Article
Proteasome regulation by reversible tyrosine phosphorylation at the membrane.
Oncogene - 1 Mar 2021
Chen Lu, Zhang Yanan, Shu Xin, Chen Qiong, Wei Tiantian, Wang Heman, Wang Xiaorong, Wu Qirou, Zhang Xiaomei, Liu Xiaoyan, Zheng Suya, Huang Lan, Xiao Junyu, Jiang Chao, Yang Bing, Wang Zhiping, Guo Xing
Abstract excerpt
Reversible phosphorylation has emerged as an important mechanism for regulating 26S proteasome function in health and disease. Over 100 phospho-tyrosine sites of the human proteasome have been detected, and yet their function and regulation remain poorly understood. Here we show that the 19S subunit Rpt2 is phosphorylated at Tyr439, a strictly conserved residue within the C-terminal HbYX motif of Rpt2 that is...
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