TorsinA participates in endoplasmic reticulum-associated degradation

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TorsinA participates in endoplasmic reticulum-associated degradation

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Title: TorsinA participates in endoplasmic reticulum-associated degradation
Author: Nery, Flávia C.; Armata, Ioanna A.; Farley, Jonathan E.; Cho, JinAh; Yaqub, Uzma; Chen, Pan; da Hora, Cintia Carla; Wang, Qiuyan; Tagaya, Mitsuo; Klein, Christine; Tannous, Bakhos A.; Caldwell, Kim A.; Caldwell, Guy A.; Lencer, Wayne I.; Ye, Yihong; Breakefield, Xandra Owens

Note: Order does not necessarily reflect citation order of authors.

Citation: Nery, Flávia C., Ioanna A. Armata, Jonathan E. Farley, JinAh Cho, Uzma Yaqub, Pan Chen, Cintia Carla da Hora, et al. 2012. TorsinA participates in endoplasmic reticulum-associated degradation. Nature Communications 2(7): 393.
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Abstract: TorsinA is an \(AAA^+\) ATPase located within the lumen of the endoplasmic reticulum and nuclear envelope, with a mutant form causing early onset torsion dystonia (DYT1). Here we report a new function for torsinA in endoplasmic reticulum-associated degradation (ERAD). Retro-translocation and proteosomal degradation of a mutant cystic fibrosis transmembrane conductance regulator \((CFTR\Delta F508)\) was inhibited by downregulation of torsinA or overexpression of mutant torsinA, and facilitated by increased torsinA. Retro-translocation of cholera toxin was also decreased by downregulation of torsinA. TorsinA associates with proteins implicated in ERAD, including Derlin-1, VIMP, and p97. Further, torsinA reduces endoplasmic reticulum stress in nematodes overexpressing \(CFTR\Delta F508\), and fibroblasts from DYT1 dystonia patients are more sensitive than controls to endoplasmic reticulum stress and less able to degrade mutant CFTR. Therefore, compromised ERAD function in the cells of DYT1 patients may increase sensitivity to endoplasmic reticulum stress with consequent alterations in neuronal function contributing to the disease state.
Published Version: doi:10.1038/ncomms1383
Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3529909/pdf/
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:10578990
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