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2015 ; 72
(22
): 4221-35
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Complexins: small but capable
#MMPMID26245303
Mohrmann R
; Dhara M
; Bruns D
Cell Mol Life Sci
2015[Nov]; 72
(22
): 4221-35
PMID26245303
show ga
Despite intensive research, it is still unclear how an immediate and profound
acceleration of exocytosis is triggered by appropriate Ca(2+)-stimuli in
presynaptic terminals. This is due to the fact that the molecular mechanisms of
"docking" and "priming" reactions, which set up secretory vesicles to fuse at
millisecond time scale, are extremely hard to study. Yet, driven by a fruitful
combination of in vitro and in vivo analyses, our mechanistic understanding of
Ca(2+)-triggered vesicle fusion has certainly advanced in the past few years. In
this review, we aim to highlight recent progress and emerging views on the
molecular mechanisms, by which constitutively forming SNAREpins are organized in
functional, tightly regulated units for synchronized release. In particular, we
will focus on the role of the small regulatory factor complexin whose function in
Ca(2+)-dependent exocytosis has been controversially discussed for more than a
decade. Special emphasis will also be laid on the functional relationship of
complexin and synaptotagmin, as both proteins possibly act as allies and/or
antagonists to govern SNARE-mediated exocytosis.
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