The bip molecular chaperone plays multiple roles during the biogenesis of torsina, an aaa atpase associated with the neurological disease early-onset torsion dystonia

Lucía F. Zacchi, Hui Chuan Wu, Samantha L. Bell, Linda Millen, Adrienne W. Paton, James C. Paton, Philip J. Thomas, Michal Zolkiewski, Jeffrey L. Brodsky

Research output: Contribution to journalArticle

14 Scopus citations

Abstract

Background: The E mutation in the AAA ATPase torsinA is associated with the neurological disease torsion dystonia. Results: BiP and its co-factors maintain torsinA and torsinAE stability, glycosylation, and solubility. Conclusion: torsinA/E, a chaperone-like protein, requires the assistance of other chaperones to fold. Significance: Therapeutics that modulate BiP may counteract torsinAE-associated physiological defects.

Original languageEnglish (US)
Pages (from-to)12727-12747
Number of pages21
JournalJournal of Biological Chemistry
Volume289
Issue number18
DOIs
StatePublished - Jan 1 2014

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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