The ubiquitin ligase UBR5 suppresses proteostasis collapse in pluripotent stem cells from Huntington’s disease patients

Seda Koyuncu; Isabel Saez; Hyun Ju Lee; Ricardo Gutierrez-Garcia; Wojciech Pokrzywa; Azra Fatima; Thorsten Hoppe; David Vilchez

doi:10.1038/s41467-018-05320-3

Nature Communications (Jul 2018)

The ubiquitin ligase UBR5 suppresses proteostasis collapse in pluripotent stem cells from Huntington’s disease patients

Seda Koyuncu,
Isabel Saez,
Hyun Ju Lee,
Ricardo Gutierrez-Garcia,
Wojciech Pokrzywa,
Azra Fatima,
Thorsten Hoppe,
David Vilchez

Affiliations

Seda Koyuncu: Institute for Genetics and Cologne Excellence Cluster for Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne
Isabel Saez: Institute for Genetics and Cologne Excellence Cluster for Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne
Hyun Ju Lee: Institute for Genetics and Cologne Excellence Cluster for Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne
Ricardo Gutierrez-Garcia: Institute for Genetics and Cologne Excellence Cluster for Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne
Wojciech Pokrzywa: Institute for Genetics and Cologne Excellence Cluster for Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne
Azra Fatima: Institute for Genetics and Cologne Excellence Cluster for Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne
Thorsten Hoppe: Institute for Genetics and Cologne Excellence Cluster for Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne
David Vilchez: Institute for Genetics and Cologne Excellence Cluster for Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne

DOI: https://doi.org/10.1038/s41467-018-05320-3
Journal volume & issue: Vol. 9, no. 1
pp. 1 – 22

Abstract

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Induced pluripotent stem cells (iPSCs) suppress the aggregation of Huntington’s disease (HD) polyQ-expanded huntingtin (HTT). Here the authors show that proteasome activity determines the levels of mutant HTT in HD-iPSCs and find that UBR5 is a modulator of super-vigilant proteostasis of iPSCs.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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