Ma. Kalchman et al., HUNTINGTIN IS UBIQUITINATED AND INTERACTS WITH A SPECIFIC UBIQUITIN-CONJUGATING ENZYME, The Journal of biological chemistry, 271(32), 1996, pp. 19385-19394
Using the yeast two-hybrid system, we have identified a human ubiquiti
n-conjugating enzyme (hE2-25K) as a protein that interacts with the ge
ne product for Huntington disease (HD) (Huntingtin). This protein has
complete amino acid identity with the bovine E2-25K protein and has st
riking similarity to the UBC-1, -4 and -5 enzymes of Saccharomyces cer
evisiae. This protein is highly expressed in brain and a slightly larg
er protein recognized by an anti-E2-25K polyclonal antibody is selecti
vely expressed in brain regions affected in HD. The huntingtin-E2-25K
interaction is not obviously modulated by CAG length. We also demonstr
ate that huntingtin is ubiquitinated. These findings have implications
for the regulated catabolism of the gene product for HD.