The Septin CDCrel-1 Binds Syntaxin and Inhibits Exocytosis

Nat Neurosci. 1999 May;2(5):434-9. doi: 10.1038/8100.

Abstract

Septins are GTPases required for the completion of cytokinesis in diverse organisms, yet their roles in cytokinesis or other cellular processes remain unknown. Here we describe studies of a newly identified septin, CDCrel-1, which is predominantly expressed in the nervous system. This protein was associated with membrane fractions, and a significant fraction of the protein copurified and coprecipitated with synaptic vesicles. In detergent extracts, CDCrel-1 and another septin, Nedd5, immunoprecipitated with the SNARE protein syntaxin by directly binding to syntaxin via the SNARE interaction domain. Transfection of HIT-T15 cells with wild-type CDCrel-1 inhibited secretion, whereas GTPase dominant-negative mutants enhanced secretion. These data suggest that septins may regulate vesicle dynamics through interactions with syntaxin.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Cell Membrane / metabolism
  • Cytoskeletal Proteins / metabolism
  • Exocytosis / physiology*
  • GTP Phosphohydrolases / metabolism*
  • Gene Library
  • Humans
  • Hybridomas
  • Immunohistochemistry
  • Membrane Proteins / metabolism*
  • Nerve Tissue Proteins / metabolism*
  • PC12 Cells
  • Protein Binding
  • Qa-SNARE Proteins
  • Rats
  • Transfection

Substances

  • Cytoskeletal Proteins
  • Membrane Proteins
  • Nerve Tissue Proteins
  • Qa-SNARE Proteins
  • GTP Phosphohydrolases