Friends and foes in synaptic transmission: the role of tomosyn in vesicle priming

Uri Ashery*, Noa Bielopolski, Boaz Barak, Ofer Yizhar

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

47 Scopus citations

Abstract

Priming is the process by which vesicles become available for fusion at nerve terminals and is modulated by numerous proteins and second messengers. One of the prominent members of this diverse family is tomosyn. Tomosyn has been identified as a syntaxin-binding protein; it inhibits vesicle priming, but its mode of action is not fully understood. The inhibitory activity of tomosyn depends on its N-terminal WD40-repeat domain and is regulated by the binding of its SNARE motif to syntaxin. Here, we describe new physiological information on the function of tomosyn and address possible interpretations of these results in the framework of the recently described crystal structure of the yeast tomosyn homolog Sro7. We also present possible molecular scenarios for vesicle priming and the involvement of tomosyn in these processes.

Original languageEnglish
Pages (from-to)275-282
Number of pages8
JournalTrends in Neurosciences
Volume32
Issue number5
DOIs
StatePublished - May 2009

Funding

FundersFunder number
National Institutes of HealthRO1 NS053978
National Institute on AgingZIAAG000317
Israel Science Foundation1211/07

    Fingerprint

    Dive into the research topics of 'Friends and foes in synaptic transmission: the role of tomosyn in vesicle priming'. Together they form a unique fingerprint.

    Cite this