Biosynthesis of the dystonia-associated AAA+ ATPase torsinA at the endoplasmic reticulum
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...
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Published in | Biochemical journal Vol. 401; no. 2; pp. 607 - 612 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
England
Portland Press
15.01.2007
Portland Press Ltd |
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Abstract | 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 reticulum) lumen. However, in the present study we show that torsinA is not in fact an integral membrane protein. Instead we find that the mature protein associates peripherally with the ER membrane, most likely through an interaction with an integral membrane protein. Consistent with this model, we provide evidence that the signal peptidase complex cleaves the signal sequence of torsinA, and we show that the region previously suggested to form a transmembrane domain is translocated into the lumen of the ER. The finding that torsinA is a peripheral, and not an integral membrane protein as previously thought, has important implications for understanding the function of this novel ATPase. |
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AbstractList | TorsinA is a widely expressed AAA +} 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 endoplasmic reticulum (ER) lumen. However, we now show that torsinA is not in fact an integral membrane protein. Instead we find that the mature protein associates peripherally with the ER membrane, most likely through an interaction with an integral membrane protein. Consistent with this model, we provide evidence that the signal peptidase complex cleaves the signal sequence of torsinA, and show that the region previously suggested to form a transmembrane domain is translocated into the lumen of the ER. The finding that torsinA is a peripheral, and not an integral membrane protein as previously thought, has important implications for understanding the function of this novel ATPase. 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 reticulum) lumen. However, in the present study we show that torsinA is not in fact an integral membrane protein. Instead we find that the mature protein associates peripherally with the ER membrane, most likely through an interaction with an integral membrane protein. Consistent with this model, we provide evidence that the signal peptidase complex cleaves the signal sequence of torsinA, and we show that the region previously suggested to form a transmembrane domain is translocated into the lumen of the ER. The finding that torsinA is a peripheral, and not an integral membrane protein as previously thought, has important implications for understanding the function of this novel ATPase. 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 reticulum) lumen. However, in the present study we show that torsinA is not in fact an integral membrane protein. Instead we find that the mature protein associates peripherally with the ER membrane, most likely through an interaction with an integral membrane protein. Consistent with this model, we provide evidence that the signal peptidase complex cleaves the signal sequence of torsinA, and we show that the region previously suggested to form a transmembrane domain is translocated into the lumen of the ER. The finding that torsinA is a peripheral, and not an integral membrane protein as previously thought, has important implications for understanding the function of this novel ATPase. |
Author | Jones, Owen T Bunning, Sandra Callan, Anna C High, Stephen Swanton, Eileithyia |
Author_xml | – sequence: 1 givenname: Anna C surname: Callan fullname: Callan, Anna C organization: Faculty of Life Sciences, University of Manchester, The Michael Smith Building, Oxford Road, Manchester M13 9PT, UK – sequence: 2 givenname: Sandra surname: Bunning fullname: Bunning, Sandra – sequence: 3 givenname: Owen T surname: Jones fullname: Jones, Owen T – sequence: 4 givenname: Stephen surname: High fullname: High, Stephen – sequence: 5 givenname: Eileithyia surname: Swanton fullname: Swanton, Eileithyia |
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Snippet | TorsinA is a widely expressed AAA(+) (ATPases associated with various cellular activities) ATPase of unknown function. Previous studies have described torsinA... TorsinA is a widely expressed AAA+ (ATPases associated with various cellular activities) ATPase of unknown function. Previous studies have described torsinA as... TorsinA is a widely expressed AAA +} ATPase of unknown function. Previous studies have described torsinA as a type II protein with a cleavable signal sequence,... TorsinA is a widely expressed AAA + (ATPases associated with various cellular activities) ATPase of unknown function. Previous studies have described torsinA... |
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SubjectTerms | 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 |
Title | Biosynthesis of the dystonia-associated AAA+ ATPase torsinA at the endoplasmic reticulum |
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