Work

PI(4,5)P 2 -dependent regulation of exocytosis by amisyn, the vertebrate-specific competitor of synaptobrevin 2

Year: 2020

Type: article

Abstract: Significance Exocytosis is of vital importance for life, as it allows cells to communicate with each other and with their environment. This dynamic process is highly regulated with a set of both positive and negative regulators. While promotors of exocytosis are well studied, negative regulators are poorly understood. We discovered that a small SNARE protein amisyn (STXBP6) acts as a vertebrate-specific competitor of synaptobrevin-2, a key player in exocytosis. Amisyn contains an N-terminal pleckstrin homology domain that mediates its transient association with the plasma membrane by binding to phospholipid PI(4,5)P 2 . Both the pleckstrin homology and SNARE domains are needed to inhibit exocytosis. Understanding the mechanisms by which amisyn regulates exocytosis will advance our comprehension of pathological processes in diabetes and autism.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.1908232117