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Complexins: small but capable
- Source :
- Cellular and Molecular Life Sciences
- Publication Year :
- 2015
- Publisher :
- Springer Science and Business Media LLC, 2015.
-
Abstract
- 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.
- Subjects :
- Vesicle fusion
Membrane fusion
Nerve Tissue Proteins
Review
Complexin
Biology
Models, Biological
Synaptic vesicle
Exocytosis
Synaptotagmin 1
Synaptotagmins
Cellular and Molecular Neuroscience
Humans
Ca2+ triggered exocytosis
Molecular Biology
Pharmacology
STX1A
Munc-18
Cell Biology
Secretory Vesicle
Synaptotagmin
Cell biology
Adaptor Proteins, Vesicular Transport
SNARE regulators
Molecular Medicine
Calcium
Synaptic Vesicles
SNARE Proteins
Protein Binding
Subjects
Details
- ISSN :
- 14209071 and 1420682X
- Volume :
- 72
- Database :
- OpenAIRE
- Journal :
- Cellular and Molecular Life Sciences
- Accession number :
- edsair.doi.dedup.....d550228bf51f93e090424106f81503bf