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

doi:10.1074/jbc.M113.529123

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 journal › Article › peer-review

20 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 language	English (US)
Pages (from-to)	12727-12747
Number of pages	21
Journal	Journal of Biological Chemistry
Volume	289
Issue number	18
DOIs	https://doi.org/10.1074/jbc.M113.529123
State	Published - 2014

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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Zacchi, L. F., Wu, H. C., Bell, S. L., Millen, L., Paton, A. W., Paton, J. C., Thomas, P. J., Zolkiewski, M., & Brodsky, J. L. (2014). The bip molecular chaperone plays multiple roles during the biogenesis of torsina, an aaa atpase associated with the neurological disease early-onset torsion dystonia. Journal of Biological Chemistry, 289(18), 12727-12747. https://doi.org/10.1074/jbc.M113.529123

The bip molecular chaperone plays multiple roles during the biogenesis of torsina, an aaa atpase associated with the neurological disease early-onset torsion dystonia. / Zacchi, Lucía F.; Wu, Hui Chuan; Bell, Samantha L. et al.
In: Journal of Biological Chemistry, Vol. 289, No. 18, 2014, p. 12727-12747.

Research output: Contribution to journal › Article › peer-review

Zacchi, LF, Wu, HC, Bell, SL, Millen, L, Paton, AW, Paton, JC, Thomas, PJ, Zolkiewski, M & Brodsky, JL 2014, 'The bip molecular chaperone plays multiple roles during the biogenesis of torsina, an aaa atpase associated with the neurological disease early-onset torsion dystonia', Journal of Biological Chemistry, vol. 289, no. 18, pp. 12727-12747. https://doi.org/10.1074/jbc.M113.529123

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

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.",

author = "Zacchi, {Luc{\'i}a F.} and Wu, {Hui Chuan} and Bell, {Samantha L.} and Linda Millen and Paton, {Adrienne W.} and Paton, {James C.} and Thomas, {Philip J.} and Michal Zolkiewski and Brodsky, {Jeffrey L.}",

year = "2014",

doi = "10.1074/jbc.M113.529123",

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AU - Zacchi, Lucía F.

AU - Wu, Hui Chuan

AU - Bell, Samantha L.

AU - Millen, Linda

AU - Paton, Adrienne W.

AU - Paton, James C.

AU - Thomas, Philip J.

AU - Zolkiewski, Michal

AU - Brodsky, Jeffrey L.

PY - 2014

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AB - 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.

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

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