RGD Reference Report - Staring, a novel E3 ubiquitin-protein ligase that targets syntaxin 1 for degradation. - Rat Genome Database

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

Authors: Chin, LS  Vavalle, JP  Li, L 
Citation: Chin LS, etal., J Biol Chem 2002 Sep 20;277(38):35071-9.
RGD ID: 633892
Pubmed: PMID:12121982   (View Abstract at PubMed)
DOI: DOI:10.1074/jbc.M203300200   (Journal Full-text)

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.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Rnf40Ratpositive regulation of proteasomal protein catabolic process  IDA  RGD 
Rnf40Ratpositive regulation of protein polyubiquitination  IDA  RGD 
Rnf40Ratubiquitin-dependent protein catabolic process  IDA  RGD 

Cellular Component

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Rnf40Ratprotein-containing complex  IDA  RGD 

Molecular Function

  

Objects Annotated

Genes (Rattus norvegicus)
Rnf40  (ring finger protein 40)
Stx1b  (syntaxin 1B)


Additional Information