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Volumn 117, Issue 2, 2004, Pages 233-242

A domain-specific usherin/collagen IV interaction may be required for stable integration into the basement membrane superstructure

Author keywords

Basement membrane; Collagen (IV); Protein interaction; Usher syndrome; Usherin

Indexed keywords

COLLAGEN TYPE 4; MEMBRANE PROTEIN; PEPTIDE; RECOMBINANT PROTEIN;

EID: 1642462397     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.00850     Document Type: Article
Times cited : (45)

References (46)
  • 1
    • 0025900908 scopus 로고
    • Localization of the major heparin binding site in fibronectin
    • Barkalow, F. J. and Schwarzbauer, J. E. (1991). Localization of the major heparin binding site in fibronectin. J. Biol. Chem. 266, 7812-7818.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7812-7818
    • Barkalow, F.J.1    Schwarzbauer, J.E.2
  • 2
    • 0029984547 scopus 로고    scopus 로고
    • Structure of the nidogen binding LE module of the laminin gamma1 chain in solution
    • Baumgartner, R., Czisch, M., Mayer, U., Poschl, E., Huber, R. and Holak, T. A. (1996). Structure of the nidogen binding LE module of the laminin gamma1 chain in solution. J. Mol. Biol. 257, 658-667.
    • (1996) J. Mol. Biol. , vol.257 , pp. 658-667
    • Baumgartner, R.1    Czisch, M.2    Mayer, U.3    Poschl, E.4    Huber, R.5    Holak, T.A.6
  • 3
    • 0025165018 scopus 로고
    • Structure and function of laminin: Anatomy of a multidomain glycoprotein
    • Beck, K., Hunter, I. and Engel, J. (1990). Structure and function of laminin: anatomy of a multidomain glycoprotein. FASEB J. 4, 148-160.
    • (1990) FASEB J. , vol.4 , pp. 148-160
    • Beck, K.1    Hunter, I.2    Engel, J.3
  • 4
    • 0034644748 scopus 로고    scopus 로고
    • Thrombospondin type 1 repeats interact with matrix metalloproteinases 2. Regulation of metalloproteinases activity
    • Bein, K. and Simons, M. (2000). Thrombospondin type 1 repeats interact with matrix metalloproteinases 2. Regulation of metalloproteinases activity. J. Biol. Chem. 275, 32167-32173.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32167-32173
    • Bein, K.1    Simons, M.2
  • 5
    • 0036156556 scopus 로고    scopus 로고
    • Localization and expression of usherin: A novel basement membrane protein defective in people with Usher syndrome type IIa
    • Bhattacharya, G., Miller, C., Kimberling, W. J., Jablonski, M. M. and Cosgrove, D. (2002). Localization and expression of usherin: a novel basement membrane protein defective in people with Usher syndrome type IIa. Hear Res. 163, 1-11.
    • (2002) Hear Res. , vol.163 , pp. 1-11
    • Bhattacharya, G.1    Miller, C.2    Kimberling, W.J.3    Jablonski, M.M.4    Cosgrove, D.5
  • 6
    • 0029777325 scopus 로고    scopus 로고
    • Structure and distribution of modules in extracellular proteins
    • Bork, P., Downing, A. K., Kieffer, B. and Campbell, I. D. (1996). Structure and distribution of modules in extracellular proteins. Q. Rev. Biophys. 29, 119-167.
    • (1996) Q. Rev. Biophys. , vol.29 , pp. 119-167
    • Bork, P.1    Downing, A.K.2    Kieffer, B.3    Campbell, I.D.4
  • 7
    • 0020619770 scopus 로고
    • Usher syndrome: Definition and estimate of prevalence from two high-risk populations
    • Boughman, J. A., Vernon, M. and Shaver, K. A. (1983). Usher syndrome: definition and estimate of prevalence from two high-risk populations. J. Chron. Dis. 36, 595-603.
    • (1983) J. Chron. Dis. , vol.36 , pp. 595-603
    • Boughman, J.A.1    Vernon, M.2    Shaver, K.A.3
  • 9
    • 0024463888 scopus 로고
    • Dissection of laminin by cathespsin G into its long-arm and short-arm structures and localization of regions involved in calcium dependent stabilization and self-association
    • Bruch, M., Landwehr, R. and Engle, J. (1989). Dissection of laminin by cathespsin G into its long-arm and short-arm structures and localization of regions involved in calcium dependent stabilization and self-association. Eur. J. Biochem. 185, 271-279.
    • (1989) Eur. J. Biochem. , vol.185 , pp. 271-279
    • Bruch, M.1    Landwehr, R.2    Engle, J.3
  • 10
    • 0028952738 scopus 로고
    • Mapping of network-forming, heparin-binding, and α1β1 integrin-recognition sites within the α-chain short arm of laminin-1
    • Colognato-Pyke, H., O'Rear, J. J., Yamada, Y., Carbonetto, S., Cheng, Y. S. and Yurchenco, P. D. (1995). Mapping of network-forming, heparin-binding, and α1β1 integrin-recognition sites within the α-chain short arm of laminin-1. J. Biol. Chem. 270, 9398-9406.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9398-9406
    • Colognato-Pyke, H.1    O'Rear, J.J.2    Yamada, Y.3    Carbonetto, S.4    Cheng, Y.S.5    Yurchenco, P.D.6
  • 11
    • 0031875064 scopus 로고    scopus 로고
    • Ultrastructural, physiological, and molecular defects in the inner ear of a gene-knockout mouse model for autosomal Alport syndrome
    • Cosgrove, D., Samuelson, G., Meehan, D. T., Miller, C., McGee, J., Walsh, E. J. and Siegel, M. (1998). Ultrastructural, physiological, and molecular defects in the inner ear of a gene-knockout mouse model for autosomal Alport syndrome. Hear Res. 121, 84-98.
    • (1998) Hear Res. , vol.121 , pp. 84-98
    • Cosgrove, D.1    Samuelson, G.2    Meehan, D.T.3    Miller, C.4    McGee, J.5    Walsh, E.J.6    Siegel, M.7
  • 12
    • 0019800793 scopus 로고
    • Type IV collagen's isolation and characterization of 7S collagen from human kidney, liver, and lung
    • Dixit, S. N., Stuart, J. M., Seyer, J. M., Risteli, J., Timpl, R. and Kang, A. H. (1981). Type IV collagen's isolation and characterization of 7S collagen from human kidney, liver, and lung. Coll. Relat. Res. 1, 549-556.
    • (1981) Coll. Relat. Res. , vol.1 , pp. 549-556
    • Dixit, S.N.1    Stuart, J.M.2    Seyer, J.M.3    Risteli, J.4    Timpl, R.5    Kang, A.H.6
  • 14
    • 0024413453 scopus 로고
    • EGF-like domains in extracellular matrix proteins: Localized signals for growth and differentiation?
    • Engel, J. (1989). EGF-like domains in extracellular matrix proteins: localized signals for growth and differentiation? FEBS Lett. 251, 1-7.
    • (1989) FEBS Lett. , vol.251 , pp. 1-7
    • Engel, J.1
  • 15
    • 0032479214 scopus 로고    scopus 로고
    • The N-terminal globular domain of the laminin α1 chain binds to α1β1 and α2β1 integrins and to the heparan sulfate-containing domains of perlecan
    • Ettner, N., Gohring, W., Sasaki, T., Mann, K. and Timpl, R. (1998). The N-terminal globular domain of the laminin α1 chain binds to α1β1 and α2β1 integrins and to the heparan sulfate-containing domains of perlecan. FEBS Lett. 430, 217-221.
    • (1998) FEBS Lett. , vol.430 , pp. 217-221
    • Ettner, N.1    Gohring, W.2    Sasaki, T.3    Mann, K.4    Timpl, R.5
  • 17
    • 0034680794 scopus 로고    scopus 로고
    • Tbrombospondin mediates focal adhesion disassembly through interactions with cell surface calreticulin
    • Goicoechea, S., Orr, A. W., Pallero, M. A., Eggleton, P. and Murphy-Ullrich, J. E. (2000). Tbrombospondin mediates focal adhesion disassembly through interactions with cell surface calreticulin. J. Biol. Chem. 275, 36358.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36358
    • Goicoechea, S.1    Orr, A.W.2    Pallero, M.A.3    Eggleton, P.4    Murphy-Ullrich, J.E.5
  • 18
    • 0025744359 scopus 로고
    • Glomerular basement membrane: Identification of the dimeric subunits of the non-collagenous domain (hexamer) of collagen IV and the goodpasture antigen
    • Gunwar, S., Ballester, F, Kalluri, R., Tlmoneda, J., Chonko, C. M., Edwards, S., Noelken, M. E. and Hudson, B. G. (1991). Glomerular basement membrane: identification of the dimeric subunits of the non-collagenous domain (hexamer) of collagen IV and the goodpasture antigen. J. Biol. Chem. 266, 15318-15324.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15318-15324
    • Gunwar, S.1    Ballester, F.2    Kalluri, R.3    Tlmoneda, J.4    Chonko, C.M.5    Edwards, S.6    Noelken, M.E.7    Hudson, B.G.8
  • 19
    • 0032502667 scopus 로고    scopus 로고
    • Glomerular basement membrane: Identification of a novel disulfide-cross-linked network of α3, α4, and α5 chains of type IV collagen and its implications for the pathogenesis of Alport syndrome
    • Gunwar, S., Ballester, F., Kalluri, R., Timoneda, J., Chonko, C. M., Edwards, S., Noelken, M. E. and Hudson, B. G. (1998). Glomerular basement membrane: Identification of a novel disulfide-cross-linked network of α3, α4, and α5 chains of type IV collagen and its implications for the pathogenesis of Alport syndrome. J. Biol. Chem. 273, 8767-8775.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8767-8775
    • Gunwar, S.1    Ballester, F.2    Kalluri, R.3    Timoneda, J.4    Chonko, C.M.5    Edwards, S.6    Noelken, M.E.7    Hudson, B.G.8
  • 20
    • 7944229728 scopus 로고
    • Retinitis pigmentosa combined with congenital deafness; with vestibulo-cerebellar ataxia and neural abnormality in a proportion of cases
    • Hallgren, B. (1959). Retinitis pigmentosa combined with congenital deafness; with vestibulo-cerebellar ataxia and neural abnormality in a proportion of cases. Acta Psychiatr. Scand. Supplement 138, 1-100.
    • (1959) Acta Psychiatr. Scand. , Issue.SUPPL. 138 , pp. 1-100
    • Hallgren, B.1
  • 21
    • 1642533686 scopus 로고
    • Identification of α3(IV) chain of basement membrane collagen as the target for alloantibodies from an Alport patient with complete CO14A5 deletion
    • Kalluri, R., van den Heuvel, L. P., Smeets, H. J., Schroder, C. H., Lemmink, H. H., Boutaud, A., Neilson, E. G. and Hudson, B. G. (1993). Identification of α3(IV) chain of basement membrane collagen as the target for alloantibodies from an Alport patient with complete CO14A5 deletion. Kidney Int. 45, 721-726.
    • (1993) Kidney Int. , vol.45 , pp. 721-726
    • Kalluri, R.1    van den Heuvel, L.P.2    Smeets, H.J.3    Schroder, C.H.4    Lemmink, H.H.5    Boutaud, A.6    Neilson, E.G.7    Hudson, B.G.8
  • 22
    • 15844378205 scopus 로고    scopus 로고
    • Goodpasture autoantigen: Delineation of two inummolgically privileged epitopes on the α3 chain of type IV collagen
    • Kalluri, R., Sun, M. J., Hudson, B. G., and Neilson, E. G. (1996). Goodpasture autoantigen: delineation of two inummolgically privileged epitopes on the α3 chain of type IV collagen. J. Biol. Chem. 271, 9062-9068.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9062-9068
    • Kalluri, R.1    Sun, M.J.2    Hudson, B.G.3    Neilson, E.G.4
  • 23
    • 0031000529 scopus 로고    scopus 로고
    • Isoform switching of type IV glomerular collagen is developmentally arrested in x-linked Alport syndrome increasing its susceptibility to endoproteolysis
    • Kalluri, R., Shield, F., Todd, P., Hudson, B. G. and Neilson, E. G. (1997). Isoform switching of type IV glomerular collagen is developmentally arrested in x-linked Alport syndrome increasing its susceptibility to endoproteolysis. J. Clin. Invest. 99, 2470-2478.
    • (1997) J. Clin. Invest. , vol.99 , pp. 2470-2478
    • Kalluri, R.1    Shield, F.2    Todd, P.3    Hudson, B.G.4    Neilson, E.G.5
  • 24
    • 0034724892 scopus 로고    scopus 로고
    • Assembly of type IV collagen. Insights from α3(IV) collagen-deficient mice
    • Kalluri, R. and Cosgrove, D. (2000). Assembly of type IV collagen. Insights from α3(IV) collagen-deficient mice. J. Biol. Chem. 275, 12719-12724.
    • (2000) J. Biol. Chem. , vol.275 , pp. 12719-12724
    • Kalluri, R.1    Cosgrove, D.2
  • 25
    • 0025876152 scopus 로고
    • Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system
    • Karlsson, R., Michaelsson, A. and Mattsson, L. (1991). Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system. J. Immunol. Meth. 145, 229-240.
    • (1991) J. Immunol. Meth. , vol.145 , pp. 229-240
    • Karlsson, R.1    Michaelsson, A.2    Mattsson, L.3
  • 27
    • 0024465455 scopus 로고
    • Amino acid sequence of mouse nidogen, a multidomain basement membrane protein with binding activity for lammin, collagen IV and cells
    • Mann, K., Deutzmann, R., Aumailley, M., Timpl, R., Raimondi, L., Yamada, Y., Pan, T. C., Conway, D. and Chu, M. L. (1989). Amino acid sequence of mouse nidogen, a multidomain basement membrane protein with binding activity for lammin, collagen IV and cells. EMBO J. 8, 65-72.
    • (1989) EMBO J. , vol.8 , pp. 65-72
    • Mann, K.1    Deutzmann, R.2    Aumailley, M.3    Timpl, R.4    Raimondi, L.5    Yamada, Y.6    Pan, T.C.7    Conway, D.8    Chu, M.L.9
  • 28
    • 0029060614 scopus 로고
    • Low nidogen affinity of laminin-5 can be attributed to two serine residues in EGF-like motif γ2III4
    • Mayer, U., Poschl, E., Gerecke, D. R., Wagman, D. W., Burgeson, R. E. and Timpl, R. (1995). Low nidogen affinity of laminin-5 can be attributed to two serine residues in EGF-like motif γ2III4. FEBS Lett. 365, 129-132.
    • (1995) FEBS Lett. , vol.365 , pp. 129-132
    • Mayer, U.1    Poschl, E.2    Gerecke, D.R.3    Wagman, D.W.4    Burgeson, R.E.5    Timpl, R.6
  • 29
    • 0034109215 scopus 로고    scopus 로고
    • Activation of latent TGF-β by thrombospondin-1: Mechanisms and physiology
    • Murphy-Ullrich, J. E. and Poczatek, M. (2000). Activation of latent TGF-β by thrombospondin-1: Mechanisms and physiology. Cytokine Growth Factor Rev. 11, 59-69.
    • (2000) Cytokine Growth Factor Rev. , vol.11 , pp. 59-69
    • Murphy-Ullrich, J.E.1    Poczatek, M.2
  • 30
    • 0028157338 scopus 로고
    • Matrix-bound thrombospondin promotes angiogenesis in vitro
    • Nicosia, R. F. and Tiszynski, G. P. (1994). Matrix-bound thrombospondin promotes angiogenesis in vitro. J. Cell Biol. 124, 183-193.
    • (1994) J. Cell Biol. , vol.124 , pp. 183-193
    • Nicosia, R.F.1    Tiszynski, G.P.2
  • 31
    • 0014780501 scopus 로고
    • Dystrophia retinae pigmentosa-dyscusis syndrome DRD. A study of the usher or hallgren syndrome
    • Nuutila, A. (1979). Dystrophia retinae pigmentosa-dyscusis syndrome DRD. A study of the usher or hallgren syndrome. J. Genet. Hum. 18, 57-58.
    • (1979) J. Genet. Hum. , vol.18 , pp. 57-58
    • Nuutila, A.1
  • 33
    • 0035775666 scopus 로고    scopus 로고
    • Usher syndrome: From genetics to pathogenesis
    • Petit, C. (2001). Usher syndrome: from genetics to pathogenesis. Annu. Rev. Genomics Hum. Genet. 2, 271-297.
    • (2001) Annu. Rev. Genomics Hum. Genet. , vol.2 , pp. 271-297
    • Petit, C.1
  • 34
    • 0028149335 scopus 로고
    • Binding of purified collagen receptors α1β1, α2β1, and RGD-dependent integrins to laminins and laminin fragments
    • Pfaff, M., Gohring, W., Brown, J. C. and Timpl, R. (1994). Binding of purified collagen receptors α1β1, α2β1, and RGD-dependent integrins to laminins and laminin fragments. Eur. J. Biochem. 225, 975-984.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 975-984
    • Pfaff, M.1    Gohring, W.2    Brown, J.C.3    Timpl, R.4
  • 35
    • 0019138166 scopus 로고
    • 7-S collagen: Characterization of an unusual basement membrane structure
    • Risteli, J., Bachinger, H. P., Engel, J., Furthmayr, H. and Timpl, R. (1980). 7-S collagen: characterization of an unusual basement membrane structure. Eur. J. Biochem. 108, 239-250.
    • (1980) Eur. J. Biochem. , vol.108 , pp. 239-250
    • Risteli, J.1    Bachinger, H.P.2    Engel, J.3    Furthmayr, H.4    Timpl, R.5
  • 36
    • 0033927821 scopus 로고    scopus 로고
    • Missense mutation in the USH2A gene: Association with recessive retinitis pigmentosa without hearing loss
    • Rivolta, C., Sweklo, E. A., Berson, E. L. and Dryja, T. P. (2000). Missense mutation in the USH2A gene: Association with recessive retinitis pigmentosa without hearing loss. Am. J. Hum. Genet. 66, 1975-1978.
    • (2000) Am. J. Hum. Genet. , vol.66 , pp. 1975-1978
    • Rivolta, C.1    Sweklo, E.A.2    Berson, E.L.3    Dryja, T.P.4
  • 37
    • 0028815977 scopus 로고
    • Structural characterization of two variants of fibulin-1 that differ in nidogen affinity
    • Sasaki, T., Kostka, G, Gohring, W., Wiedemann, H., Mann, K., Chu, M. L. and Timpl, R. (1995). Structural characterization of two variants of fibulin-1 that differ in nidogen affinity. J. Mol. Biol. 245, 241-250.
    • (1995) J. Mol. Biol. , vol.245 , pp. 241-250
    • Sasaki, T.1    Kostka, G.2    Gohring, W.3    Wiedemann, H.4    Mann, K.5    Chu, M.L.6    Timpl, R.7
  • 39
    • 0033559259 scopus 로고    scopus 로고
    • Crystal structure of a heparin- and integrin-binding segment of human fibronectin
    • Sharma, A., Askari, J. A., Humphries, M. J., Jones, E. Y. and Stuart, D. I. (1999). Crystal structure of a heparin- and integrin-binding segment of human fibronectin. EMBO J. 18, 1468-1479.
    • (1999) EMBO J. , vol.18 , pp. 1468-1479
    • Sharma, A.1    Askari, J.A.2    Humphries, M.J.3    Jones, E.Y.4    Stuart, D.I.5
  • 40
    • 0033529626 scopus 로고    scopus 로고
    • Cooperation between thrombospondin-1 type 1 repeat peptides and α(v)β(3) Integrin ligands to promote melanoma cell spreading and focal adhesion kinase phosphorylation
    • Sipes, J. M., Krutzsch, H. C., Lawler, J. and Roberts, D. D. (1999). Cooperation between thrombospondin-1 type 1 repeat peptides and α(v)β(3) Integrin ligands to promote melanoma cell spreading and focal adhesion kinase phosphorylation. J. Biol. Chem. 274, 22755-22762.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22755-22762
    • Sipes, J.M.1    Krutzsch, H.C.2    Lawler, J.3    Roberts, D.D.4
  • 41
    • 0029967684 scopus 로고    scopus 로고
    • Crystal structure of three consecutive laminin-type epidermal growth factor-like (LE) modules of laminin gamma1 chain harboring the nidogen binding site
    • Stetefeld, J., Mayer, U., Timpl, R. and Huber, R. (1996). Crystal structure of three consecutive laminin-type epidermal growth factor-like (LE) modules of laminin gamma1 chain harboring the nidogen binding site. J. Mol. Biol. 257, 644-657.
    • (1996) J. Mol. Biol. , vol.257 , pp. 644-657
    • Stetefeld, J.1    Mayer, U.2    Timpl, R.3    Huber, R.4
  • 42
    • 0025370524 scopus 로고
    • Platelet thrombospondin modulates endothelial cell adhesion, motility, and growth: A potential angiogenesis regulatory factor
    • Taraboletti, G., Roberts, D., Liotta, L. A. and Giavazzi, R. (1990). Platelet thrombospondin modulates endothelial cell adhesion, motility, and growth: A potential angiogenesis regulatory factor. J. Cell Biol. 111, 765-772.
    • (1990) J. Cell Biol. , vol.111 , pp. 765-772
    • Taraboletti, G.1    Roberts, D.2    Liotta, L.A.3    Giavazzi, R.4
  • 45
    • 0036333442 scopus 로고    scopus 로고
    • Specific ablation of the nidogen-binding site in the laminin Y1 chain interferes with kidney and lung development
    • Willem, M., Miosge, N., Halfter, W., Smyth, N., Jannetti, I., Burghart, E., Timpl, R. and Mayer, U. (2002). Specific ablation of the nidogen-binding site in the laminin Y1 chain interferes with kidney and lung development. Development 129, 2711-2722.
    • (2002) Development , vol.129 , pp. 2711-2722
    • Willem, M.1    Miosge, N.2    Halfter, W.3    Smyth, N.4    Jannetti, I.5    Burghart, E.6    Timpl, R.7    Mayer, U.8
  • 46
    • 0027313437 scopus 로고
    • Self-assembly and calcium-binding sites in laminin. A three-arm interation model
    • Yurchenco, P. D. and Cheng, Y. S. (1993). Self-assembly and calcium-binding sites in laminin. A three-arm interation model. J. Biol. Chem. 268, 17286-17299.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17286-17299
    • Yurchenco, P.D.1    Cheng, Y.S.2


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