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Lysine ubiquitination and acetylation of human cardiac 20S proteasomes

✍ Scribed by Zong, Nobel; Ping, Peipei; Lau, Edward; Choi, Howard J. H.; Ng, Dominic C. M.; Meyer, David; Fang, Caiyun; Li, Haomin; Wang, Ding; Zelaya, Ivette M.; Yates, John R.; Lam, Maggie P. Y.

Book ID
126909861
Publisher
John Wiley and Sons
Year
2014
Tongue
English
Weight
537 KB
Volume
8
Category
Article
ISSN
1862-8346

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It is now becoming apparent that cross-talk between two protein lysine modifications, acetylation and ubiquitination, is a critical regulatory mechanism controlling vital cellular functions. The most apparent effect is the inhibition of proteasome-mediated protein degradation by lysine acetylation.