Biosynthesis of the dystonia-associated AAA+ ATPase torsinA at the endoplasmic reticulum

• Published in: Biochemical journal Vol. 401; no. 2; pp. 607 - 612
• Main Authors: Callan, Anna C, Bunning, Sandra, Jones, Owen T, High, Stephen, Swanton, Eileithyia
• Format: Journal Article
• Language: English
• Published: England Portland Press 15.01.2007; Portland Press Ltd
• Subjects: Adenosine Triphosphatases - biosynthesis; Amino Acid Sequence; Cell-Free System; Endoplasmic Reticulum - metabolism; HeLa Cells; Humans; Membrane Proteins - metabolism; Molecular Chaperones - biosynthesis; Protein Transport; Serine Endopeptidases - metabolism; Life Sciences

TorsinA is a widely expressed AAA(+) (ATPases associated with various cellular activities) ATPase of unknown function. Previous studies have described torsinA as a type II protein with a cleavable signal sequence, a single membrane spanning domain, and its C-terminus located in the ER (endoplasmic r...