Staring, a novel E3 ubiquitin-protein ligase that targets syntaxin 1 for degradation

J Biol Chem. 2002 Sep 20;277(38):35071-9. doi: 10.1074/jbc.M203300200. Epub 2002 Jul 16.


Syntaxin 1 is an essential component of the neurotransmitter release machinery, and regulation of syntaxin 1 expression levels is thought to contribute to the mechanism underlying learning and memory. However, the molecular events that control the degradation of syntaxin 1 remain undefined. Here we report the identification and characterization of a novel RING finger protein, Staring, that interacts with syntaxin 1. Staring is expressed throughout the brain, where it exists in both cytosolic and membrane-associated pools. Staring binds and recruits the brain-enriched E2 ubiquitin-conjugating enzyme UbcH8 to syntaxin 1 and facilitates the ubiquitination and proteasome-dependent degradation of syntaxin 1. These findings suggest that Staring is a novel E3 ubiquitin-protein ligase that targets syntaxin 1 for degradation by the ubiquitin-proteasome pathway.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antigens, Surface / metabolism*
  • Blotting, Northern
  • Blotting, Western
  • Cloning, Molecular
  • DNA, Complementary
  • Humans
  • Hydrolysis
  • Ligases / chemistry
  • Ligases / genetics
  • Ligases / metabolism*
  • Molecular Sequence Data
  • Nerve Tissue Proteins / metabolism*
  • Rats
  • Sequence Homology, Amino Acid
  • Syntaxin 1
  • Ubiquitin-Protein Ligases


  • Antigens, Surface
  • DNA, Complementary
  • Nerve Tissue Proteins
  • STX1A protein, human
  • Stx1a protein, rat
  • Syntaxin 1
  • RNF40 protein, human
  • Ubiquitin-Protein Ligases
  • Ligases

Associated data

  • GENBANK/AF352815