Syntaxin 1A interacts with multiple exocytic proteins to regulate neurotransmitter release in vivo

Mark N. Wu, Tim Fergestad, Thomas E. Lloyd, Yuchun He, Kendal Broadie, Hugo J. Bellen

Research output: Contribution to journalArticlepeer-review

Abstract

Biochemical studies suggest that syntaxin 1A participates in multiple protein-protein interactions in the synaptic terminal, but the in vivo significance of these interactions is poorly understood. We used a targeted mutagenesis approach to eliminate specific syntaxin binding interactions and demonstrate that Drosophila syntaxin 1A plays multiple regulatory roles in neurotransmission in vivo. Syntaxin mutations that eliminate ROP/Munc-18 binding display increased neurotransmitter release, suggesting that ROP inhibits neurosecretion through its interaction with syntaxin. Syntaxin mutations that block Ca2+ channel binding also cause an increase in neurotransmitter release, suggesting that syntaxin normally functions in inhibiting Ca2+ channel opening. Additionally, we identify and characterize a syntaxin Ca2+ effector domain, which may spatially organize the Ca2+ channel, cysteine string protein, and synaptotagmin for effective excitation- secretion coupling in the presynaptic terminal.

Original languageEnglish (US)
Pages (from-to)593-605
Number of pages13
JournalNeuron
Volume23
Issue number3
DOIs
StatePublished - Jul 1999
Externally publishedYes

ASJC Scopus subject areas

  • Neuroscience(all)

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