Chapter Category: Cell Metabolism

From the book SNARE Proteins

SNARE Protein Effectors

Travis L. Rodkey and James McNew

SNARE proteins have been well characterized as the minimal machinery necessary for membrane fusion. SNARE‑mediated fusion at the plasma membrane begins with regulated formation of a t‑SNARE complex composed of syntaxin1A and SNAP25. This binary t‑SNARE complex can then bind to the v‑SNARE VAMP2, pulling the lipid bilayers into intimate contact and providing mechanical force for membrane fusion. Several regulatory proteins interact with the SNAREs to affect the fusion event. The regulatory role of SM proteins, complexins and synaptotagmins are the best characterized SNARE regulators to date, although many others are under investigation. SM proteins are thought to inhibit fusion by binding free syntaxin, preventing t‑SNARE complex formation. However, recent in vivo and in vitro data suggest SM proteins play a positive role in fusion by bridging v‑t‑SNARE interactions. Complexins function as fusion clamps that bind the assembled ternary SNARE complex and arrest fusion at the hemifusion intermediate. Synaptotagmins act as calcium sensors and facilitate fusion after calcium influx and relieve the hemifusion block imposed by complexins. Although the functions of these SNARE regulators have been well studied, much remains to be learned about the interactions between SNAREs and their regulatory factors on the molecular level.

Taken from the book

SNARE Proteins

Edited by: Francesco Filippini and David Banfield

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