Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro.
A cell-free system that mimics the reassembly of Golgi stacks at the end of mitosis requires two ATPases, NSF and p97, to rebuild Golgi cisternae. Morphological studies now show that alpha-SNAP, a component of the NSF pathway, can inhibit the p97 pathway, whereas p47, a component of the p97 pathway, can inhibit the NSF pathway. Anti-syntaxin 5 antibodies and a soluble, recombinant syntaxin 5 inhibited both pathways, suggesting that this t-SNARE is a common component. Biochemical studies confirmed this, showing that p47 binds directly to syntaxin 5 and competes for binding with alpha-SNAP. p47 also mediates the binding of p97 to syntaxin 5 and so plays an analogous role to alpha-SNAP, which mediates the binding of NSF.
Pubmed ID: 9506515 RIS Download
Adenosine Triphosphatases | Animals | Binding, Competitive | Carrier Proteins | Cell-Free System | Cytosol | Golgi Apparatus | HeLa Cells | Humans | Intracellular Membranes | Liver | Membrane Fusion | Membrane Proteins | Mitosis | N-Ethylmaleimide-Sensitive Proteins | Protein Binding | Qa-SNARE Proteins | Rats | Recombinant Fusion Proteins | Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins | Vesicular Transport Proteins