메뉴 건너뛰기




Volumn 16, Issue 5, 2004, Pages 470-476

A prehistory of cell adhesion

Author keywords

(sponge) aggregation factor; AF; AGP; arabinogalactan protein; CAM; cell adhesion molecule; EGF; epidermal growth factor; Fasciclin like arabinogalactan protein; FLA; glycosylphosphatidylinositol; GPI; phosphatidyl 3 kinase; PI3 kinase; SRCR

Indexed keywords

COLLAGEN; EPIDERMAL GROWTH FACTOR RECEPTOR; FAS ANTIGEN; FASCICLIN I; IMMUNOGLOBULIN G; INTERCELLULAR ADHESION MOLECULE 1; LECTIN; THROMBOSPONDIN;

EID: 4444355854     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2004.07.011     Document Type: Review
Times cited : (32)

References (41)
  • 1
    • 0034799201 scopus 로고    scopus 로고
    • Cloning and expression of the putative aggregation factor from the marine sponge Geodia cydonium
    • J. Schutze, A. Krasko, B. Diehl-Seifert, and W.E. Muller Cloning and expression of the putative aggregation factor from the marine sponge Geodia cydonium J Cell Sci 114 2001 3189 3198
    • (2001) J Cell Sci , vol.114 , pp. 3189-3198
    • Schutze, J.1    Krasko, A.2    Diehl-Seifert, B.3    Muller, W.E.4
  • 2
    • 0035909922 scopus 로고    scopus 로고
    • A receptor tyrosine kinase from choanoflagellates: Molecular insights into early animal evolution
    • N. King, and S.B. Carroll A receptor tyrosine kinase from choanoflagellates: molecular insights into early animal evolution Proc Natl Acad Sci USA 98 2001 15032 15037
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 15032-15037
    • King, N.1    Carroll, S.B.2
  • 3
    • 0042313795 scopus 로고    scopus 로고
    • Conflicting phylogenetic signals at the base of the metazoan tree
    • A. Rokas, N. King, J. Finnerty, and S.B. Carroll Conflicting phylogenetic signals at the base of the metazoan tree Evol Dev 5 2003 346 359
    • (2003) Evol Dev , vol.5 , pp. 346-359
    • Rokas, A.1    King, N.2    Finnerty, J.3    Carroll, S.B.4
  • 4
    • 0037962406 scopus 로고    scopus 로고
    • Evolution of key cell signaling and adhesion protein families predates animal origins
    • N. King, C.T. Hittinger, and S.B. Carroll Evolution of key cell signaling and adhesion protein families predates animal origins Science 301 2003 361 363 A survey of >5000 ESTs (expressed sequence tags) from two species demonstrates the presence of metazoan-like adhesion and signal molecules in choanoflagellate protozoa.
    • (2003) Science , vol.301 , pp. 361-363
    • King, N.1    Hittinger, C.T.2    Carroll, S.B.3
  • 5
    • 0020690859 scopus 로고
    • Fine structures of sponge cell membranes: Comparative study with freeze-fracture and conventional thin section methods
    • C. Lethias, R. Garrone, and M. Mazzorana Fine structures of sponge cell membranes: comparative study with freeze-fracture and conventional thin section methods Tissue Cell 15 1983 523 535
    • (1983) Tissue Cell , vol.15 , pp. 523-535
    • Lethias, C.1    Garrone, R.2    Mazzorana, M.3
  • 6
    • 0031662558 scopus 로고    scopus 로고
    • The putative sponge aggregation receptor. Isolation and characterization of a molecule composed of scavenger receptor cysteine-rich domains and short consensus repeats
    • B. Blumbach, Z. Pancer, B. Diehl-Seifert, R. Steffen, J. Munkner, I. Muller, and W.E. Muller The putative sponge aggregation receptor. Isolation and characterization of a molecule composed of scavenger receptor cysteine-rich domains and short consensus repeats J Cell Sci 111 1998 2635 2644
    • (1998) J Cell Sci , vol.111 , pp. 2635-2644
    • Blumbach, B.1    Pancer, Z.2    Diehl-Seifert, B.3    Steffen, R.4    Munkner, J.5    Muller, I.6    Muller, W.E.7
  • 8
    • 0042357386 scopus 로고    scopus 로고
    • Emergence and disappearance of an immune molecule, an antimicrobial lectin, in basal metazoa. A tachylectin-related protein in the sponge Suberites domuncula
    • H.C. Schroder, H. Ushijima, A. Krasko, V. Gamulin, N.L. Thakur, B. Diehl-Seifert, I.M. Muller, and W.E. Muller Emergence and disappearance of an immune molecule, an antimicrobial lectin, in basal metazoa. A tachylectin-related protein in the sponge Suberites domuncula J Biol Chem 278 2003 32810 32817
    • (2003) J Biol Chem , vol.278 , pp. 32810-32817
    • Schroder, H.C.1    Ushijima, H.2    Krasko, A.3    Gamulin, V.4    Thakur, N.L.5    Diehl-Seifert, B.6    Muller, I.M.7    Muller, W.E.8
  • 9
    • 0035090591 scopus 로고    scopus 로고
    • Isolation and cloning of a C-type lectin from the hexactinellid sponge Aphrocallistes vastus: A putative aggregation factor
    • D. Gundacker, S.P. Leys, H.C. Schroder, I.M. Muller, and W.E. Muller Isolation and cloning of a C-type lectin from the hexactinellid sponge Aphrocallistes vastus: a putative aggregation factor Glycobiology 11 2001 21 29
    • (2001) Glycobiology , vol.11 , pp. 21-29
    • Gundacker, D.1    Leys, S.P.2    Schroder, H.C.3    Muller, I.M.4    Muller, W.E.5
  • 10
    • 3042774003 scopus 로고    scopus 로고
    • Matrix-mediated canal formation in primmorphs from the sponge Suberites domuncula involves the expression of a CD36 receptor-ligand system
    • W.E. Muller, N.L. Thakur, H. Ushijima, A.N. Thakur, A. Krasko, G. Le Pennec, M.M. Indap, S. Perovic-Ottstadt, H.C. Schroder, and G. Lang Matrix-mediated canal formation in primmorphs from the sponge Suberites domuncula involves the expression of a CD36 receptor-ligand system J Cell Sci 117 2004 2579 2590 When transferred to a galectin matrix, cells from Suberites domuncula form 3D-cell aggregates that possess canal-like structures. This involves a CD36/LIMPII receptor homologue and an ADAMTS homologue that contains a CSVTCG domain, also found in thrombospondin-1. This aggregation is suppressed by a bacterial secondary metabolite with anti-angiogenic properties.
    • (2004) J Cell Sci , vol.117 , pp. 2579-2590
    • Muller, W.E.1    Thakur, N.L.2    Ushijima, H.3    Thakur, A.N.4    Krasko, A.5    Le Pennec, G.6    Indap, M.M.7    Perovic-Ottstadt, S.8    Schroder, H.C.9    Lang, G.10
  • 11
    • 0036670881 scopus 로고    scopus 로고
    • Adhesion in Candida spp
    • P. Sundstrom Adhesion in Candida spp Cell Microbiol 4 2002 461 469
    • (2002) Cell Microbiol , vol.4 , pp. 461-469
    • Sundstrom, P.1
  • 12
    • 0345236609 scopus 로고    scopus 로고
    • Mid2p stabilizes septin rings during cytokinesis in fission yeast
    • A. Berlin, A. Paoletti, and F. Chang Mid2p stabilizes septin rings during cytokinesis in fission yeast J Cell Biol 160 2003 1083 1092
    • (2003) J Cell Biol , vol.160 , pp. 1083-1092
    • Berlin, A.1    Paoletti, A.2    Chang, F.3
  • 13
    • 0032570872 scopus 로고    scopus 로고
    • Linkage of adhesion, filamentous growth, and virulence in Candida albicans to a single gene, INT1
    • C.A. Gale, C.M. Bendel, M. McClellan, M. Hauser, J.M. Becker, J. Berman, and M.K. Hostetter Linkage of adhesion, filamentous growth, and virulence in Candida albicans to a single gene, INT1 Science 279 1998 1355 1358
    • (1998) Science , vol.279 , pp. 1355-1358
    • Gale, C.A.1    Bendel, C.M.2    McClellan, M.3    Hauser, M.4    Becker, J.M.5    Berman, J.6    Hostetter, M.K.7
  • 14
    • 0036126711 scopus 로고    scopus 로고
    • Cadherin-like domains in α-dystroglycan, α/ε-sarcoglycan and yeast and bacterial proteins
    • N.J. Dickens, S. Beatson, and C.P. Ponting Cadherin-like domains in α-dystroglycan, α/ε-sarcoglycan and yeast and bacterial proteins Curr Biol 12 2002 R197 R199 A bioinformatic analysis suggesting that cadherin-like structural domains may be present in a wider range of proteins and organisms was than previously suspected.
    • (2002) Curr Biol , vol.12
    • Dickens, N.J.1    Beatson, S.2    Ponting, C.P.3
  • 15
    • 0029995116 scopus 로고    scopus 로고
    • Selection of axial growth sites in yeast requires Axl2p, a novel plasma membrane glycoprotein
    • T. Roemer, K. Madden, J. Chang, and M. Snyder Selection of axial growth sites in yeast requires Axl2p, a novel plasma membrane glycoprotein Genes Dev 10 1996 777 793
    • (1996) Genes Dev , vol.10 , pp. 777-793
    • Roemer, T.1    Madden, K.2    Chang, J.3    Snyder, M.4
  • 16
    • 0036734451 scopus 로고    scopus 로고
    • The roles of bud-site-selection proteins during haploid invasive growth in yeast
    • P.J. Cullen, and G.F. Sprague Jr. The roles of bud-site-selection proteins during haploid invasive growth in yeast Mol Biol Cell 13 2002 2990 3004
    • (2002) Mol Biol Cell , vol.13 , pp. 2990-3004
    • Cullen, P.J.1    Sprague Jr., G.F.2
  • 17
    • 0035860689 scopus 로고    scopus 로고
    • Fusion of docked membranes requires the armadillo repeat protein Vac8p
    • Y.X. Wang, E.J. Kauffman, J.E. Duex, and L.S. Weisman Fusion of docked membranes requires the armadillo repeat protein Vac8p J Biol Chem 276 2001 35133 35140
    • (2001) J Biol Chem , vol.276 , pp. 35133-35140
    • Wang, Y.X.1    Kauffman, E.J.2    Duex, J.E.3    Weisman, L.S.4
  • 18
    • 0037422115 scopus 로고    scopus 로고
    • Regulated degradation of a class V myosin receptor directs movement of the yeast vacuole
    • F. Tang, E.J. Kauffman, J.L. Novak, J.J. Nau, N.L. Catlett, and L.S. Weisman Regulated degradation of a class V myosin receptor directs movement of the yeast vacuole Nature 422 2003 87 92 In yeast, Vac17p is a vacuole-specific receptor for a class V myosin Myo2p that simultaneously binds to Vac8p, an Arm repeat protein. This complex moves the vacuole into the bud, and is regulated by degradation of Vac17p.
    • (2003) Nature , vol.422 , pp. 87-92
    • Tang, F.1    Kauffman, E.J.2    Novak, J.L.3    Nau, J.J.4    Catlett, N.L.5    Weisman, L.S.6
  • 19
    • 0035697060 scopus 로고    scopus 로고
    • Cell-cell adhesion and signal transduction during Dictyostelium development
    • J.C. Coates, and A.J. Harwood Cell-cell adhesion and signal transduction during Dictyostelium development J Cell Sci 114 2001 4349 4358
    • (2001) J Cell Sci , vol.114 , pp. 4349-4358
    • Coates, J.C.1    Harwood, A.J.2
  • 20
    • 0030872950 scopus 로고    scopus 로고
    • The cell adhesion molecule DdCAD-1 in Dictyostelium is targeted to the cell surface by a nonclassical transport pathway involving contractile vacuoles
    • H. Sesaki, E.F. Wong, and C.H. Siu The cell adhesion molecule DdCAD-1 in Dictyostelium is targeted to the cell surface by a nonclassical transport pathway involving contractile vacuoles J Cell Biol 138 1997 939 951
    • (1997) J Cell Biol , vol.138 , pp. 939-951
    • Sesaki, H.1    Wong, E.F.2    Siu, C.H.3
  • 21
    • 0036670034 scopus 로고    scopus 로고
    • Disruption of the gene encoding the cell adhesion molecule DdCAD-1 leads to aberrant cell sorting and cell-type proportioning during Dictyostelium development
    • E. Wong, C. Yang, J. Wang, D. Fuller, W.F. Loomis, and C.H. Siu Disruption of the gene encoding the cell adhesion molecule DdCAD-1 leads to aberrant cell sorting and cell-type proportioning during Dictyostelium development Development 129 2002 3839 3850
    • (2002) Development , vol.129 , pp. 3839-3850
    • Wong, E.1    Yang, C.2    Wang, J.3    Fuller, D.4    Loomis, W.F.5    Siu, C.H.6
  • 22
    • 0037462749 scopus 로고    scopus 로고
    • Cytoskeleton interactions involved in the assembly and function of glycoprotein-80 adhesion complexes in Dictyostelium
    • T.J. Harris, A. Ravandi, D.E. Awrey, and C.H. Siu Cytoskeleton interactions involved in the assembly and function of glycoprotein-80 adhesion complexes in Dictyostelium J Biol Chem 278 2003 2614 2623
    • (2003) J Biol Chem , vol.278 , pp. 2614-2623
    • Harris, T.J.1    Ravandi, A.2    Awrey, D.E.3    Siu, C.H.4
  • 23
    • 0344925819 scopus 로고    scopus 로고
    • A cell-adhesion pathway regulates intercellular communication during Dictyostelium development
    • K. Kibler, J. Svetz, T.L. Nguyen, C. Shaw, and G. Shaulsky A cell-adhesion pathway regulates intercellular communication during Dictyostelium development Dev Biol 264 2003 506 521 Dictyostelium chimeras are used to examine the interaction between different mutants. This approach indicates that the adhesion proteins lagC, lagD and the EGF repeat protein comC group into a functional pathway required for spore cell formation.
    • (2003) Dev Biol , vol.264 , pp. 506-521
    • Kibler, K.1    Svetz, J.2    Nguyen, T.L.3    Shaw, C.4    Shaulsky, G.5
  • 24
    • 0037164750 scopus 로고    scopus 로고
    • SadA, a novel adhesion receptor in Dictyostelium
    • P. Fey, S. Stephens, M.A. Titus, and R.L. Chisholm SadA, a novel adhesion receptor in Dictyostelium J Cell Biol 159 2002 1109 1119
    • (2002) J Cell Biol , vol.159 , pp. 1109-1119
    • Fey, P.1    Stephens, S.2    Titus, M.A.3    Chisholm, R.L.4
  • 25
    • 0346335806 scopus 로고    scopus 로고
    • Dynamic actin patterns and Arp2/3 assembly at the substrate-attached surface of motile cells
    • T. Bretschneider, S. Diez, K. Anderson, J. Heuser, M. Clarke, A. Muller-Taubenberger, J. Kohler, and G. Gerisch Dynamic actin patterns and Arp2/3 assembly at the substrate-attached surface of motile cells Curr Biol 14 2004 1 10 A combination of TIRF microscopy and labelling of actin filaments shows a rapid restructuring of single and bundled actin filaments during cell movement. Recruitment of the Arp2/3 complex to these structures characterises stationary foci and travelling actin waves.
    • (2004) Curr Biol , vol.14 , pp. 1-10
    • Bretschneider, T.1    Diez, S.2    Anderson, K.3    Heuser, J.4    Clarke, M.5    Muller-Taubenberger, A.6    Kohler, J.7    Gerisch, G.8
  • 26
    • 2342442599 scopus 로고    scopus 로고
    • Dynamics of novel feet of Dictyostelium cells during migration
    • K.S. Uchida, and S. Yumura Dynamics of novel feet of Dictyostelium cells during migration J Cell Sci 117 2004 1443 1455 Actin foci form at contact sites between the cell and substratum, and cell velocity is inversely proportional to the number of actin foci. Measurement of traction force using a silicone substratum demonstrates that the traction force is transmitted to the substratum through the actin foci.
    • (2004) J Cell Sci , vol.117 , pp. 1443-1455
    • Uchida, K.S.1    Yumura, S.2
  • 27
    • 3042541534 scopus 로고    scopus 로고
    • Talin B is required for force transmission in morphogenesis of Dictyostelium
    • in press.
    • Tsujioka M, Yoshida K, Inouye K: Talin B is required for force transmission in morphogenesis of Dictyostelium. Embo J 2004, in press. talB, a Dictyostelium talin gene, is present at adhesion sites on the plasma membrane, and is required for force transmission between the cytoskeleton and the cell exterior during multicellular development.
    • (2004) Embo J
    • Tsujioka, M.1    Yoshida, K.2    Inouye, K.3
  • 28
    • 0037162284 scopus 로고    scopus 로고
    • Visualizing PI3 kinase-mediated cell-cell signaling during Dictyostelium development
    • D. Dormann, G. Weijer, C.A. Parent, P.N. Devreotes, and C.J. Weijer Visualizing PI3 kinase-mediated cell-cell signaling during Dictyostelium development Curr Biol 12 2002 1178 1188
    • (2002) Curr Biol , vol.12 , pp. 1178-1188
    • Dormann, D.1    Weijer, G.2    Parent, C.A.3    Devreotes, P.N.4    Weijer, C.J.5
  • 29
    • 0034619825 scopus 로고    scopus 로고
    • Adherens junctions and β-catenin-mediated cell signalling in a non-metazoan organism
    • M.J. Grimson, J.C. Coates, J.P. Reynolds, M. Shipman, R.L. Blanton, and A.J. Harwood Adherens junctions and β-catenin-mediated cell signalling in a non-metazoan organism Nature 408 2000 727 731
    • (2000) Nature , vol.408 , pp. 727-731
    • Grimson, M.J.1    Coates, J.C.2    Reynolds, J.P.3    Shipman, M.4    Blanton, R.L.5    Harwood, A.J.6
  • 30
    • 0038381715 scopus 로고    scopus 로고
    • High-throughput viral expression of cDNA-green fluorescent protein fusions reveals novel subcellular addresses and identifies unique proteins that interact with plasmodesmata
    • N.M. Escobar, S. Haupt, G. Thow, P. Boevink, S. Chapman, and K. Oparka High-throughput viral expression of cDNA-green fluorescent protein fusions reveals novel subcellular addresses and identifies unique proteins that interact with plasmodesmata Plant Cell 15 2003 1507 1523 A high-throughput screen of random cDNA-GFP fusions finds only 12 proteins that specifically localise to plasmodesmata. Except for Rab11b, none has similarity to animal cytoskeletal or signaling proteins.
    • (2003) Plant Cell , vol.15 , pp. 1507-1523
    • Escobar, N.M.1    Haupt, S.2    Thow, G.3    Boevink, P.4    Chapman, S.5    Oparka, K.6
  • 31
    • 1142286348 scopus 로고    scopus 로고
    • Nanotubular highways for intercellular organelle transport
    • A. Rustom, R. Saffrich, I. Markovi, P. Walther, and H.H. Gerdes Nanotubular highways for intercellular organelle transport Science 303 2004 1007 1010
    • (2004) Science , vol.303 , pp. 1007-1010
    • Rustom, A.1    Saffrich, R.2    Markovi, I.3    Walther, P.4    Gerdes, H.H.5
  • 32
    • 0019847971 scopus 로고
    • Cleavage patterns, cell lineages, and development of a cytoplasmic bridge system in Volvox embryos
    • K.J. Green, and D.L. Kirk Cleavage patterns, cell lineages, and development of a cytoplasmic bridge system in Volvox embryos J Cell Biol 91 1981 743 755
    • (1981) J Cell Biol , vol.91 , pp. 743-755
    • Green, K.J.1    Kirk, D.L.2
  • 33
    • 0038005358 scopus 로고    scopus 로고
    • A kinesin, invA, plays an essential role in Volvox morphogenesis
    • I. Nishii, S. Ogihara, and D.L. Kirk A kinesin, invA, plays an essential role in Volvox morphogenesis Cell 113 2003 743 753 InvA encodes a kinesin protein that localises to cytoplasmic bridges and is probably associated with microtubules. InvA mediates a dramatic cell shape change in all the somatic cells to turn the embryo inside-out to form the adult.
    • (2003) Cell , vol.113 , pp. 743-753
    • Nishii, I.1    Ogihara, S.2    Kirk, D.L.3
  • 34
    • 0142070917 scopus 로고    scopus 로고
    • AtAGP30, an arabinogalactan-protein in the cell walls of the primary root, plays a role in root regeneration and seed germination
    • A.J. van Hengel, and K. Roberts AtAGP30, an arabinogalactan-protein in the cell walls of the primary root, plays a role in root regeneration and seed germination Plant J 36 2003 256 270
    • (2003) Plant J , vol.36 , pp. 256-270
    • Van Hengel, A.J.1    Roberts, K.2
  • 35
    • 0027980523 scopus 로고
    • Algal-CAMs: Isoforms of a cell adhesion molecule in embryos of the alga Volvox with homology to Drosophila fasciclin I
    • O. Huber, and M. Sumper Algal-CAMs: isoforms of a cell adhesion molecule in embryos of the alga Volvox with homology to Drosophila fasciclin I EMBO J 13 1994 4212 4222
    • (1994) EMBO J , vol.13 , pp. 4212-4222
    • Huber, O.1    Sumper, M.2
  • 36
    • 0346433840 scopus 로고    scopus 로고
    • The fasciclin-like arabinogalactan proteins of Arabidopsis. A multigene family of putative cell adhesion molecules
    • K.L. Johnson, B.J. Jones, A. Bacic, and C.J. Schultz The fasciclin-like arabinogalactan proteins of Arabidopsis. A multigene family of putative cell adhesion molecules Plant Physiol 133 2003 1911 1925
    • (2003) Plant Physiol , vol.133 , pp. 1911-1925
    • Johnson, K.L.1    Jones, B.J.2    Bacic, A.3    Schultz, C.J.4
  • 37
    • 0037256529 scopus 로고    scopus 로고
    • The Arabidopsis SOS5 locus encodes a putative cell surface adhesion protein and is required for normal cell expansion
    • H. Shi, Y. Kim, Y. Guo, B. Stevenson, and J.K. Zhu The Arabidopsis SOS5 locus encodes a putative cell surface adhesion protein and is required for normal cell expansion Plant Cell 15 2003 19 32 The Arabidopsis sos5 mutant has roots that are hypersensitive to salt stress. Sos5 encodes an FLA protein. Electron microscopy of sos5 root cells shows disordered cell walls and disrupted plasma-membrane-cell-wall attachments.
    • (2003) Plant Cell , vol.15 , pp. 19-32
    • Shi, H.1    Kim, Y.2    Guo, Y.3    Stevenson, B.4    Zhu, J.K.5
  • 38
    • 0033615981 scopus 로고    scopus 로고
    • Conservation of a gliding motility and cell invasion machinery in Apicomplexan parasites
    • S. Kappe, T. Bruderer, S. Gantt, H. Fujioka, V. Nussenzweig, and R. Menard Conservation of a gliding motility and cell invasion machinery in Apicomplexan parasites J Cell Biol 147 1999 937 944
    • (1999) J Cell Biol , vol.147 , pp. 937-944
    • Kappe, S.1    Bruderer, T.2    Gantt, S.3    Fujioka, H.4    Nussenzweig, V.5    Menard, R.6
  • 39
    • 0037007205 scopus 로고    scopus 로고
    • Plasmodium sporozoite invasion into insect and mammalian cells is directed by the same dual binding system
    • K. Matuschewski, A.C. Nunes, V. Nussenzweig, and R. Menard Plasmodium sporozoite invasion into insect and mammalian cells is directed by the same dual binding system EMBO J 21 2002 1597 1606
    • (2002) EMBO J , vol.21 , pp. 1597-1606
    • Matuschewski, K.1    Nunes, A.C.2    Nussenzweig, V.3    Menard, R.4
  • 40
    • 0037841805 scopus 로고    scopus 로고
    • The deep roots of eukaryotes
    • S.L. Baldauf The deep roots of eukaryotes Science 300 2003 1703 1706 The author discusses recent developments that radically revise our view of the phylogenetic relationships between eukaryotic groups.
    • (2003) Science , vol.300 , pp. 1703-1706
    • Baldauf, S.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.