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Volumn 18, Issue 23, 1999, Pages 6762-6770

Interaction of agrin with laminin requires a coiled-coil conformation of the agrin-binding site within the laminin γ1 chain

Author keywords

Agrin; Coiled coil domain; Extracellular matrix; Laminin isoforms; Protein protein interactions

Indexed keywords

AGRIN; LAMININ;

EID: 0033485262     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (71)

References (41)
  • 1
    • 0025823541 scopus 로고
    • Cross-linking of laminin-nidogen complexes by tissue transglutaminase. A novel mechanism for basement membrane stabilization
    • Aeschlimann, D. and Paulsson, M. (1991) Cross-linking of laminin-nidogen complexes by tissue transglutaminase. A novel mechanism for basement membrane stabilization. J. Biol. Chem., 266, 15308-15317.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15308-15317
    • Aeschlimann, D.1    Paulsson, M.2
  • 2
    • 0026845838 scopus 로고
    • Structure of the leucine zipper
    • Alber, T. (1992) Structure of the leucine zipper. Curr. Opin. Genet. Dev., 2, 205-210.
    • (1992) Curr. Opin. Genet. Dev. , vol.2 , pp. 205-210
    • Alber, T.1
  • 3
    • 0003338119 scopus 로고
    • Extracellular protein modules: A proposed nomenclature
    • Bork, P. and Bairoch, A. (1995) Extracellular protein modules: a proposed nomenclature. Trends Biochem. Sci. (Suppl.), 20, 104-105.
    • (1995) Trends Biochem. Sci. (Suppl.) , vol.20 , pp. 104-105
    • Bork, P.1    Bairoch, A.2
  • 4
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark, E.A. and Brugge, J.S. (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
    • 0025272940 scopus 로고
    • α-Helical coiled coils and bundles: How to design an α-helical protein
    • Cohen, C. and Parry, D.A.D. (1990) α-Helical coiled coils and bundles: how to design an α-helical protein. Proteins, 7, 1-15.
    • (1990) Proteins , vol.7 , pp. 1-15
    • Cohen, C.1    Parry, D.A.D.2
  • 6
    • 0000920828 scopus 로고
    • The packing of α-helices: Simple coiled-coils
    • Crick, F.H.C. (1953) The packing of α-helices: simple coiled-coils. Acta Crystallogr., 6, 689-697.
    • (1953) Acta Crystallogr. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 7
    • 0029591857 scopus 로고
    • An amino-terminal extension is required for the secretion of chick agrin and its binding to extracellular matrix
    • Denzer, A.J., Gesemann, M., Schumacher, B. and Ruegg, M.A. (1995) An amino-terminal extension is required for the secretion of chick agrin and its binding to extracellular matrix. J. Cell Biol., 131, 1547-1560.
    • (1995) J. Cell Biol. , vol.131 , pp. 1547-1560
    • Denzer, A.J.1    Gesemann, M.2    Schumacher, B.3    Ruegg, M.A.4
  • 8
    • 0030561523 scopus 로고    scopus 로고
    • Diverse functions of the extracellular matrix molecule agrin
    • Denzer, A.J., Gesemann, M. and Ruegg, M.A. (1996) Diverse functions of the extracellular matrix molecule agrin. Semin. Neurosci., 8, 357-366.
    • (1996) Semin. Neurosci. , vol.8 , pp. 357-366
    • Denzer, A.J.1    Gesemann, M.2    Ruegg, M.A.3
  • 11
    • 0025315789 scopus 로고
    • Cell adhesion, spreading and neurite stimulation by laminin fragment E8 depends on maintenance of secondary and tertiary structure in its rod and globular domain
    • Deutzmann, R., Aumailley, M., Wiedemann, H., Pysny, W., Timpl, R. and Edgar, D. (1990) Cell adhesion, spreading and neurite stimulation by laminin fragment E8 depends on maintenance of secondary and tertiary structure in its rod and globular domain. Eur. J. Biochem., 191, 513-522.
    • (1990) Eur. J. Biochem. , vol.191 , pp. 513-522
    • Deutzmann, R.1    Aumailley, M.2    Wiedemann, H.3    Pysny, W.4    Timpl, R.5    Edgar, D.6
  • 12
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch, H. (1967) Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry, 6, 1948-1954.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 13
    • 0027934571 scopus 로고
    • Crystal structure of an isoleucine-zipper trimer
    • Harbury, P.B., Kim, P.S. and Alber, T. (1994) Crystal structure of an isoleucine-zipper trimer. Nature, 371, 80-83.
    • (1994) Nature , vol.371 , pp. 80-83
    • Harbury, P.B.1    Kim, P.S.2    Alber, T.3
  • 14
    • 0030272647 scopus 로고    scopus 로고
    • Dystroglycan: An extracellular matrix receptor linked to the cytoskeleton
    • Henry, M.D. and Campbell, K.P (1996) Dystroglycan: an extracellular matrix receptor linked to the cytoskeleton. Curr. Opin. Cell Biol., 8, 625-631.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 625-631
    • Henry, M.D.1    Campbell, K.P.2
  • 15
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: Gene splicing by overlap extension
    • Horton, R.M., Hunt, H.D., Ho, S.N., Pullen, J.K. and Pease, L.R. (1989) Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene, 77, 61-68.
    • (1989) Gene , vol.77 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 16
    • 0026754516 scopus 로고
    • A truncated laminin chain homologous to the B2 chain: Structure, spatial expression, and chromosomal assignment
    • Kallunki, P. et al. (1992) A truncated laminin chain homologous to the B2 chain: structure, spatial expression, and chromosomal assignment. J. Cell Biol., 119, 679-693.
    • (1992) J. Cell Biol. , vol.119 , pp. 679-693
    • Kallunki, P.1
  • 17
    • 0030935246 scopus 로고    scopus 로고
    • α-Helical coiled-coil oligomerization domains in extracellular proteins
    • Kammerer, R.A. (1997) α-Helical coiled-coil oligomerization domains in extracellular proteins. Matrix Biol., 15, 555-565.
    • (1997) Matrix Biol. , vol.15 , pp. 555-565
    • Kammerer, R.A.1
  • 18
    • 0032562663 scopus 로고    scopus 로고
    • Tenascin-C hexabrachion assembly is a sequential two-step process initiated by coiled-coil α-helices
    • Kammerer, R.A., Schulthess, T., Landwehr, R., Lustig, A., Fischer, D. and Engel, J. (1998a) Tenascin-C hexabrachion assembly is a sequential two-step process initiated by coiled-coil α-helices. J. Biol. Chem., 273, 10602-10608.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10602-10608
    • Kammerer, R.A.1    Schulthess, T.2    Landwehr, R.3    Lustig, A.4    Fischer, D.5    Engel, J.6
  • 20
    • 0033519298 scopus 로고    scopus 로고
    • Characterization and expression of the laminin γ3 chain: A novel, non-basement membrane-associated, laminin chain
    • Koch, M., Olson, P.F., Albus, A., Jin, W., Hunter, D.D., Brunken, W.J., Burgeson, R.E. and Champliaud, M.F. (1999) Characterization and expression of the laminin γ3 chain: a novel, non-basement membrane-associated, laminin chain. J. Cell Biol., 145, 605-618.
    • (1999) J. Cell Biol. , vol.145 , pp. 605-618
    • Koch, M.1    Olson, P.F.2    Albus, A.3    Jin, W.4    Hunter, D.D.5    Brunken, W.J.6    Burgeson, R.E.7    Champliaud, M.F.8
  • 21
    • 0024295767 scopus 로고
    • The leucine zipper: A hypothetical structure common to a new class of DNA binding proteins
    • Landschulz, W.H., Johnson, P.F. and McKnight, S.L. (1988) The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins. Science, 240, 1759-1764.
    • (1988) Science , vol.240 , pp. 1759-1764
    • Landschulz, W.H.1    Johnson, P.F.2    McKnight, S.L.3
  • 22
    • 0030271515 scopus 로고    scopus 로고
    • Coiled coils: New structures and new functions
    • Lupas, A. (1996) Coiled coils: new structures and new functions. Trends Biochem. Sci., 21, 375-382.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 375-382
    • Lupas, A.1
  • 23
    • 0002748308 scopus 로고    scopus 로고
    • Structure of laminins and their chain assembly
    • Ekblom, P. and Timpl, R. (eds), Harwood Academic Publishers, The Netherlands
    • Maurer, P. and Engel, J. (1996) Structure of laminins and their chain assembly. In Ekblom, P. and Timpl, R. (eds), The Laminins. Harwood Academic Publishers, The Netherlands, pp. 27-49.
    • (1996) The Laminins , pp. 27-49
    • Maurer, P.1    Engel, J.2
  • 24
    • 0016774265 scopus 로고
    • Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure
    • McLachlan, A.D. and Stewart, M. (1975) Tropomyosin coiled-coil interactions: evidence for an unstaggered structure. J. Mol. Biol., 98, 293-304.
    • (1975) J. Mol. Biol. , vol.98 , pp. 293-304
    • McLachlan, A.D.1    Stewart, M.2
  • 26
    • 0030919488 scopus 로고    scopus 로고
    • The laminin α chains: Expression, developmental transitions, and chromosomal locations of α1-5, identification of heterotrimeric laminins 8-11, and cloning of a novel α3 isoform
    • Miner, J.H., Patton, B.L., Lentz, S.I, Gilbert, D.J., Snider, W.D., Jenkins, N.A., Copeland, N.G. and Sanes, J.R. (1997) The laminin α chains: expression, developmental transitions, and chromosomal locations of α1-5, identification of heterotrimeric laminins 8-11, and cloning of a novel α3 isoform. J. Cell Biol., 137, 685-701.
    • (1997) J. Cell Biol. , vol.137 , pp. 685-701
    • Miner, J.H.1    Patton, B.L.2    Lentz, S.I.3    Gilbert, D.J.4    Snider, W.D.5    Jenkins, N.A.6    Copeland, N.G.7    Sanes, J.R.8
  • 27
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
    • O'Shea, E.K., Klemm, J.D., Kim, P.S. and Alber, T. (1991) X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science, 254, 539-544.
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 28
    • 0028920977 scopus 로고
    • A motoneuron-selective stop signal in the synaptic protein S-laminin
    • Porter, B.E., Weis, J. and Sanes, J.R. (1995) A motoneuron-selective stop signal in the synaptic protein S-laminin. Neuron, 14, 549-559.
    • (1995) Neuron , vol.14 , pp. 549-559
    • Porter, B.E.1    Weis, J.2    Sanes, J.R.3
  • 29
    • 0025879967 scopus 로고
    • Kalinin: An epithelium-specific basement membrane adhesion molecule that is a component of anchoring filaments
    • Rousselle, P., Lunstrum, G.P., Keene, D.R. and Burgeson, R.E. (1991) Kalinin: an epithelium-specific basement membrane adhesion molecule that is a component of anchoring filaments. J. Cell Biol., 114, 567-576.
    • (1991) J. Cell Biol. , vol.114 , pp. 567-576
    • Rousselle, P.1    Lunstrum, G.P.2    Keene, D.R.3    Burgeson, R.E.4
  • 30
    • 0023657117 scopus 로고
    • The laminin B2 chain has a multidomain structure homologous to the B1 chain
    • Sasaki, M. and Yamada, Y. (1987) The laminin B2 chain has a multidomain structure homologous to the B1 chain. J. Biol. Chem., 262, 17111-17117.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17111-17117
    • Sasaki, M.1    Yamada, Y.2
  • 31
    • 0042383817 scopus 로고
    • Sequence of the cDNA encoding the laminin B1 chain reveals a multidomain protein containing cysteine-rich repeats
    • Sasaki, M., Kato, S., Kohno, K., Martin, G.R. and Yamada, Y. (1987) Sequence of the cDNA encoding the laminin B1 chain reveals a multidomain protein containing cysteine-rich repeats. Proc. Natl Acad. Sci. USA, 84, 935-939.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 935-939
    • Sasaki, M.1    Kato, S.2    Kohno, K.3    Martin, G.R.4    Yamada, Y.5
  • 32
    • 0023701420 scopus 로고
    • Laminin, a multidomain protein. The A chain has a unique globular domain and homology with the basement membrane proteoglycan and the B chains
    • Sasaki, M., Kleinman, H.K., Huber, H., Deutzmann, R. and Yamada, Y. (1988) Laminin, a multidomain protein. The A chain has a unique globular domain and homology with the basement membrane proteoglycan and the B chains. J. Biol. Chem., 263, 16536-16544.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16536-16544
    • Sasaki, M.1    Kleinman, H.K.2    Huber, H.3    Deutzmann, R.4    Yamada, Y.5
  • 33
    • 0015463470 scopus 로고
    • Amino-acid sequence of rabbit skeletal tropomyosin and its coiled-coil structure
    • Sodek, J., Hodges, R.S., Smillie, L.B. and Jurasek, L. (1972) Amino-acid sequence of rabbit skeletal tropomyosin and its coiled-coil structure. Proc. Natl Acad. Sci. USA, 69, 3800-3804.
    • (1972) Proc. Natl Acad. Sci. USA , vol.69 , pp. 3800-3804
    • Sodek, J.1    Hodges, R.S.2    Smillie, L.B.3    Jurasek, L.4
  • 34
    • 0031570687 scopus 로고    scopus 로고
    • Structure of bacteriophage T4 fibritin: A segmented coiled coil and the role of the C-terminal domain
    • Tao, Y., Strelkov, S.V., Mesyanzhinov, V.V. and Rossmann, M.G. (1997) Structure of bacteriophage T4 fibritin: a segmented coiled coil and the role of the C-terminal domain. Structure, 5, 789-798.
    • (1997) Structure , vol.5 , pp. 789-798
    • Tao, Y.1    Strelkov, S.V.2    Mesyanzhinov, V.V.3    Rossmann, M.G.4
  • 37
  • 38
    • 0025734184 scopus 로고
    • Adhesive recognition sequences
    • Yamada, K.M. (1991) Adhesive recognition sequences. J. Biol. Chem., 266, 12809-12812.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12809-12812
    • Yamada, K.M.1
  • 39
    • 0027313437 scopus 로고
    • Self-assembly and calcium-binding sites in laminin: A three-arm interaction model
    • Yurchenco, P.D. and Cheng, Y.S. (1993) Self-assembly and calcium-binding sites in laminin: a three-arm interaction model. J. Biol. Chem., 268, 17286-17299.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17286-17299
    • Yurchenco, P.D.1    Cheng, Y.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.