Biochemical characterization of torsinB

Casey O'Farrell, Paul J. Lockhart, Sarah Lincoln, Michael De Lucia, Andrew B. Singleton, Dennis W. Dickson, Mark R. Cookson

Research output: Contribution to journalArticlepeer-review

10 Scopus citations


Mutations in torsinA, a member of the AAA+ family of ATPases, are associated with early onset-dystonia. A closely related homologue, torsinB, has also been described but the significance of this second form is not clear. Here, we demonstrate that in transfected cells, torsinB has similar electrophoretic mobility to torsinA but is more basic consistent with predictions from the cDNA sequence. Like torsinA, torsinB is glycosylated and localized to PDI-positive structures in cells. However, torsinB unlike torsinA has a tendency to form intracellular inclusions when expressed at similar levels. We were able to confirm previous reports that torsinA is present in brainstem Lewy bodies, but we saw no torsinB-like immunoreactivity in the same structures. These results show that torsins A and B are similar proteins, although there are differences in the abundance of the two homologues and in their recruitment into Lewy bodies.

Original languageEnglish (US)
Pages (from-to)1-9
Number of pages9
JournalMolecular Brain Research
Issue number1-2
StatePublished - Aug 23 2004


  • DYT1
  • Disorders of the nervous system
  • Dystonia
  • Genetic models
  • Glycosylation
  • Lewy bodies
  • Torsin

ASJC Scopus subject areas

  • Molecular Biology
  • Cellular and Molecular Neuroscience


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