메뉴 건너뛰기




Volumn 14, Issue 4, 1997, Pages 391-398

On the origin of metazoan adhesion receptors: Cloning of integrin α subunit from the sponge Geodia cydonium

Author keywords

animals; eumetazoa; Geodia cydonium; integrin; monophyly

Indexed keywords

COMPLEMENTARY DNA; INTEGRIN; RNA;

EID: 0030937506     PISSN: 07374038     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.molbev.a025775     Document Type: Article
Times cited : (98)

References (46)
  • 1
    • 0028245538 scopus 로고
    • Evidence for cell surface extracellular matrix binding proteins in Hydra vulgaris
    • AGBAS, A. and M. P. SARRAS. 1994. Evidence for cell surface extracellular matrix binding proteins in Hydra vulgaris. Cell Adhes. Commun. 2:59-73.
    • (1994) Cell Adhes. Commun. , vol.2 , pp. 59-73
    • Agbas, A.1    Sarras, M.P.2
  • 3
    • 0023663872 scopus 로고
    • The Drosophila PS2 antigen is an invertebrate integrin that, like the fibronectin receptor, becomes localized to muscle attachments
    • BOGAERT, T., N. BROWN, and M. WILLCOX. 1987. The Drosophila PS2 antigen is an invertebrate integrin that, like the fibronectin receptor, becomes localized to muscle attachments. Cell 51:929-940.
    • (1987) Cell , vol.51 , pp. 929-940
    • Bogaert, T.1    Brown, N.2    Willcox, M.3
  • 4
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • CLARK, E. A., and J. S. BRUGGE. 1995. Integrins and signal transduction pathways: the road taken. Science 268:233-239.
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 5
    • 0025865325 scopus 로고
    • Laminin receptors in the retina: Sequence analysis of the chick integrin α6 subunit
    • CURTIS, I. DE, V. QUARANTA, R. N. TAMURA, and L. F. REICHARDT. 1991. Laminin receptors in the retina: sequence analysis of the chick integrin α6 subunit. J. Cell Biol. 113: 405-416.
    • (1991) J. Cell Biol. , vol.113 , pp. 405-416
    • De Curtis, I.1    Quaranta, V.2    Tamura, R.N.3    Reichardt, L.F.4
  • 6
    • 0000228203 scopus 로고
    • A model of evolutionary change in protein
    • M. O. DAYHOFF, ed. National Biomedical Research Foundation, Washington, D.C.
    • DAYHOFF, M. O., R. M. SCHWARTZ, and B. C. ORCUTT. 1978. A model of evolutionary change in protein. Pp. 345-352 in M. O. DAYHOFF, ed. Atlas of protein sequence and structure. National Biomedical Research Foundation, Washington, D.C.
    • (1978) Atlas of Protein Sequence and Structure , pp. 345-352
    • Dayhoff, M.O.1    Schwartz, R.M.2    Orcutt, B.C.3
  • 8
    • 0025216612 scopus 로고
    • The ligand binding site of the platelet integrin receptor GPIIb-IIIa is proximal to the second calcium binding domain of its subunit
    • D'SOUZA, S. E., M. H. GINSBERG, T. A. BURKE, and E. F. PLOW. 1990. The ligand binding site of the platelet integrin receptor GPIIb-IIIa is proximal to the second calcium binding domain of its subunit. J. Biol. Chem. 265:3440-3446.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3440-3446
    • D'Souza, S.E.1    Ginsberg, M.H.2    Burke, T.A.3    Plow, E.F.4
  • 9
    • 0025016078 scopus 로고
    • Characterization of a fibrillar collagen gene in sponges reveals the early evolutionary appearance of two collagen families
    • EXPOSITIO, J. Y., and R. GARRONE. 1990. Characterization of a fibrillar collagen gene in sponges reveals the early evolutionary appearance of two collagen families. Proc. Natl. Acad. Sci. USA 87:6669-6673.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6669-6673
    • Expositio, J.Y.1    Garrone, R.2
  • 10
    • 0003437299 scopus 로고
    • University of Washington, Seattle, Wash.
    • FELSENSTEIN, J. 1993. PHYLIP. Version 3.5. University of Washington, Seattle, Wash.
    • (1993) PHYLIP. Version 3.5
    • Felsenstein, J.1
  • 11
    • 0028501036 scopus 로고
    • Cell adhesion receptors and nuclear receptors are highly conserved from the lowest Metazoa [marine sponges] to vertebrates
    • GAMULIN, V., B. RINKEVICH, H. SCHÄCKE, M. KRUSE, I. M. MÜLLER, and W. E. G. MÜLLER. 1994. Cell adhesion receptors and nuclear receptors are highly conserved from the lowest Metazoa [marine sponges] to vertebrates. Biol. Chem. Hoppe Seyler 375:583-588.
    • (1994) Biol. Chem. Hoppe Seyler , vol.375 , pp. 583-588
    • Gamulin, V.1    Rinkevich, B.2    Schäcke, H.3    Kruse, M.4    Müller, I.M.5    Müller, W.E.G.6
  • 13
    • 0011245335 scopus 로고
    • Formation and involvement of extracellular matrix in the development of sponges, a primitive multicellular system
    • R. L. TRELSTAD, ed. A. R. Liss, New York
    • _. 1984. Formation and involvement of extracellular matrix in the development of sponges, a primitive multicellular system. Pp. 461-477 in R. L. TRELSTAD, ed. The role of extracellular matrix in development. A. R. Liss, New York.
    • (1984) The Role of Extracellular Matrix in Development , pp. 461-477
  • 14
    • 0026249489 scopus 로고
    • Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120 kDa protein
    • GUAN, J. L., J. E. TREVITHICK, and R. O. HYNES. 1991. Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120 kDa protein. Cell Regulat. 2:951-964.
    • (1991) Cell Regulat. , vol.2 , pp. 951-964
    • Guan, J.L.1    Trevithick, J.E.2    Hynes, R.O.3
  • 16
    • 0027169990 scopus 로고
    • The family of metazoan metal-independent β-galactoside-binding lectins: Structure, function and molecular evolution
    • HIRABAYASHI, J., and K. KASAI. 1993. The family of metazoan metal-independent β-galactoside-binding lectins: structure, function and molecular evolution. Glycobiology 3:297-304.
    • (1993) Glycobiology , vol.3 , pp. 297-304
    • Hirabayashi, J.1    Kasai, K.2
  • 17
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation and signaling in cell adhesion
    • HYNES, R. O. 1992. Integrins: versatility, modulation and signaling in cell adhesion. Cell 69:11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 19
    • 0018816959 scopus 로고
    • Structure and evolution of calcium-modulated proteins
    • KRETSINGER, R. H. 1980. Structure and evolution of calcium-modulated proteins. CRC Crit. Rev. Biochem. 8:119-174.
    • (1980) CRC Crit. Rev. Biochem. , vol.8 , pp. 119-174
    • Kretsinger, R.H.1
  • 23
    • 1842302488 scopus 로고
    • Gustav Fischer Verlag, Stuttgart, Germany
    • MEHLHORN, H., ed. 1989. Grundriß der Zoologie. Gustav Fischer Verlag, Stuttgart, Germany.
    • (1989) Grundriß der Zoologie
    • Mehlhorn, H.1
  • 24
    • 0025311949 scopus 로고
    • Evolution of EF-hand calcium-modulated proteins. I. Relationships based on amino acid sequences
    • MONCRIEF, N. D., R. H. KRETSINGER, and M. GOODMAN. 1990. Evolution of EF-hand calcium-modulated proteins. I. Relationships based on amino acid sequences. J. Mol. Evol. 30:522-562.
    • (1990) J. Mol. Evol. , vol.30 , pp. 522-562
    • Moncrief, N.D.1    Kretsinger, R.H.2    Goodman, M.3
  • 25
    • 0004547161 scopus 로고
    • The developmental role of the extracellular matrix suggests a monophyletic origin of the kingdom animalia
    • MORRIS, P. J. 1993. The developmental role of the extracellular matrix suggests a monophyletic origin of the kingdom animalia. Evolution 47:152-165.
    • (1993) Evolution , vol.47 , pp. 152-165
    • Morris, P.J.1
  • 26
    • 85012658242 scopus 로고
    • Cell membranes in sponges
    • MÜLLER, W. E. G. 1982. Cell membranes in sponges. Int. Rev. Cytol. 77:129-181.
    • (1982) Int. Rev. Cytol. , vol.77 , pp. 129-181
    • Müller, W.E.G.1
  • 27
    • 0029092813 scopus 로고
    • Molecular phylogeny of metazoa [animals]: Monophyletic origin
    • _. 1995. Molecular phylogeny of metazoa [animals]: monophyletic origin. Naturwissenschaften 82:321-329.
    • (1995) Naturwissenschaften , vol.82 , pp. 321-329
  • 30
    • 0003764925 scopus 로고
    • IntelliGenetics, Mountain View, Calif.
    • PC/GENE 1995. Data Banks CD-ROM. Release 14.0. IntelliGenetics, Mountain View, Calif.
    • (1995) Data Banks CD-ROM. Release 14.0
  • 31
    • 0027161599 scopus 로고
    • S-type lectins occur also in invertebrates: Unusual subunit composition and high conservation of the carbohydrate recognition domain in the lectin genes from the marine sponge Geodia cydonium
    • PFEIFER, K., M. HAASEMANN, D. UGARKOVIC, H. BRETTING, F. FAHRENHOLZ, and W. E. G. MÜLLER. 1993. S-type lectins occur also in invertebrates: unusual subunit composition and high conservation of the carbohydrate recognition domain in the lectin genes from the marine sponge Geodia cydonium. Glycobiology 3:179-184.
    • (1993) Glycobiology , vol.3 , pp. 179-184
    • Pfeifer, K.1    Haasemann, M.2    Ugarkovic, D.3    Bretting, H.4    Fahrenholz, F.5    Müller, W.E.G.6
  • 33
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • SAITOU, N., and M. NEI. 1987. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4:406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 34
    • 0028134825 scopus 로고
    • The Ig superfamily includes members from the lowest invertebrates to the highest vertebrates
    • SCHÄCKE, H., W. E. G. MÜLLER, V. GAMULIN, and B. RINKEVICH. 1994a The Ig superfamily includes members from the lowest invertebrates to the highest vertebrates. Immunol. Today 15:497-498.
    • (1994) Immunol. Today , vol.15 , pp. 497-498
    • Schäcke, H.1    Müller, W.E.G.2    Gamulin, V.3    Rinkevich, B.4
  • 35
    • 0028675637 scopus 로고
    • Immunoglobulin-like domain is present in the extracellular part of the receptor tyrosine kinase from the marine sponge Geodia cydonium
    • SCHÄCKE, H., B. RINKEVICH, V. GAMULIN, I. M. MÜLLER, and W. E. G. MÜLLER. 1994b. Immunoglobulin-like domain is present in the extracellular part of the receptor tyrosine kinase from the marine sponge Geodia cydonium. J. Mol. Recognit. 7:272-276.
    • (1994) J. Mol. Recognit. , vol.7 , pp. 272-276
    • Schäcke, H.1    Rinkevich, B.2    Gamulin, V.3    Müller, I.M.4    Müller, W.E.G.5
  • 36
    • 0028417436 scopus 로고
    • Molecular cloning of a receptor tyrosine kinase from the marine sponge Geodia cydonium: A new member of the receptor tyrosine kinase class II family in invertebrates
    • SCHÄCKE, H., H. C. SCHRÖDER, V. GAMULIN, B. RINKEVICH, I. M. MÜLLER, and W. E. G. MÜLLER. 1994c. Molecular cloning of a receptor tyrosine kinase from the marine sponge Geodia cydonium: a new member of the receptor tyrosine kinase class II family in invertebrates. Mol. Membr. Biol. 11:101-107.
    • (1994) Mol. Membr. Biol. , vol.11 , pp. 101-107
    • Schäcke, H.1    Schröder, H.C.2    Gamulin, V.3    Rinkevich, B.4    Müller, I.M.5    Müller, W.E.G.6
  • 37
    • 0030919681 scopus 로고    scopus 로고
    • Isolation and characterization of the cDNA clone encoding the serum response factor homolog in the marine sponge Geodia cydonium: High conservation of this transcription factor within Metazoa
    • in press
    • SCHEFFER, U., A. KRASKO, Z. PANCER, AND W. E. G. MÜLLER. 1997. Isolation and characterization of the cDNA clone encoding the serum response factor homolog in the marine sponge Geodia cydonium: high conservation of this transcription factor within Metazoa. Biol. J. Linnean Soc. (in press).
    • (1997) Biol. J. Linnean Soc.
    • Scheffer, U.1    Krasko, A.2    Pancer, Z.3    Müller, W.E.G.4
  • 40
    • 0024382716 scopus 로고
    • 2 subunit (platelet GPIa): Homology to other integrins and the presence of a possible collagen-binding domain
    • 2 subunit (platelet GPIa): homology to other integrins and the presence of a possible collagen-binding domain. J. Cell Biol. 109:397-407.
    • (1989) J. Cell Biol. , vol.109 , pp. 397-407
    • Takada, Y.1    Hemler, M.E.2
  • 41
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • THOMPSON, J. D., D. G. HIGGINS, and T. J. GIBSON. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 42
    • 0027241482 scopus 로고
    • Monophyletic origins of the metazoa: An evolutionary link with fungi
    • WAINRIGHT, P. O., G. HINKLE, M. L. SOGIN, and S. K. STICKEL. 1993. Monophyletic origins of the metazoa: an evolutionary link with fungi. Science 260:340-342.
    • (1993) Science , vol.260 , pp. 340-342
    • Wainright, P.O.1    Hinkle, G.2    Sogin, M.L.3    Stickel, S.K.4
  • 45
    • 0022751114 scopus 로고
    • The AAUAAA sequence is required both for cleavage and for polyadenylation of simian virus 40 pre-mRNA in vitro
    • ZARKOWER, D., P. STEPHENSON, M. SHEETS, and M. WICKENS. 1986. The AAUAAA sequence is required both for cleavage and for polyadenylation of simian virus 40 pre-mRNA in vitro. Mol. Cell. Biol. 6:2317-2323.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 2317-2323
    • Zarkower, D.1    Stephenson, P.2    Sheets, M.3    Wickens, M.4
  • 46
    • 0026645841 scopus 로고
    • The attachment of nematocytes from the primitive invertebrate Hydra to fibronectin is specific and RGD-dependent
    • ZIEGLER, U., and R. P. STIDWILL. 1992. The attachment of nematocytes from the primitive invertebrate Hydra to fibronectin is specific and RGD-dependent. Exp. Cell Res. 202: 281-286.
    • (1992) Exp. Cell Res. , vol.202 , pp. 281-286
    • Ziegler, U.1    Stidwill, R.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.