Abstract
SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins are a highly conserved set of membrane-associated proteins that mediate intracellular membrane fusion. Cognate SNAREs from two separate membranes zipper to facilitate membrane apposition and fusion. Though the stable post-fusion conformation of SNARE complex has been extensively studied with biochemical and biophysical means, the pathway of SNARE zippering has been elusive. In this review, we describe some recent progress in understanding the pathway of SNARE zippering. We particularly focus on the half-zippered intermediate, which is most likely to serve as the main point of regulation by the auxiliary factors.
Highlights
Many vital life processes in eukaryotic cells, such as trafficking of proteins or membranes and secretion of hormones or neurotransmitters, require membrane fusion
It is established that widely conserved soluble N-ethylmaleimidesensitive factor attachment protein receptor (SNARE) proteins are the primary fusogen, responsible for most intracellular membrane fusion [1,2,3]
Cognate coiled–coiled interactions between v- and target membrane-anchored SNARE (t-SNARE) are the basis for SNARE complex formation [6,7]
Summary
Synopsis SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins are a highly conserved set of membrane-associated proteins that mediate intracellular membrane fusion. Cognate SNAREs from two separate membranes zipper to facilitate membrane apposition and fusion. Though the stable post-fusion conformation of SNARE complex has been extensively studied with biochemical and biophysical means, the pathway of SNARE zippering has been elusive. We describe some recent progress in understanding the pathway of SNARE zippering. We focus on the half-zippered intermediate, which is most likely to serve as the main point of regulation by the auxiliary factors.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have