Studies on post-golgi syntaxins: Molecular characterisation and function

Abstract

Membrane transport along the exocytic and endocytic pathways are mediated by complex cellular machineries. One determinant for the specificity of fusion of transport vesicles to the target membrane is Soluble N-ethylemaleimide sensitive factor (NSF) attachment protein (SNAP) receptors (SNAREs). SNAREs can be broadly classified into three families: vesicle-associated membrane proteins (VAMPs), syntaxins and SNAP25. Like other SNAREs, syntaxins serve a docking/fusion role in vesicular transport. Sixteen mammalian syntaxins have been identified in the human genome to date. Each of these has a specific cellular localization and corresponding function. This thesis focuses on the molecular and cellular characterization of two post-Golgi syntaxins, syntaxin 9 and syntaxin 10.