Do SNARE Protein Isoforms Determine Fusion Pore Characteristics?
نویسندگان
چکیده
منابع مشابه
Nanodisc-cell fusion: control of fusion pore nucleation and lifetimes by SNARE protein transmembrane domains
The initial, nanometer-sized connection between the plasma membrane and a hormone- or neurotransmitter-filled vesicle -the fusion pore- can flicker open and closed repeatedly before dilating or resealing irreversibly. Pore dynamics determine release and vesicle recycling kinetics, but pore properties are poorly known because biochemically defined single-pore assays are lacking. We isolated sing...
متن کاملFusion Pore Dynamics Are Regulated by Synaptotagmin•t-SNARE Interactions
Exocytosis involves the formation of a fusion pore that connects the lumen of secretory vesicles with the extracellular space. Exocytosis from neurons and neuroendocrine cells is tightly regulated by intracellular [Ca2+] and occurs rapidly, but the molecular events that mediate the opening and subsequent dilation of fusion pores remain to be determined. A putative Ca2+ sensor for release, synap...
متن کاملThe role of the C terminus of the SNARE protein SNAP-25 in fusion pore opening and a model for fusion pore mechanics.
Formation of a fusion pore between a vesicle and its target membrane is thought to involve the so-called SNARE protein complex. However, there is no mechanistic model explaining how the fusion pore is opened by conformational changes in the SNARE complex. It has been suggested that C-terminal zipping triggers fusion pore opening. A SNAP-25 mutant named SNAP-25Delta9 (lacking the last nine C-ter...
متن کاملExocytotic pore in a SNARE
In 2013, the Nobel prize was awarded for discoveries related to the regulation of the cellular transport system (https://www.nobelprize.org/nobel_prizes/medicine/ laureates/2013/). In addition to studies by Südhof’s lab of signals that tell secretory vesicles when to release their cargo and the work of Schekman’s lab describing a set of genes required for vesicle transport, the Rothman’s lab de...
متن کاملPositively charged amino acids at the SNAP-25 C terminus determine fusion rates, fusion pore properties, and energetics of tight SNARE complex zippering.
SNAP-25 is a Q-SNARE protein mediating exocytosis of neurosecretory vesicles including chromaffin granules. Previous results with a SNAP-25 construct lacking the nine C terminal residues (SNAP-25Δ9) showed changed fusion pore properties (Fang et al., 2008), suggesting a model for fusion pore mechanics that couple C terminal zipping of the SNARE complex to the opening of the fusion pore. The del...
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ژورنال
عنوان ژورنال: The Journal of Neuroscience
سال: 2015
ISSN: 0270-6474,1529-2401
DOI: 10.1523/jneurosci.2087-15.2015