Publications by authors named "Adam Snow"
Synaptotagmin-1 (syt1) functions as the Ca-dependent sensor that triggers the rapid and synchronous release of neurotransmitters from neurotransmitter-containing vesicles during neuronal exocytosis. The syt1 protein has two homologous tandem C2 domains that interact with phospholipids in a Ca-dependent manner. Despite the crucial role of syt1 in exocytosis, the precise interactions between Ca, syt1, and phospholipids are not fully understood.
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- Limb-Girdle Muscular Dystrophy Type-2B/2R is linked to mutations in the dysferlin gene, particularly two specific missense mutations in the C2A domain.
- These mutations disrupt dysferlin's function in cell membrane repair, likely due to their tendency to form amyloid structures that trigger an inflammatory response.
- The study indicates that inflammation and muscle dysfunction in this condition may result from the pathological effects of these C2A mutations and other similar mutations affecting the protein's hydrophobic core.
Dysferlin plays a critical role in the Ca²⁺-dependent repair of microlesions that occur in the muscle sarcolemma. Of the seven C2 domains in dysferlin, only C2A is reported to bind both Ca²⁺ and phospholipid, thus acting as a key sensor in membrane repair. Dysferlin C2A exists as two isoforms, the "canonical" C2A and C2A variant 1 (C2Av1).
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