Pikachurin

Dystroglycan ligand with other proteins is essential. Glycosylation of dystroglycan is necessary for its ligand binding activity. Mutations in glycosyltransferase enzymes cause abnormal glycosylation of dystroglycan. This hypoglycosylation is associated with less binding with other proteins and causes some congenital muscular dystrophy. Pikachurin is the most recently identified dystroglycan ligand protein and is localized in the synaptic cleft in the photoreceptor ribbon synapse. The binding between dystroglycan and pikachurin requires divalent cations. Ca2+ produces strongest binding; Mn2+ produces only faint bindings and no binding with Mg2+ alone. Dystroglycan has different domains that allow multiple Ca2+ sites to form a stable pikachurin-dystroglycan connection. This shows that pikachurin can form oligomeric structures; and suggests the possibility of clustering effects can be important in modulating pikachurin-dystroglycan interactions. Another thing to be considered is that the presence of NaCl (0. 5M) strongly inhibits interaction between DG and other ligand proteins but has a modest inhibitory effect with pikachurin-DG ligand. This shows that there are differences between the binding of pikachurin-DG binding and DG binding with other proteins. Pikachurin seems to have more domains to bind with DG than other proteins. For example, experiments in ligand competition shows that presence of pikachurin inhibits laminin-111 binding with DG, but high concentrations of laminin-111 do not inhibit pikachurin binding to DG.

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Figure 1 - Pikachurin is necessary for the apposition of photoreceptor ...

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Figure 6 : Pikachurin, a dystroglycan ligand, is essential for ...

Dystroglycans (Dystroglycan)

Figure 1 : Pikachurin, a dystroglycan ligand, is essential for ...

Dystroglycans (Dystroglycan)

Figure 2 - Pikachurin localizes to the synaptic cleft of photoreceptor ...

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Pikachurin - Wikipedia

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