Membrane fusion::SNARE (protein)


Journal::snare    Membrane::fusion    Title::volume    Pages::proteins    Complex::snap-    Issue::vauthors

Membrane fusion

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Layering of the core SNARE complex. In the center is the zero hydrophilic ionic layer, flanked by hydrophobic leucine-zipper layers.

During membrane fusion, v-SNARE and t-SNARE proteins on separate membranes combine to form a trans-SNARE complex, also known as a "SNAREpin". Depending on the stage of fusion of the membranes, these complexes may be referred to differently.

During fusion of trans-SNARE complexes, the membranes merge and SNARE proteins involved in complex formation after fusion are then referred to as a "cis"-SNARE complex, because they now reside in a single (or cis) resultant membrane. After fusion, the cis-SNARE complex is bound and disassembled by an adaptor protein, alphaSNAP. Then, the hexameric AAA-ATPase NSF catalyzes the ATP-dependent unfolding of the SNARE proteins and releases them into the cytosol for recycling.

SNAREs are thought to be the core required components of the fusion machinery and can function independently of additional cytosolic accessory proteins. This was demonstrated by engineering "flipped" SNAREs, where the SNARE domains face the extracellular space rather than the cytosol. When cells containing v-SNAREs contact cells containing t-SNAREs, trans-SNARE complexes form and cell-cell fusion ensues.<ref>{{#invoke:Citation/CS1|citation |CitationClass=journal }}</ref>

SNARE (protein) sections
Intro   Types    Structure    Membrane fusion    Components    Mechanism of membrane fusion   Regulatory Effects on Exocytosis   Toxins    Role in neurotransmitter release    Role in autophagy   References  External links  

Membrane fusion