Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro

Cell. 1998 Mar 6;92(5):603-10. doi: 10.1016/s0092-8674(00)81128-9.

Abstract

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.

MeSH terms

  • Adenosine Triphosphatases / metabolism*
  • Animals
  • Binding, Competitive
  • Carrier Proteins / metabolism*
  • Cell-Free System
  • Cytosol
  • Golgi Apparatus / metabolism*
  • HeLa Cells
  • Humans
  • Intracellular Membranes
  • Liver
  • Membrane Fusion / physiology*
  • Membrane Proteins / metabolism*
  • Mitosis
  • N-Ethylmaleimide-Sensitive Proteins
  • Protein Binding
  • Qa-SNARE Proteins
  • Rats
  • Recombinant Fusion Proteins / metabolism
  • Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
  • Vesicular Transport Proteins*

Substances

  • Carrier Proteins
  • Membrane Proteins
  • Nsfl1c protein, rat
  • Qa-SNARE Proteins
  • Recombinant Fusion Proteins
  • Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
  • Vesicular Transport Proteins
  • Adenosine Triphosphatases
  • N-Ethylmaleimide-Sensitive Proteins
  • Nsf protein, rat