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

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

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.

Bibliographic Details
Main Authors: Seda Koyuncu, Isabel Saez, Hyun Ju Lee, Ricardo Gutierrez-Garcia, Wojciech Pokrzywa, Azra Fatima, Thorsten Hoppe, David Vilchez
Format: Article
Language:English
Published: Nature Publishing Group 2018-07-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-018-05320-3
id doaj-3208ae5c34064dfaa117ff00fd735b20
record_format Article
spelling doaj-3208ae5c34064dfaa117ff00fd735b202021-05-11T09:37:48ZengNature Publishing GroupNature Communications2041-17232018-07-019112210.1038/s41467-018-05320-3The ubiquitin ligase UBR5 suppresses proteostasis collapse in pluripotent stem cells from Huntington’s disease patientsSeda Koyuncu0Isabel Saez1Hyun Ju Lee2Ricardo Gutierrez-Garcia3Wojciech Pokrzywa4Azra Fatima5Thorsten Hoppe6David Vilchez7Institute for Genetics and Cologne Excellence Cluster for Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of CologneInstitute for Genetics and Cologne Excellence Cluster for Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of CologneInstitute for Genetics and Cologne Excellence Cluster for Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of CologneInstitute for Genetics and Cologne Excellence Cluster for Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of CologneInstitute for Genetics and Cologne Excellence Cluster for Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of CologneInstitute for Genetics and Cologne Excellence Cluster for Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of CologneInstitute for Genetics and Cologne Excellence Cluster for Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of CologneInstitute for Genetics and Cologne Excellence Cluster for Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of CologneInduced 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.https://doi.org/10.1038/s41467-018-05320-3
collection DOAJ
language English
format Article
sources DOAJ
author Seda Koyuncu
Isabel Saez
Hyun Ju Lee
Ricardo Gutierrez-Garcia
Wojciech Pokrzywa
Azra Fatima
Thorsten Hoppe
David Vilchez
spellingShingle Seda Koyuncu
Isabel Saez
Hyun Ju Lee
Ricardo Gutierrez-Garcia
Wojciech Pokrzywa
Azra Fatima
Thorsten Hoppe
David Vilchez
The ubiquitin ligase UBR5 suppresses proteostasis collapse in pluripotent stem cells from Huntington’s disease patients
Nature Communications
author_facet Seda Koyuncu
Isabel Saez
Hyun Ju Lee
Ricardo Gutierrez-Garcia
Wojciech Pokrzywa
Azra Fatima
Thorsten Hoppe
David Vilchez
author_sort Seda Koyuncu
title The ubiquitin ligase UBR5 suppresses proteostasis collapse in pluripotent stem cells from Huntington’s disease patients
title_short The ubiquitin ligase UBR5 suppresses proteostasis collapse in pluripotent stem cells from Huntington’s disease patients
title_full The ubiquitin ligase UBR5 suppresses proteostasis collapse in pluripotent stem cells from Huntington’s disease patients
title_fullStr The ubiquitin ligase UBR5 suppresses proteostasis collapse in pluripotent stem cells from Huntington’s disease patients
title_full_unstemmed The ubiquitin ligase UBR5 suppresses proteostasis collapse in pluripotent stem cells from Huntington’s disease patients
title_sort ubiquitin ligase ubr5 suppresses proteostasis collapse in pluripotent stem cells from huntington’s disease patients
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2018-07-01
description 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.
url https://doi.org/10.1038/s41467-018-05320-3
work_keys_str_mv AT sedakoyuncu theubiquitinligaseubr5suppressesproteostasiscollapseinpluripotentstemcellsfromhuntingtonsdiseasepatients
AT isabelsaez theubiquitinligaseubr5suppressesproteostasiscollapseinpluripotentstemcellsfromhuntingtonsdiseasepatients
AT hyunjulee theubiquitinligaseubr5suppressesproteostasiscollapseinpluripotentstemcellsfromhuntingtonsdiseasepatients
AT ricardogutierrezgarcia theubiquitinligaseubr5suppressesproteostasiscollapseinpluripotentstemcellsfromhuntingtonsdiseasepatients
AT wojciechpokrzywa theubiquitinligaseubr5suppressesproteostasiscollapseinpluripotentstemcellsfromhuntingtonsdiseasepatients
AT azrafatima theubiquitinligaseubr5suppressesproteostasiscollapseinpluripotentstemcellsfromhuntingtonsdiseasepatients
AT thorstenhoppe theubiquitinligaseubr5suppressesproteostasiscollapseinpluripotentstemcellsfromhuntingtonsdiseasepatients
AT davidvilchez theubiquitinligaseubr5suppressesproteostasiscollapseinpluripotentstemcellsfromhuntingtonsdiseasepatients
AT sedakoyuncu ubiquitinligaseubr5suppressesproteostasiscollapseinpluripotentstemcellsfromhuntingtonsdiseasepatients
AT isabelsaez ubiquitinligaseubr5suppressesproteostasiscollapseinpluripotentstemcellsfromhuntingtonsdiseasepatients
AT hyunjulee ubiquitinligaseubr5suppressesproteostasiscollapseinpluripotentstemcellsfromhuntingtonsdiseasepatients
AT ricardogutierrezgarcia ubiquitinligaseubr5suppressesproteostasiscollapseinpluripotentstemcellsfromhuntingtonsdiseasepatients
AT wojciechpokrzywa ubiquitinligaseubr5suppressesproteostasiscollapseinpluripotentstemcellsfromhuntingtonsdiseasepatients
AT azrafatima ubiquitinligaseubr5suppressesproteostasiscollapseinpluripotentstemcellsfromhuntingtonsdiseasepatients
AT thorstenhoppe ubiquitinligaseubr5suppressesproteostasiscollapseinpluripotentstemcellsfromhuntingtonsdiseasepatients
AT davidvilchez ubiquitinligaseubr5suppressesproteostasiscollapseinpluripotentstemcellsfromhuntingtonsdiseasepatients
_version_ 1721449503640256512

Similar Items