Correction: Chon-Kit Chou, et al. The Regulations of Deubiquitinase USP15 and Its Pathophysiological Mechanisms in Diseases. Int. J. Mol. Sci. 2017, 18, 483

Autor: Ya-Ting Yang, Steve Leu, Chon-Kit Chou, Chien-Chih Chiu, Yu-Ting Chang, Michal Korinek, I-Ling Lin, Chin-Ju Tang, Yei Tsung Chen
Rok vydání: 2017
Předmět:
0301 basic medicine
CHON
Intracellular Space
Gene Expression
Computational biology
Bioinformatics
Catalysis
Deubiquitinating enzyme
lcsh:Chemistry
Inorganic Chemistry
Structure-Activity Relationship
03 medical and health sciences
Animals
Humans
Medicine
Protein Interaction Domains and Motifs
Physical and Theoretical Chemistry
lcsh:QH301-705.5
Molecular Biology
Spectroscopy
biology
business.industry
Organic Chemistry
INT
Ubiquitination
Correction
Chromosome Mapping
General Medicine
Computer Science Applications
Isoenzymes
Protein Transport
n/a
Cell Transformation
Neoplastic
030104 developmental biology
lcsh:Biology (General)
lcsh:QD1-999
Gene Expression Regulation
Drug Resistance
Neoplasm
biology.protein
Disease Susceptibility
Ubiquitin-Specific Proteases
business
Protein Binding
Signal Transduction
Zdroj: International Journal of Molecular Sciences
International Journal of Molecular Sciences, Vol 18, Iss 5, p 902 (2017)
ISSN: 1422-0067
DOI: 10.3390/ijms18050902
Popis: Deubiquitinases (DUBs) play a critical role in ubiquitin-directed signaling by catalytically removing the ubiquitin from substrate proteins. Ubiquitin-specific protease 15 (USP15), a member of the largest subfamily of cysteine protease DUBs, contains two conservative cysteine (Cys) and histidine (His) boxes. USP15 harbors two zinc-binding motifs that are essential for recognition of poly-ubiquitin chains. USP15 is grouped into the same category with USP4 and USP11 due to high degree of homology in an N-terminal region consisting of domains present in ubiquitin-specific proteases (DUSP) domain and ubiquitin-like (UBL) domain. USP15 cooperates with COP9 signalosome complex (CSN) to maintain the stability of cullin-ring ligase (CRL) adaptor proteins by removing the conjugated ubiquitin chains from RBX1 subunit of CRL. USP15 is also implicated in the stabilization of the human papillomavirus type 16 E6 oncoprotein, adenomatous polyposis coli, and IκBα. Recently, reports have suggested that USP15 acts as a key regulator of TGF-β receptor-signaling pathways by deubiquitinating the TGF-β receptor itself and its downstream transducers receptor-regulated SMADs (R-SMADs), including SMAD1, SMAD2, and SMAD3, thus activating the TGF-β target genes. Although the importance of USP15 in pathologic processes remains ambiguous so far, in this review, we endeavor to summarize the literature regarding the relationship of the deubiquitinating action of USP15 with the proteins involved in the regulation of Parkinson's disease, virus infection, and cancer-related signaling networks.
Databáze: OpenAIRE
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