TY - JOUR
T1 - Friends and foes in synaptic transmission
T2 - the role of tomosyn in vesicle priming
AU - Ashery, Uri
AU - Bielopolski, Noa
AU - Barak, Boaz
AU - Yizhar, Ofer
N1 - Funding Information:
We would like to thank Kristen C. Alexander for graphic assistance. This study was supported by grants from the Israel Science Foundation (grant 1211/07; U.A.; www.isf.org.il ), the Adams Super Center for Brain Studies ( www.brain.tau.ac.il ) and the National Institutes of Health (RO1 NS053978; U.A.; www.nih.gov ).
PY - 2009/5
Y1 - 2009/5
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=65349152502&partnerID=8YFLogxK
U2 - 10.1016/j.tins.2009.01.004
DO - 10.1016/j.tins.2009.01.004
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AN - SCOPUS:65349152502
SN - 0166-2236
VL - 32
SP - 275
EP - 282
JO - Trends in Neurosciences
JF - Trends in Neurosciences
IS - 5
ER -