메뉴 건너뛰기




Volumn 332, Issue 3, 2003, Pages 635-642

Distinct requirements for heparin and α-dystroglycan binding revealed by structure-based mutagenesis of the laminin α2 LG4-LG5 domain pair

Author keywords

Basement membrane; Cell adhesion; Extracellular matrix; Laminin G like domain; Receptor binding

Indexed keywords

ALPHA DYSTROGLYCAN; CALCIUM ION; GLYCAN DERIVATIVE; HEPARIN; LAMININ; LAMININ G4; LAMININ G5; PROTEIN SUBUNIT; SULFATIDE; UNCLASSIFIED DRUG;

EID: 0042736851     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00848-9     Document Type: Article
Times cited : (68)

References (33)
  • 1
    • 0034075654 scopus 로고    scopus 로고
    • Form and function: The laminin family of heterotrimers
    • Colognato H., Yurchenco P.D. Form and function: the laminin family of heterotrimers. Dev. Dyn. 218:2000;213-234.
    • (2000) Dev. Dyn. , vol.218 , pp. 213-234
    • Colognato, H.1    Yurchenco, P.D.2
  • 2
    • 0038330238 scopus 로고    scopus 로고
    • The role of laminin in embryonic cell polarization and tissue organization
    • Li S., Edgar D., Fässler R., Wadsworth W., Yurchenco P.D. The role of laminin in embryonic cell polarization and tissue organization. Dev. Cell. 4:2003;613-624.
    • (2003) Dev. Cell , vol.4 , pp. 613-624
    • Li, S.1    Edgar, D.2    Fässler, R.3    Wadsworth, W.4    Yurchenco, P.D.5
  • 3
    • 0030087944 scopus 로고    scopus 로고
    • Supramolecular assembly of basement membranes
    • Timpl R., Brown J.C. Supramolecular assembly of basement membranes. Bioessays. 18:1996;123-132.
    • (1996) Bioessays , vol.18 , pp. 123-132
    • Timpl, R.1    Brown, J.C.2
  • 5
    • 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 domains
    • Deutzmann R., Aumailley M., Wiedemann H., Pysny W., Timpl R., Edgar D. Cell adhesion, spreading and neurite stimulation by laminin fragment E8 depends on maintenance of secondary and tertiary structure in its rod and globular domains. Eur. J. Biochem. 191:1990;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
  • 6
    • 0027520442 scopus 로고
    • Cell and heparin binding in the distal long arm of laminin: Identification of active and cryptic sites with recombinant and hybrid glycoprotein
    • Sung U., O'Rear J.J., Yurchenco P.D. Cell and heparin binding in the distal long arm of laminin: identification of active and cryptic sites with recombinant and hybrid glycoprotein. J. Cell Biol. 123:1993;1255-1268.
    • (1993) J. Cell Biol. , vol.123 , pp. 1255-1268
    • Sung, U.1    O'Rear, J.J.2    Yurchenco, P.D.3
  • 7
    • 0027321171 scopus 로고
    • Laminin-binding protein 120 from brain is closely related to the dystrophin-associated glycoprotein, dystroglycan, and binds with high affinity to the major heparin binding domain of laminin
    • Gee S.H., Blacher R.W., Douville P.J., Provost P.R., Yurchenco P.D., Carbonetto S. Laminin-binding protein 120 from brain is closely related to the dystrophin-associated glycoprotein, dystroglycan, and binds with high affinity to the major heparin binding domain of laminin. J. Biol. Chem. 268:1993;14972-14980.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14972-14980
    • Gee, S.H.1    Blacher, R.W.2    Douville, P.J.3    Provost, P.R.4    Yurchenco, P.D.5    Carbonetto, S.6
  • 8
    • 0033605915 scopus 로고    scopus 로고
    • Analysis of heparin, α-dystroglycan and sulfatide binding to the G domain of laminin α1 chain by site-directed mutagenesis
    • Andac Z., Sasaki T., Mann K., Brancaccio A., Deutzmann R., Timpl R. Analysis of heparin, α-dystroglycan and sulfatide binding to the G domain of laminin α1 chain by site-directed mutagenesis. J. Mol. Biol. 287:1999;253-264.
    • (1999) J. Mol. Biol. , vol.287 , pp. 253-264
    • Andac, Z.1    Sasaki, T.2    Mann, K.3    Brancaccio, A.4    Deutzmann, R.5    Timpl, R.6
  • 9
    • 0037166935 scopus 로고    scopus 로고
    • Matrix assembly, regulation, and survival functions of laminin and its receptors in embryonic stem cell differentiation
    • Li S., Harrison D., Carbonetto S., Fässler R., Smyth N., Edgar D., Yurchenco P.D. Matrix assembly, regulation, and survival functions of laminin and its receptors in embryonic stem cell differentiation. J. Cell Biol. 157:2002;1279-1290.
    • (2002) J. Cell Biol. , vol.157 , pp. 1279-1290
    • Li, S.1    Harrison, D.2    Carbonetto, S.3    Fässler, R.4    Smyth, N.5    Edgar, D.6    Yurchenco, P.D.7
  • 10
    • 0030026572 scopus 로고    scopus 로고
    • Differential heparin inhibition of skeletal muscle α-dystroglycan binding to laminins
    • Pall E.A., Bolton K.M., Ervasti J.M. Differential heparin inhibition of skeletal muscle α-dystroglycan binding to laminins. J. Biol. Chem. 271:1996;3817-3821.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3817-3821
    • Pall, E.A.1    Bolton, K.M.2    Ervasti, J.M.3
  • 11
    • 0033557707 scopus 로고    scopus 로고
    • Binding of the G domains of laminin α1 and α2 chains and perlecan to heparin, sulfatides, α-dystroglycan and several extracellular matrix proteins
    • Talts J.F., Andac Z., Göhring W., Brancaccio A., Timpl R. Binding of the G domains of laminin α1 and α2 chains and perlecan to heparin, sulfatides, α-dystroglycan and several extracellular matrix proteins. EMBO J. 18:1999;863-870.
    • (1999) EMBO J. , vol.18 , pp. 863-870
    • Talts, J.F.1    Andac, Z.2    Göhring, W.3    Brancaccio, A.4    Timpl, R.5
  • 13
    • 0038182574 scopus 로고    scopus 로고
    • Dystrophin-glycoprotein complex: Post-translational processing and dystroglycan function
    • Michele D.E., Campbell K.P. Dystrophin-glycoprotein complex: post-translational processing and dystroglycan function. J. Biol. Chem. 278:2003;15457-15460.
    • (2003) J. Biol. Chem. , vol.278 , pp. 15457-15460
    • Michele, D.E.1    Campbell, K.P.2
  • 14
    • 0034600063 scopus 로고    scopus 로고
    • Structure of the C-terminal laminin G-like domain pair of the laminin α2 chain harbouring binding sites for α-dystroglycan and heparin
    • Tisi D., Talts J.F., Timpl R., Hohenester E. Structure of the C-terminal laminin G-like domain pair of the laminin α2 chain harbouring binding sites for α-dystroglycan and heparin. EMBO J. 19:2000;1432-1440.
    • (2000) EMBO J. , vol.19 , pp. 1432-1440
    • Tisi, D.1    Talts, J.F.2    Timpl, R.3    Hohenester, E.4
  • 16
    • 0033231551 scopus 로고    scopus 로고
    • The crystal structure of a laminin G-like module reveals the molecular basis of α-dystroglycan binding to laminins, perlecan and agrin
    • Hohenester E., Tisi D., Talts J.F., Timpl R. The crystal structure of a laminin G-like module reveals the molecular basis of α-dystroglycan binding to laminins, perlecan and agrin. Mol. Cell. 4:1999;783-792.
    • (1999) Mol. Cell , vol.4 , pp. 783-792
    • Hohenester, E.1    Tisi, D.2    Talts, J.F.3    Timpl, R.4
  • 18
    • 0345148341 scopus 로고    scopus 로고
    • Structural basis of glycosaminoglycan modification and of heterotypic interactions of perlecan domain V
    • Friedrich M.V., Göhring W., Mörgelin M., Brancaccio A., David G., Timpl R. Structural basis of glycosaminoglycan modification and of heterotypic interactions of perlecan domain V. J. Mol. Biol. 294:1999;259-270.
    • (1999) J. Mol. Biol. , vol.294 , pp. 259-270
    • Friedrich, M.V.1    Göhring, W.2    Mörgelin, M.3    Brancaccio, A.4    David, G.5    Timpl, R.6
  • 19
    • 0032502958 scopus 로고    scopus 로고
    • Structural analysis and proteolytic processing of recombinant G domain of mouse laminin α2 chain
    • Talts J.F., Mann K., Yamada Y., Timpl R. Structural analysis and proteolytic processing of recombinant G domain of mouse laminin α2 chain. FEBS Letters. 426:1998;71-76.
    • (1998) FEBS Letters , vol.426 , pp. 71-76
    • Talts, J.F.1    Mann, K.2    Yamada, Y.3    Timpl, R.4
  • 20
    • 0029664729 scopus 로고    scopus 로고
    • Characterization of dystroglycan-laminin interactions in peripheral nerve
    • Yamada H., Chiba A., Endo T., Kobata A., Anderson L.V.B., Hori H., et al. Characterization of dystroglycan-laminin interactions in peripheral nerve. J. Neurochem. 66:1996;1518-1524.
    • (1996) J. Neurochem. , vol.66 , pp. 1518-1524
    • Yamada, H.1    Chiba, A.2    Endo, T.3    Kobata, A.4    Anderson, L.V.B.5    Hori, H.6
  • 22
    • 0038607100 scopus 로고    scopus 로고
    • Calcium plays a critical role in determining the AchR-clustering activities of alternatively spliced isoforms of agrin
    • Tseng C.-N., Zhang L., Cascio M., Wang Z.-Z. Calcium plays a critical role in determining the AchR-clustering activities of alternatively spliced isoforms of agrin. J. Biol. Chem. 278:2003;17236-17245.
    • (2003) J. Biol. Chem. , vol.278 , pp. 17236-17245
    • Tseng, C.-N.1    Zhang, L.2    Cascio, M.3    Wang, Z.-Z.4
  • 23
    • 0037055258 scopus 로고    scopus 로고
    • Genetic evidence for a dystrophin-glycoprotein complex (DGC) in Caenorhabditis elegans
    • Grisoni K., Martin E., Gieseler K., Mariol M.C., Segalat L. Genetic evidence for a dystrophin-glycoprotein complex (DGC) in Caenorhabditis elegans. Gene. 294:2002;77-86.
    • (2002) Gene , vol.294 , pp. 77-86
    • Grisoni, K.1    Martin, E.2    Gieseler, K.3    Mariol, M.C.4    Segalat, L.5
  • 25
    • 0034634679 scopus 로고    scopus 로고
    • Structural and functional analysis of the recombinant G domain of the laminin α4 chain and its proteolytic processing in tissues
    • Talts J.F., Sasaki T., Miosge N., Göhring W., Mann K., Mayne R., Timpl R. Structural and functional analysis of the recombinant G domain of the laminin α4 chain and its proteolytic processing in tissues. J. Biol. Chem. 275:2000;35192-35199.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35192-35199
    • Talts, J.F.1    Sasaki, T.2    Miosge, N.3    Göhring, W.4    Mann, K.5    Mayne, R.6    Timpl, R.7
  • 26
    • 0038414615 scopus 로고    scopus 로고
    • β1 integrin and α-dystroglycan binding sites are localized to different LG modules within the laminin α5 chain
    • Yu H., Talts J.F. β1 integrin and α-dystroglycan binding sites are localized to different LG modules within the laminin α5 chain. J. Biochem. 371:2003;289-299.
    • (2003) J. Biochem. , vol.371 , pp. 289-299
    • Yu, H.1    Talts, J.F.2
  • 27
    • 0030804282 scopus 로고    scopus 로고
    • Properties of the extracellular calcium binding module of the proteoglycan testican
    • Kohfeldt E., Maurer P., Vannahme C., Timpl R. Properties of the extracellular calcium binding module of the proteoglycan testican. FEBS Letters. 414:1997;557-561.
    • (1997) FEBS Letters , vol.414 , pp. 557-561
    • Kohfeldt, E.1    Maurer, P.2    Vannahme, C.3    Timpl, R.4
  • 29
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite: programs for protein crystallography. Acta Crystallog. D. 20:1994;760-763.
    • (1994) Acta Crystallog. D , vol.20 , pp. 760-763
  • 31
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11:1991;281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 32
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MOLSCRIPT which includes greatly enhanced colouring facilities
    • Esnouf R.M. An extensively modified version of MOLSCRIPT which includes greatly enhanced colouring facilities. J. Mol. Graph. 15:1997;132-134.
    • (1997) J. Mol. Graph. , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 33
    • 0028057108 scopus 로고
    • Raster3D version 2.0. A program for photorealistic molecular graphics
    • Merritt E.A., Murphy M.E.P. Raster3D version 2.0. A program for photorealistic molecular graphics. Acta Crystallog. D50:1994;869-873.
    • (1994) Acta Crystallog. , vol.50 D , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.