Huntingtin is ubiquitinated and interacts with a specific ubiquitin-conjugating enzyme - PubMed (original) (raw)
. 1996 Aug 9;271(32):19385-94.
doi: 10.1074/jbc.271.32.19385.
Affiliations
- PMID: 8702625
- DOI: 10.1074/jbc.271.32.19385
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Huntingtin is ubiquitinated and interacts with a specific ubiquitin-conjugating enzyme
M A Kalchman et al. J Biol Chem. 1996.
Free article
Abstract
Using the yeast two-hybrid system, we have identified a human ubiquitin-conjugating enzyme (hE2-25K) as a protein that interacts with the gene product for Huntington disease (HD) (Huntingtin). This protein has complete amino acid identity with the bovine E2-25K protein and has striking similarity to the UBC-1, -4 and -5 enzymes of Saccharomyces cerevisiae. This protein is highly expressed in brain and a slightly larger protein recognized by an anti-E2-25K polyclonal antibody is selectively expressed in brain regions affected in HD. The huntingtin-E2-25K interaction is not obviously modulated by CAG length. We also demonstrate that huntingtin is ubiquitinated. These findings have implications for the regulated catabolism of the gene product for HD.
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