The ubiquitin-specific protease 8 gene is frequently mutated in adenomas causing Cushing's disease

2015 ◽  
Author(s):  
Luis Gustavo Perez Rivas ◽  
Marily Theodoropoulou ◽  
Francesco Ferrau ◽  
Clara Nusser ◽  
Kohei Kawaguchi ◽  
...  
Keyword(s):  
Cushing’S Disease ◽  
Cushing's Disease ◽  
Specific Protease ◽  
Ubiquitin Specific Protease

scholarly journals The Gene of the Ubiquitin-Specific Protease 8 Is Frequently Mutated in Adenomas Causing Cushing's Disease

2015 ◽  
Vol 100 (7) ◽  
pp. E997-E1004 ◽  
Author(s):  
Luis G. Perez-Rivas ◽  
Marily Theodoropoulou ◽  
Francesco Ferraù ◽  
Clara Nusser ◽  
Kohei Kawaguchi ◽  
...  
Keyword(s):  
Cushing’S Disease ◽  
Cushing's Disease ◽  
Specific Protease ◽  
Ubiquitin Specific Protease

scholarly journals Molecular basis of ubiquitin-specific protease 8 autoinhibition by the WW-like domain

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Keijun Kakihara ◽  
Kengo Asamizu ◽  
Kei Moritsugu ◽  
Masahide Kubo ◽  
Tetsuya Kitaguchi ◽  
...  
Keyword(s):  
Single Molecule ◽  
Membrane Trafficking ◽  
Cushing’S Disease ◽  
Molecular Basis ◽  
Binding Pocket ◽  
Cushing's Disease ◽  
Binding Motif ◽  
Single Molecule Fret ◽  
Specific Protease ◽  
Ubiquitin Specific Protease

AbstractUbiquitin-specific protease 8 (USP8) is a deubiquitinating enzyme involved in multiple membrane trafficking pathways. The enzyme activity is inhibited by binding to 14-3-3 proteins. Mutations in the 14-3-3-binding motif in USP8 are related to Cushing’s disease. However, the molecular basis of USP8 activity regulation remains unclear. This study identified amino acids 645–684 of USP8 as an autoinhibitory region, which might interact with the catalytic USP domain, as per the results of pull-down and single-molecule FRET assays performed in this study. In silico modelling indicated that the region forms a WW-like domain structure, plugs the catalytic cleft, and narrows the entrance to the ubiquitin-binding pocket. Furthermore, 14-3-3 inhibited USP8 activity partly by enhancing the interaction between the WW-like and USP domains. These findings provide the molecular basis of USP8 autoinhibition via the WW-like domain. Moreover, they suggest that the release of autoinhibition may underlie Cushing’s disease due to USP8 mutations.

Abstract #825 Psychosis in Cushing’s Disease Treated with Etomidate

2018 ◽  
Vol 24 ◽  
pp. 185-186
Author(s):  
Sydney Blount ◽  
Marie Caldwell
Keyword(s):  
Cushing’S Disease ◽  
Cushing's Disease

Abstract #762: Treatment of Recurrent Cushing’s Disease

2005 ◽  
Vol 11 ◽  
pp. 54-55
Author(s):  
Daniel K. Short ◽  
William F. Young
Keyword(s):  
Cushing’S Disease ◽  
Cushing's Disease
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