Journal
JOURNAL OF NEUROCHEMISTRY
Volume 89, Issue 5, Pages 1186-1194Publisher
WILEY
DOI: 10.1111/j.1471-4159.2004.02404.x
Keywords
AAA(+); chaperone; dystonia; endoplasmic reticulum; nuclear envelope; torsinA; torsinB
Categories
Funding
- NINDS NIH HHS [NS 37409, NS 28384] Funding Source: Medline
Ask authors/readers for more resources
The torsins comprise a four-member family of AAA(+) chaperone proteins, including torsinA, torsinB, torp2A and torp3A in humans. Mutations in torsinA underlie early onset torsion dystonia, an autosomal dominant, neurologically based movement disorder. TorsinB is highly homologous to torsinA with its gene adjacent to that for torsinA on human chromosome 9q34. Antibodies have been generated which can distinguish torsinA and torsinB from each other, and from the torps in human and rodent cells. TorsinB (similar to MW 38 kDa), like torsinA (similar to MW 37 kDa), is an N-glycosylated protein and both reside primarily in the endoplasmic reticulum (ER) and nuclear envelope in cultured cells. Immunoprecipitation studies in cultured cells and human brain tissue indicate that torsinA and torsinB are associated with each other in cells. Overexpression of both wild-type torsinB and mutant torsinA lead to enrichment of the protein in the nuclear envelope and formation of large cytoplasmic inclusions. We conclude that torsinB and torsinA are localized in overlapping cell compartments within the same protein complex, and thus may carry out related functions in vivo.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available