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TorsinB – perinuclear location and association with torsinA
Author(s) -
Hewett Jeffrey W.,
Kamm Christoph,
Boston Heather,
Beauchamp Roberta,
Naismith Teri,
Ozelius Laurie,
Hanson Phyllis I.,
Breakefield Xandra O.,
Ramesh Vijaya
Publication year - 2004
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2004.02404.x
Subject(s) - endoplasmic reticulum , biology , microbiology and biotechnology , immunoprecipitation , chaperone (clinical) , cytoplasm , mutant , nuclear protein , calnexin , gene , genetics , transcription factor , pathology , medicine , calreticulin
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 (∼ MW 38 kDa), like torsinA (∼ 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 .