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#cellular trafficking

2 public questions tagged with this topic.

Which protein is responsible for recycling SNARE complexes for reuse?

Maintenance of available fusion-competent SNAREs requires constant recycling machinery whose failure halts secretion rapidly. After vesicle fusion, v- and t-SNAREs intertwined as cis complex on acceptor membrane representing low-energy product. Soluble alpha-SNAP 35 kDa oligomerizes along complex as three to four copies per bundle recognizing acidic surface patches. Hexameric NSF ATPase binds SNAP coat via N-domains forming 20S particle originally observed in detergent extracts. Upon ATP hydrolysis D1 ring undergoes large movements pulling SNAREs through central pore with mechanical force unfo

Ref: Alberts et al., MBC Chapter 13: NSF recycling of SNARE complexes for multiple rounds.

What triggers the disassembly of SNARE complexes after membrane fusion?

Cis-SNARE complexes formed post-fusion are extremely stable four-helix bundles with melting temperature above 90 Celsius requiring energy for recycling. Disassembly machinery uses ATP. Hexameric AAA+ ATPase NSF N-ethylmaleimide sensitive factor assembles as ring with two stacked ATPase tiers D1 catalytic and D2 structural. Adaptor alpha-SNAP soluble attachment protein binds grooves along rod-like bundle via tetratricopeptide repeats and recruits NSF via N domains interaction with SNAP C-terminus. ATP hydrolysis in D1 causes power stroke threading SNARE polypeptide through central pore with tyr

Ref: Lodish et al., MCB Chapter 14: NSF and alpha-SNAP disassemble cis-SNARE complexes via ATP hydrolysis.