Intracellular membrane fusion is conserved from @entity375 to @entity1 as well as among different intracellular trafficking pathways. This process can be generally divided into several well-defined biochemical reactions. First, an early recognition (or tethering) takes place between donor and acceptor membranes, mediated by ypt/rab GTPases and complexes of tethering factors. Subsequently, a closer association between the two membranes is achieved by a docking process, which involves tight association between membrane proteins termed SNAREs. The formation of such a trans-SNARE complex leads to the final membrane fusion, resulting in an accumulation of cis-SNARE complexes on the acceptor membrane. Thus, multiple rounds of transport and delivery of the donor SNARE back to its original membrane require dissociation of the SNARE complexes. SNARE dissociation, termed priming, is mediated by the AAA ATPase, @entity8816 -sensitive factor (NSF) and its partner, soluble NSF attachment protein (SNAP), in a reaction that requires @entity855 hydrolysis. In the present review we focus on @entity41947 and GATE-16, two low-molecular-weight proteins, which assist in priming SNARE molecules in the vacuole in @entity375 and the Golgi complex in mammals, respectively. @entity41947 and GATE-16 are suggested to keep the dissociated cis-SNAREs apart from each other, allowing multiple fusion processes to take place. GATE-16 belongs to a novel family of ubiquitin-like proteins conserved from @entity375 to @entity1 . We discuss here the involvement of this family in multiple intracellular trafficking pathways.

Involvement of XXXX and GATE-16 family members in intracellular membrane dynamics.

@entity1 :: ('9606', 'Species') :: ['man'] @entity8816 :: ('MESH:D005033', 'Chemical') :: ['N-ethylmaleimide'] @entity41947 :: ('855717(Tax:4932)', 'Gene') :: ['LMA1'] @entity375 :: ('4932', 'Species') :: ['yeast'] @entity855 :: ('MESH:D000255', 'Chemical') :: ['ATP']
@entity41947 :: (855717(Tax:4932),Gene) :: ['LMA1']
