scholarly journals The role of the ubiquitination-proteasome pathway in breast cancer: Use of mouse models for analyzing ubiquitination processes

2002 ◽  
Vol 5 (1) ◽  
Author(s):  
Sabrina Rossi ◽  
Massimo Loda
Bone Reports ◽  
2021 ◽  
Vol 14 ◽  
pp. 100900
Author(s):  
Evi Gkikopoulou ◽  
Anthi Kolokotroni ◽  
Vagelis Rinotas ◽  
Melina Dragolia ◽  
Vasileios Ntafis ◽  
...  

2007 ◽  
Vol 25 (2) ◽  
pp. 109-118 ◽  
Author(s):  
Sunny Y. Wong ◽  
Denise Crowley ◽  
Roderick T. Bronson ◽  
Richard O. Hynes
Keyword(s):  

2022 ◽  
Author(s):  
Yushan Zhu ◽  
Qiangqiang Liu ◽  
Qian Luo ◽  
Jianyu Feng ◽  
Yanping Zhao ◽  
...  

DBC1 has been characterized as a key regulator of physiological and pathophysiological activities, such as DNA damage, senescence and tumorigenesis. However, the mechanism by which the functional stability of DBC1 is regulated has yet to be elucidated. Here, we report that the ubiquitination-mediated degradation of DBC1 is dynamically regulated by the E3 ubiquitin ligase SIAH2 and deubiquitinase OTUD5 under hypoxic stress. Mechanistically, hypoxia promoted the competitive binding of SIAH2 with OTUD5 to DBC1, resulting in the ubiquitination and subsequent degradation of DBC1 through the ubiquitin-proteasome pathway. Siah2 knockout inhibited tumor cell proliferation and migration, which could be rescued by double knockout of Siah2/DBC1. Human tissue microarray analysis further revealed that the SIAH2/DBC1 axis was responsible for tumor progression under hypoxic stress. These findings define a key role of the hypoxia-mediated SIAH2-DBC1 pathway in the progression of human breast cancer and provide novel insights into the metastatic mechanism of breast cancer.


2004 ◽  
Vol 40 ◽  
pp. 41-58 ◽  
Author(s):  
William B Pratt ◽  
Mario D Galigniana ◽  
Yoshihiro Morishima ◽  
Patrick J M Murphy

Unliganded steroid receptors are assembled into heterocomplexes with heat-shock protein (hsp) 90 by a multiprotein chaperone machinery. In addition to binding the receptors at the chaperone site, hsp90 binds cofactors at other sites that are part of the assembly machinery, as well as immunophilins that connect the assembled receptor-hsp90 heterocomplexes to a protein trafficking pathway. The hsp90-/hsp70-based chaperone machinery interacts with the unliganded glucocorticoid receptor to open the steroid-binding cleft to access by a steroid, and the machinery interacts in very dynamic fashion with the liganded, transformed receptor to facilitate its translocation along microtubular highways to the nucleus. In the nucleus, the chaperone machinery interacts with the receptor in transcriptional regulatory complexes after hormone dissociation to release the receptor and terminate transcriptional activation. By forming heterocomplexes with hsp90, the chaperone machinery stabilizes the receptor to degradation by the ubiquitin-proteasome pathway of proteolysis.


Pneumologie ◽  
2014 ◽  
Vol 68 (06) ◽  
Author(s):  
A Lorenz ◽  
M Busse ◽  
K Dalüge ◽  
AK Behrendt ◽  
G Hansen ◽  
...  
Keyword(s):  

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