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Dystroglycan binds Laminins and Dystrophin
Stable Identifier
R-HSA-2328129
Type
Reaction [binding]
Species
Homo sapiens
Compartment
plasma membrane
,
cytosol
,
extracellular region
ReviewStatus
5/5
Locations in the PathwayBrowser
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Extracellular matrix organization (Homo sapiens)
Non-integrin membrane-ECM interactions (Homo sapiens)
Dystroglycan binds Laminins and Dystrophin (Homo sapiens)
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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). G domains are relatively well conserved in all five alpha-laminin chains, so DG is likely to bind all laminin heterotrimers.
Participants
Input
DMD [cytosol]
(Homo sapiens)
Dystroglycan [plasma membrane]
(Homo sapiens)
Laminins [extracellular region]
(Homo sapiens)
Output
Dystroglycan:Dystrophin:Laminins [plasma membrane]
(Homo sapiens)
Participates
as an event of
Non-integrin membrane-ECM interactions (Homo sapiens)
Inferred From
Dystroglycan bind Laminins and Dystrophin (Mus musculus)
Authored
Jupe, S (2012-07-31)
Reviewed
Ricard-Blum, S (2013-05-22)
Created
Jupe, S (2012-06-25)
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