Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH

James R. Burke; Jan J. Enghild; Margaret E. Martin; Yuh Shan Jou; Richard M. Myers; Allen D. Roses; Jeffery M. Vance; Warren J. Strittmatter

doi:10.1038/nm0396-347

Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH

James R. Burke, Jan J. Enghild, Margaret E. Martin, Yuh Shan Jou, Richard M. Myers, Allen D. Roses, Jeffery M. Vance, Warren J. Strittmatter

Hussman Institute for Human Genomics

Research output: Contribution to journal › Article

384 Scopus citations

Abstract

At least five adult-onset neurodegenerative diseases, including Huntington disease (HD), and dentatorubral-pallidoluysian atrophy (DRPLA) are produced by genes containing a variably increased CAG repeat within the coding region ^1-4. The size range of the repeats is similar in all diseases; unaffected individuals have fewer than 30 CAG repeats, whereas affected patients usually have more than 40 repeats. The size of the inherited CAG repeat correlates with the severity and age of disease onset^1,5-7. The CAG triplet repeat produces a polyglutamine domain in the expressed proteins^3,8-10. All of these diseases are inherited in a dominant fashion, and a pathologic gain of function in gene carriers has been proposed. We sought to identify proteins in the brain that selectively interact with polyglutamine-domain proteins, hypothesizing that the polyglutamine domain may determine protein-protein interactions.

Original language	English (US)
Pages (from-to)	347-350
Number of pages	4
Journal	Nature medicine
Volume	2
Issue number	3
DOIs	https://doi.org/10.1038/nm0396-347
State	Published - 1996

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)

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Burke, J. R., Enghild, J. J., Martin, M. E., Jou, Y. S., Myers, R. M., Roses, A. D., Vance, J. M., & Strittmatter, W. J. (1996). Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH. Nature medicine, 2(3), 347-350. https://doi.org/10.1038/nm0396-347

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abstract = "At least five adult-onset neurodegenerative diseases, including Huntington disease (HD), and dentatorubral-pallidoluysian atrophy (DRPLA) are produced by genes containing a variably increased CAG repeat within the coding region 1-4. The size range of the repeats is similar in all diseases; unaffected individuals have fewer than 30 CAG repeats, whereas affected patients usually have more than 40 repeats. The size of the inherited CAG repeat correlates with the severity and age of disease onset1,5-7. The CAG triplet repeat produces a polyglutamine domain in the expressed proteins3,8-10. All of these diseases are inherited in a dominant fashion, and a pathologic gain of function in gene carriers has been proposed. We sought to identify proteins in the brain that selectively interact with polyglutamine-domain proteins, hypothesizing that the polyglutamine domain may determine protein-protein interactions.",

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