Journal article
A Novel Route for F-box Protein-mediated Ubiquitination Links CHIP to Glycoprotein Quality Control
The Journal of biological chemistry, Vol.281(29), pp.20242-20251
07/21/2006
DOI: 10.1074/jbc.M602423200
PMID: 16682404
Abstract
In SCF (Skp1/Cullin/F-box protein) ubiquitin ligases, substrate specificity is conferred by a diverse array of F-box proteins. Only in fully assembled SCF complexes, it is believed, can substrates bound to F-box proteins become ubiquitinated. Here we show that Fbx2, a brain-enriched F-box protein implicated in the ubiquitination of glycoproteins discarded from the endoplasmic reticulum, binds the co-chaperone/ubiquitin ligase CHIP (C terminus of Hsc-70-interacting protein) through a unique N-terminal PEST domain in Fbx2. CHIP facilitates the ubiquitination and degradation of Fbx2-bound glycoproteins, including unassembled NMDA receptor subunits. These findings indicate that CHIP acts with Fbx2 in a novel ubiquitination pathway that links CHIP to glycoprotein quality control in neurons. In addition, they expand the repertoire of pathways by which F-box proteins can regulate ubiquitination and suggest a new role for PEST domains as a protein interaction motif.
Details
- Title: Subtitle
- A Novel Route for F-box Protein-mediated Ubiquitination Links CHIP to Glycoprotein Quality Control
- Creators
- Rick F Nelson - Medical Scientist Training Program, University of Iowa Roy J. and Lucille A. Carver College of Medicine, Iowa City, Iowa 52242Kevin A Glenn - Department of Internal Medicine, University of Iowa Roy J. and Lucille A. Carver College of Medicine, Iowa City, Iowa 52242Victor M Miller - Graduate Program in Genetics, University of Iowa Roy J. and Lucille A. Carver College of Medicine, Iowa City, Iowa 52242Hsiang Wen - Department of Neurology, University of Iowa Roy J. and Lucille A. Carver College of Medicine, Iowa City, Iowa 52242Henry L Paulson - Medical Scientist Training Program, University of Iowa Roy J. and Lucille A. Carver College of Medicine, Iowa City, Iowa 52242
- Resource Type
- Journal article
- Publication Details
- The Journal of biological chemistry, Vol.281(29), pp.20242-20251
- DOI
- 10.1074/jbc.M602423200
- PMID
- 16682404
- NLM abbreviation
- J Biol Chem
- ISSN
- 0021-9258
- eISSN
- 1083-351X
- Publisher
- Elsevier Inc
- Language
- English
- Date published
- 07/21/2006
- Academic Unit
- Psychiatry; General Internal Medicine; Internal Medicine
- Record Identifier
- 9984094484602771
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