Cited 7 time in webofscience Cited 7 time in scopus

Deubiquitination Reactions on the Proteasome for Proteasome Versatility

Title
Deubiquitination Reactions on the Proteasome for Proteasome Versatility
Authors
Shin, Ji YeongMuniyappan, SrinivasanTran, Non-NuocPark, HyeonjeongLee, Sung BaeLee, Byung-Hoon
DGIST Authors
Shin, Ji Yeong; Muniyappan, Srinivasan; Tran, Non-Nuoc; Park, Hyeonjeong; Lee, Sung BaeLee, Byung-Hoon
Issue Date
2020-07
Citation
International Journal of Molecular Sciences, 21(15), 5312
Type
Article
Article Type
Review
Author Keywords
USP14UCH37RPN11proteasomeproteolysisubiquitindeubiquitinationdeubiquitinating enzyme
Keywords
UBIQUITINATED PROTEINS ACTIVATEENZYME USP14CONFORMATIONAL LANDSCAPESUBSTRATE DEGRADATIONREVEALS MECHANISMSPROVIDES INSIGHTSSTRUCTURAL BASISRECEPTOR HRPN13ATAXIA MICEUCH37
ISSN
1422-0067
Abstract
The 26S proteasome, a master player in proteolysis, is the most complex and meticulously contextured protease in eukaryotic cells. While capable of hosting thousands of discrete substrates due to the selective recognition of ubiquitin tags, this protease complex is also dynamically checked through diverse regulatory mechanisms. The proteasome’s versatility ensures precise control over active proteolysis, yet prevents runaway or futile degradation of many essential cellular proteins. Among the multi-layered processes regulating the proteasome’s proteolysis, deubiquitination reactions are prominent because they not only recycle ubiquitins, but also impose a critical checkpoint for substrate degradation on the proteasome. Of note, three distinct classes of deubiquitinating enzymes—USP14, RPN11, and UCH37—are associated with the 19S subunits of the human proteasome. Recent biochemical and structural studies suggest that these enzymes exert dynamic influence over proteasome output with limited redundancy, and at times act in opposition. Such distinct activities occur spatially on the proteasome, temporally through substrate processing, and differentially for ubiquitin topology. Therefore, deubiquitinating enzymes on the proteasome may fine-tune the degradation depending on various cellular contexts and for dynamic proteolysis outcomes. Given that the proteasome is among the most important drug targets, the biology of proteasome-associated deubiquitination should be further elucidated for its potential targeting in human diseases. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.
URI
http://hdl.handle.net/20.500.11750/12443
DOI
10.3390/ijms21155312
Publisher
MDPI AG
Related Researcher
  • Author Lee, Sung Bae Laboratory of Neurodegenerative Diseases and Aging
  • Research Interests Cellular mechanism of neurodegenerative diseases; Neuronal maintenance and remodeling; 퇴행성 뇌질환의 세포기전; 신경계 유지 및 리모델링 연구
Files:
Collection:
Department of Brain and Cognitive SciencesLaboratory of Neurodegenerative Diseases and Aging1. Journal Articles
Department of New BiologyLab of Protein Homeostasis and Drug Discovery1. Journal Articles


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