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- Title
USP19-Mediated Deubiquitination Facilitates the Stabilization of HRD1 Ubiquitin Ligase.
- Authors
Kumi Harada; Masako Kato; Nobuhiro Nakamura
- Abstract
In the endoplasmic reticulum (ER), misfolded and unfolded proteins are eliminated by a process called ER-associated protein degradation (ERAD) in order to maintain cell homeostasis. In the ERAD pathway, several ER-localized E3 ubiquitin ligases target ERAD substrate proteins for ubiquitination and subsequent proteasomal degradation. However, little is known about how the functions of the ERAD ubiquitin ligases are regulated. Recently, USP19, an ER-anchored deubiquitinating enzyme (DUB), has been suggested to be involved in the regulation of ERAD. In this study, HRD1, an ERAD ubiquitin ligase, is shown to be a novel substrate for USP19. We demonstrate that USP19 rescues HRD1 from proteasomal degradation by deubiquitination of K48-linked ubiquitin chains. In addition, the altered expression of USP19 affects the steady-state levels of HRD1. These results suggest that USP19 regulates the stability of HRD1 and provide insight into the regulatory mechanism of the ERAD ubiquitin ligases.
- Subjects
ENDOPLASMIC reticulum; UBIQUITINATION; POST-translational modification; UBIQUITIN ligases; PHYSIOLOGY
- Publication
International Journal of Molecular Sciences, 2016, Vol 17, Issue 11, p1829
- ISSN
1661-6596
- Publication type
Article
- DOI
10.3390/ijms17111829