Human Molecular Genetics, Vol 7, 1463-1474, Copyright © 1998 by Oxford University Press
PW Faber, GT Barnes, J Srinidhi, J Chen, JF Gusella and ME MacDonald
The hallmark neuropathology of Huntington's disease (HD) is due to
elongation of a polyglutamine segment in huntingtin, a novel approximately
350 kDa protein of unknown function. We used a yeast two- hybrid interactor
screen to identify proteins whose association with huntingtin might be
altered in the pathogenic process. Surprisingly, no interactors were found
with internal and C-terminal segments of huntingtin. In contrast,
huntingtin's N-terminus detected 13 distinct proteins, seven novel and six
reported previously. Among these, we identified a major interactor class,
comprising three distinct WW domain proteins, HYPA, HYPB and HYPC, that
bind normal and mutant huntingtin in extracts of HD lymphoblastoid cells.
This interaction is mediated by huntingtin's proline-rich region and is
enhanced by lengthening the adjacent glutamine tract. Although HYPB and
HYPC are novel, HYPA is human FBP-11, a protein implicated in spliceosome
function. The emergence of this class of proteins as huntingtin partners
argues that a WW domain-mediated process, such as non-receptor signaling,
protein degradation or pre-mRNA splicing, may participate in HD
pathogenesis.
ARTICLES
Huntingtin interacts with a family of WW domain proteins
Molecular Neurogenetics Unit, Massachusetts General Hospital East, Building 149, 13th Street, Charlestown, MA 02129, USA.
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