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Details on Person Agrin (AGRN) is a >400 kDa multi-domain heparan sulfate prot...
| Class:Id | Summation:2467442 |
|---|---|
| _displayName | Agrin (AGRN) is a >400 kDa multi-domain heparan sulfate prot... |
| _timestamp | 2012-12-19 17:24:18 |
| created | [InstanceEdit:2467443] Jupe, S, 2012-09-12 |
| literatureReference | [LiteratureReference:2467109] Defective neuromuscular synaptogenesis in agrin-deficient mutant mice [LiteratureReference:2467084] Agrin isoforms with distinct amino termini: differential expression, localization, and function [LiteratureReference:2396443] Agrin binds to the nerve-muscle basal lamina via laminin [LiteratureReference:2467085] Interaction of agrin with laminin requires a coiled-coil conformation of the agrin-binding site within the laminin gamma1 chain [LiteratureReference:2467098] An alternative amino-terminus expressed in the central nervous system converts agrin to a type II transmembrane protein [LiteratureReference:2467106] Structure and function of laminin LG modules [LiteratureReference:2396046] Integrins mediate adhesion to agrin and modulate agrin signaling [LiteratureReference:2396450] Mapping sites responsible for interactions of agrin with neurons [LiteratureReference:2467103] New insights into the roles of agrin |
| modified | [InstanceEdit:2550419] Jupe, S, 2012-11-02 [InstanceEdit:2867920] Jupe, S, 2012-12-19 |
| text | Agrin (AGRN) is a >400 kDa multi-domain heparan sulfate proteoglycan found in basement membranes. It is a critical organizer of postsynaptic differentiation at the skeletal neuromuscular junction; synaptogenesis is profoundly disrupted in its absence (Gautam et al. 1996). Two alternate N-termini exist. The predominant longer LN form (Burgess et al. 2000) starts with a secretion signal sequence and a laminin-binding domain (Denzer et al. 1995, Kammerer et al. 1999); the shorter SN form associates with the plasma membrane (Burgess et al. 2000, Neumann et al. 2001). Following the SN or LN regions are 8 follistatin repeats, known to bind growth factors and inhibit proteases in other proteins. The central region has two repeats homologous to domain III of laminin. The C-terminal portion, which is responsible for the molecule's known signaling functions, contains four EGF repeats and three LG (G) domains homologous to those found in laminin alpha chains, neurexins and slits (Timpl et al. 2000). The LG domains bind alphaVbeta1 and another beta1-containing integrin (Martin & Sanes 1997, Burgess et al. 2002, Bezakova & Ruegg 2003). The N-terminus of the LN form of AGRN binds to the laminin gamma-1 subunit (Denzer et al. 1997, Kammerer et al. 1999). This may indirectly bind AGRN to integrins on the cell surface (Bezakova & Ruegg 2003). |
| (summation) | [Reaction:2467436] AGRN binds Integrins alphaVbeta1 (Other beta1-containing integrins) [Homo sapiens] |
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