A phospho-switch controls the dynamic association of synapsins with synaptic vesicles

Masahiro Hosaka, Robert E Hammer, Thomas C. Südhof

Research output: Contribution to journalArticle

199 Scopus citations

Abstract

Synapsins constitute a family of synaptic vesicle proteins essential for regulating neurotransmitter release. Only two domains are conserved in all synapsins: a short N-terminal A domain with a single phosphorylation site for cAMP-dependent protein kinase (PKA) and CaM Kinase I, and a large central C domain that binds ATP and may be enzymatic. We now demonstrate that synapsin phosphorylation in the A domain, at the only phosphorylation site shared by all synapsins, dissociates synapsins from synaptic vesicles. Furthermore, we show that the A domain binds phospholipids and is inhibited by phosphorylation. Our results suggest a novel mechanism by which proteins reversibly bind to membranes using a phosphorylation-dependent phospholipid- binding domain. The dynamic association of synapsins with synaptic vesicles correlates with their role in activity-dependent plasticity.

Original languageEnglish (US)
Pages (from-to)377-387
Number of pages11
JournalNeuron
Volume24
Issue number2
DOIs
StatePublished - Oct 1999

ASJC Scopus subject areas

  • Neuroscience(all)

Fingerprint Dive into the research topics of 'A phospho-switch controls the dynamic association of synapsins with synaptic vesicles'. Together they form a unique fingerprint.

  • Cite this