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Article

Synaptotagmin I stabilizes synaptic vesicles via its C(2)A polylysine motif.

Genesis (New York, N.Y. : 2000) - 1 May 2009

Mace Kimberly E, Biela Laurie M, Sares Anastasia G, Reist Noreen E

Abstract excerpt

The synaptic vesicle protein, synaptotagmin I, is a multifunctional protein required for several steps in the synaptic vesicle cycle. It is primarily composed of two calcium-binding domains, C(2)A and C(2)B. Within each of these domains, a polylysine motif has been identified that is proposed to mediate specific functions within the synaptic vesicle cycle. While the C(2)B polylysine motif plays an important role...

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PMID: 19358157
DOI: 10.1002/dvg.20502

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Synaptotagmin I stabilizes synaptic vesicles via its C(2)A polylysine motif.PMID 19358157Read ↗

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The C(2)B Ca(2+)-binding motif of synaptotagmin is required for synaptic transmission in vivo.Semantic proximity Read ↗

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A de novo missense mutation in synaptotagmin-1 associated with neurodevelopmental disorder desynchronizes neurotransmitter releaseSemantic proximity Read ↗

synaptotagmin mutants reveal essential functions for the C2B domain in Ca2+-triggered fusion and recycling of synaptic vesicles in vivo.Semantic proximity Read ↗

Neural transmission. Synaptotagmin is just a calcium sensor.Semantic proximity Read ↗

Discrete residues in the c(2)b domain of synaptotagmin I independently specify endocytic rate and synaptic vesicle size.Semantic proximity Read ↗

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