Reactome | Dystroglycan (DG) is a cell-surface laminin receptor. In ske...

Schema > Summation > Entries

Dystroglycan (DG) is a cell-surface laminin receptor. In ske... Show undefined attributes

created	[InstanceEdit:2426629] Jupe, S, 2012-08-08
dbId	2426652
displayName	Dystroglycan (DG) is a cell-surface laminin receptor. In ske...
literatureReference	[LiteratureReference:2328132] Membrane organization of the dystrophin-glycoprotein complex [LiteratureReference:2328093] Muscular dystrophies and the dystrophin-glycoprotein complex [LiteratureReference:2328126] Molecular basis of muscular dystrophies [LiteratureReference:2328092] A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin [LiteratureReference:2426614] Dystroglycan is a binding protein of laminin and merosin in peripheral nerve [LiteratureReference:2328186] 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 [LiteratureReference:2396197] Beta1 integrin and alpha-dystroglycan binding sites are localized to different laminin-G-domain-like (LG) modules within the laminin alpha5 chain G domain [LiteratureReference:2328102] Binding of the G domains of laminin alpha1 and alpha2 chains and perlecan to heparin, sulfatides, alpha-dystroglycan and several extracellular matrix proteins [LiteratureReference:3597672] Laminin-?1 LG4-5 domain binding to dystroglycan mediates muscle cell survival, growth, and the AP-1 and NF-?B transcription factors but also has adverse effects
modified	[InstanceEdit:3597673] Jupe, S, 2013-05-22
schemaClass	Summation
text	Dystroglycan (DG) is a cell-surface laminin receptor. In skeletal muscle it is a central component of the dystrophin-glycoprotein (DGC) complex (Ervasti & Campbell 1991). Mutations in components of the DGC render muscle fibres more susceptible to damage and lead to various types of muscle disorder such as Duchenne muscular dystrophy and limb-girdle muscular dystrophies (Straub & Campbell, 1997, Cohn & Campbell 2000). DG is present as non-covalently associated alpha and beta subunits following cleavage at Ser654. The extracellular alpha subunit binds to laminin-2 (merosin) in the muscle basement membrane while the membrane-associated beta subunit binds dystrophin, which associates with the actin cytoskeleton (Ervasti & Campbell 1993, Yamada et al. 1994, Talts et al. 1999). Alpha-DG also binds the carboxy-terminal G domains of laminin alpha-1 (Gee et al. 1993, Zhou et al. 2012) and alpha-5 (Yu & Talts 2003). The G domains are relatively well conserved in all five alpha-laminin chains, so DG is likely to bind all laminin heterotrimers.

Referrals

(summation)

[Reaction:R-NUL-2426616] Dystroglycan bind Laminins and Dystrophin

© 2026 Reactome

Cite Us!