Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 493, Issue 1, Pages 708-717Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2017.08.126
Keywords
PolyQ protein; Huntington's disease; RQC; Nucleocytoplasmic translocation
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Funding
- Swedish Cancer Society [CAN 2012/601, CAN 2015/406]
- Swedish Natural Research Council [VR 2011-5923, VR 2015-04984]
- Carl Trygger Foundation [CTS 14: 295]
- Fund for Scientific Research Flanders (FWO-Vlaanderen), an FWO [G0A6315, G069413]
- China Scholarship Council
- European Union [608743]
- Munich Cluster for Systems Neurology (SyNergy)
- Swedish Research Council [2015-04984] Funding Source: Swedish Research Council
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The subcellular localization of polyQ-expanded huntingtin exon1 (Httex1) modulates polyQ toxicity in models of Huntington's disease. Using genome-wide screens in a yeast model system, we report that the ribosome quality control (RQC) machinery, recently implicated in neurodegeneration, is a key determinant for the nucleocytoplasmic distribution of Httex1-103Q, Deletion of the RQC genes, LTN1 or RQC1, caused the accumulation of Httex1-103Q in the nucleus through a process that required the CAT-tail tagging activity of Rqc2 and transport via the nuclear pore complex. We provide evidence that nuclear accumulation of Httex1-103Q enhances its cytotoxicity, suggesting that the RQC machinery plays an important role in protecting cells against the adverse effects of polyQ expansion proteins. (C) 2017 The Authors. Published by Elsevier Inc.
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