Human Molecular Genetics, Vol 5, 1311-1318, Copyright © 1996 by Oxford University Press
B Koshy, T Matilla, EN Burright, DE Merry, KH Fischbeck, HT Orr and HY Zoghbi
Spinocerebellar ataxia type1 (SCA1) is one of several neurodegenerative
disorders caused by expansions of translated CAG trinucleotide repeats
which code for polyglutamine in the respective proteins. Most hypotheses
about the molecular defect in these disorders suggest a gain of function,
which may involve interactions with other proteins via the expanded
polyglutamine tract. In this study we used ataxin-1, the SCA1 gene product,
as a bait in the yeast two-hybrid system and identified the glycolytic
enzyme glyceraldehyde-3-phosphate dehydrogenase as an ataxin-1 interacting
protein. In addition, the yeast two hybrid data demonstrate that wild type
and mutant ataxin-1 form homo and heterodimers. Physical interaction
between GAPDH and ataxin-1 was also demonstrated in vitro. To investigate
if GAPDH might interact with other glutamine repeat-containing proteins
involved in neurodegenerative disorders, we tested its binding to the
androgen receptor which is mutated in spinobulbar muscular atrophy. The
androgen receptor interacts with GAPDH both in the yeast two-hybrid system
and in vitro. The binding of both ataxin-1 and the androgen receptor to
GAPDH does not vary with the length of the polyglutamine tract. While
provocative, these findings do not address the selective neuronal loss in
each of these disorders in light of the wide expression patterns of GAPDH
and the respective polyglutamine containing proteins. Nonetheless, such
interactions may increase the susceptibility of specific neurons to a
variety of insults and initiate degeneration.
ARTICLES
Spinocerebellar ataxia type-1 and spinobulbar muscular atrophy gene products interact with glyceraldehyde-3-phosphate dehydrogenase
Department of Pediatrics, Baylor College of Medicine, Houston, Texas 77030, USA.
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