Huntingtin-protein interactions and the pathogenesis of Huntington's disease.

Abstract

At least nine inherited neurodegenerative diseases share a polyglutamine expansion in their respective disease proteins. These diseases show distinct neuropathological changes, suggesting that protein environment and protein-protein interactions play an important role in the specific neuropathology. A gain of toxic function as a result of an expanded polyglutamine tract can cause the protein huntingtin to interact abnormally with a variety of proteins, resulting in the complex of neuropathological changes seen in Huntington's disease. Recent studies have identified several huntingtin-interacting proteins that might be associated with the normal function of huntingtin and/or involved in the pathology of Huntington's disease. In this article, we focus on the potential roles of huntingtin-protein interactions in the pathogenesis of Huntington's disease.

• Authors: Shi-Hua Li, Xiao-Jiang Li
• Journal: Trends in genetics : TIG (Trends Genet) Vol. 20 Issue 3 Pg. 146-54 (Mar 2004) ISSN: 0168-9525 [Print] England
• PMID: 15036808 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S., Review)

Chemical References

• HTT protein, human
• Huntingtin Protein
• Nerve Tissue Proteins
• Nuclear Proteins
• Peptides
• Transcription Factors
• polyglutamine

Topics

• Humans
• Huntingtin Protein
• Huntington Disease (etiology, metabolism, pathology)
• Nerve Tissue Proteins (genetics, metabolism)
• Nuclear Proteins (genetics, metabolism)
• Peptides
• Protein Binding
• Transcription Factors (genetics, metabolism)
• Trinucleotide Repeats