rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
32
|
pubmed:dateCreated |
1996-9-16
|
pubmed:databankReference |
|
pubmed:abstractText |
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.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
0021-9258
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
9
|
pubmed:volume |
271
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
19385-94
|
pubmed:dateRevised |
2008-9-13
|
pubmed:meshHeading |
pubmed-meshheading:8702625-Amino Acid Sequence,
pubmed-meshheading:8702625-Animals,
pubmed-meshheading:8702625-Base Sequence,
pubmed-meshheading:8702625-Brain,
pubmed-meshheading:8702625-Cattle,
pubmed-meshheading:8702625-Chromosome Mapping,
pubmed-meshheading:8702625-Chromosomes, Human, Pair 4,
pubmed-meshheading:8702625-DNA, Complementary,
pubmed-meshheading:8702625-Humans,
pubmed-meshheading:8702625-Ligases,
pubmed-meshheading:8702625-Molecular Sequence Data,
pubmed-meshheading:8702625-Nerve Tissue Proteins,
pubmed-meshheading:8702625-Nuclear Proteins,
pubmed-meshheading:8702625-Saccharomyces cerevisiae,
pubmed-meshheading:8702625-Ubiquitin-Conjugating Enzymes,
pubmed-meshheading:8702625-Ubiquitins
|
pubmed:year |
1996
|
pubmed:articleTitle |
Huntingtin is ubiquitinated and interacts with a specific ubiquitin-conjugating enzyme.
|
pubmed:affiliation |
Department of Medical Genetics, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z4.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|