modulation of cell-adhesive activity of fibronectin by the alternatively spliced EDA segment
    • Manabe, R., N. Ohe, T. Maeda, T. Fukuda, and K. Sekiguchi. 1997. Modulation of cell-adhesive activity of fibronectin by the alternatively spliced EDA segment. J. Cell Biol. 139:295-307.
    • (1997) J. Cell Biol. , vol.139 , pp. 295-307
    • Manabe, R.1    Ohe, N.2    Maeda, T.3    Fukuda, T.4    Sekiguchi, K.5
  • 23
    • 0028954797 scopus 로고
    • Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function
    • Miyamoto, S., S.K. Akiyama, and K.M. Yamada. 1995. Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function. Science. 267:883-885.
    • (1995) Science , vol.267 , pp. 883-885
    • Miyamoto, S.1    Akiyama, S.K.2    Yamada, K.M.3
  • 24
    • 0027237709 scopus 로고
    • MPTPδ, a putative murine homolog of HPTPδ, is expressed in specialized regions of the brain and in the B-cell lineage
    • Mizuno, K., K. Hasegawa, T. Katagiri, M. Ogimoto, T. Ichikawa, and H. Yakura. 1993. MPTPδ, a putative murine homolog of HPTPδ, is expressed in specialized regions of the brain and in the B-cell lineage. Mol. Cell. Biol. 13:5513-5523.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5513-5523
    • Mizuno, K.1    Hasegawa, K.2    Katagiri, T.3    Ogimoto, M.4    Ichikawa, T.5    Yakura, H.6
  • 25
    • 0027984009 scopus 로고
    • Genomic organization of the human LAR protein tyrosine phosphatase gene and alternative splicing in the extracellular fibronectin type-III domains
    • O'Grady, P., N.X. Krueger, M. Streuli, and H. Saito. 1994. Genomic organization of the human LAR protein tyrosine phosphatase gene and alternative splicing in the extracellular fibronectin type-III domains. J. Biol. Chem. 269:25193-25199.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25193-25199
    • O'Grady, P.1    Krueger, N.X.2    Streuli, M.3    Saito, H.4
  • 26
    • 0028200723 scopus 로고
    • Salmonella typhimurium induces selective aggregation and internalization of host cell surface proteins during invasion of epithelial cells
    • Portillo. F., M. Pucciarelli, W. Jeffries, and B. Finlay. 1994. Salmonella typhimurium induces selective aggregation and internalization of host cell surface proteins during invasion of epithelial cells. J. Cell Sci. 107:2005-2020.
    • (1994) J. Cell Sci. , vol.107 , pp. 2005-2020
    • Portillo, F.1    Pucciarelli, M.2    Jeffries, W.3    Finlay, B.4
  • 27
    • 0030957735 scopus 로고    scopus 로고
    • Neuronal laminins and their cellular receptors
    • Powell, S.K., and H.K. Kleinman. 1997. Neuronal laminins and their cellular receptors. Int. J. Biochem. Cell Biol. 29:401-414.
    • (1997) Int. J. Biochem. Cell Biol. , vol.29 , pp. 401-414
    • Powell, S.K.1    Kleinman, H.K.2
  • 28
    • 0028934929 scopus 로고
    • Molecular characterization of the human transmembrane protein tyrosine phosphatase δ: Evidence for tissue-specific expression of alternative human transmembrane protein-tyrosine phosphatase ε isoforms
    • Pulido, R., N.X. Krueger, C. Serra-Pagès, H. Saito, and M. Streuli. 1995. Molecular characterization of the human transmembrane protein tyrosine phosphatase δ: evidence for tissue-specific expression of alternative human transmembrane protein-tyrosine phosphatase ε isoforms. J. Biol. Chem. 270:6722-6728.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6722-6728
    • Pulido, R.1    Krueger, N.X.2    Serra-Pagès, C.3    Saito, H.4    Streuli, M.5
  • 29
    • 0030601350 scopus 로고    scopus 로고
    • Common principles in cell adhesion
    • Ruoslahti, E., and B. Obrink. 1996. Common principles in cell adhesion. Exp. Cell Res. 227:1-11.
    • (1996) Exp. Cell Res. , vol.227 , pp. 1-11
    • Ruoslahti, E.1    Obrink, B.2
  • 31
    • 0029019297 scopus 로고
    • The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacling protein co-localize at focal adhesion
    • Serra-Pagès, C., N.L. Kedersha, L. Fazikas, Q. Medley, A. Debant, and M. Streuli. 1995. The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacling protein co-localize at focal adhesion. EMBO (Eur. Mol. Biol. Organ.) J. 14:2824-2838.
    • (1995) EMBO (Eur. Mol. Biol. Organ.) J. , vol.14 , pp. 2824-2838
    • Serra-Pagès, C.1    Kedersha, N.L.2    Fazikas, L.3    Medley, Q.4    Debant, A.5    Streuli, M.6
  • 32
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith, D.B., and K.S. Johnson. 1988. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene. 67:31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 33
    • 0029021132 scopus 로고
    • Axonal localization of the CAM-like tyrosine phosphatase CRYPα: A signaling molecule of embryonic growth cones
    • Stoker, A.W., B. Gehring, F. Haj, and B.-H. Bay. 1995. Axonal localization of the CAM-like tyrosine phosphatase CRYPα: a signaling molecule of embryonic growth cones. Development. 121:1833-1844.
    • (1995) Development , vol.121 , pp. 1833-1844
    • Stoker, A.W.1    Gehring, B.2    Haj, F.3    Bay, B.-H.4
  • 35
    • 0024211451 scopus 로고
    • A new member of the immunoglobulin superfamily that has a cytoplasmic region homologous to the leukocyte common antigen
    • Streuli, M., N.X. Krueger, L.R. Hall, S.F. Schlossman, and H. Saito. 1988. A new member of the immunoglobulin superfamily that has a cytoplasmic region homologous to the leukocyte common antigen. J. Exp. Med. 168:1523-1530.
    • (1988) J. Exp. Med. , vol.168 , pp. 1523-1530
    • Streuli, M.1    Krueger, N.X.2    Hall, L.R.3    Schlossman, S.F.4    Saito, H.5
  • 36
    • 0025277449 scopus 로고
    • Distinct functional roles of the two intracellular phosphatase like domains of the receptor-linked protein tyrosine phosphatases LCA and LAR
    • Streuli, M., N.X. Krueger, T. Thai, M. Tang, and H. Saito. 1990. Distinct functional roles of the two intracellular phosphatase like domains of the receptor-linked protein tyrosine phosphatases LCA and LAR. EMBO (Eur. Mol. Biol. Organ.) J. 9:2399-2407.
    • (1990) EMBO (Eur. Mol. Biol. Organ.) J. , vol.9 , pp. 2399-2407
    • Streuli, M.1    Krueger, N.X.2    Thai, T.3    Tang, M.4    Saito, H.5
  • 37
    • 0024378995 scopus 로고
    • A family of receptor-linked protein tyrosine phosphatases in humans and Drosophila
    • Streuli, M., N.X. Krueger, A.Y.M. Tsai, and H. Saito. 1989. A family of receptor-linked protein tyrosine phosphatases in humans and Drosophila. Proc. Natl. Acad. Sci. USA. 86:8698-8702.
    • (1989) Proc. Natl. Acad. Sci. USA. , vol.86 , pp. 8698-8702
    • Streuli, M.1    Krueger, N.X.2    Tsai, A.Y.M.3    Saito, H.4
  • 38
    • 0030879133 scopus 로고    scopus 로고
    • Laminin-induced acetylcholine receptor clustering: An alternative pathway
    • Sugiyama, J.E., D.J. Glass, G.D. Yancopoulos, and Z.W. Hall. 1997. Laminin-induced acetylcholine receptor clustering: an alternative pathway. J. Cell Biol. 139:181-191.
    • (1997) J. Cell Biol. , vol.139 , pp. 181-191
    • Sugiyama, J.E.1    Glass, D.J.2    Yancopoulos, G.D.3    Hall, Z.W.4
  • 39
    • 0031042493 scopus 로고    scopus 로고
    • Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton
    • Tapon, N., and A. Hall. 1997. Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton. Curr. Opin. Cell Biol. 9:86-92.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 86-92
    • Tapon, N.1    Hall, A.2
  • 41
    • 0031050449 scopus 로고    scopus 로고
    • Molecular interactions in cell adhesion complexes
    • Yamada, K., and B. Geiger. 1997. Molecular interactions in cell adhesion complexes. Curr. Opion. Cell Biol. 9:76-85.
    • (1997) Curr. Opion. Cell Biol. , vol.9 , pp. 76-85
    • Yamada, K.1    Geiger, B.2
  • 42
    • 0028926584 scopus 로고
    • LAR tyrosine phosphatasc receptor: Alternative splicing is preferential to the nervous system, coordinated with cell growth and generates novel isoforms containing extensive CAG repeats
    • Zhang, J.S., and F.M. Longo. 1995. LAR tyrosine phosphatasc receptor: alternative splicing is preferential to the nervous system, coordinated with cell growth and generates novel isoforms containing extensive CAG repeats. J. Cell Biol. 128:415-431.
    • (1995) J. Cell Biol. , vol.128 , pp. 415-431
    • Zhang, J.S.1    Longo, F.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.