Xing Guo identifies a single phosphorylation site on the proteasome to be an essential regulator for tumorigenesis

26S Proteasome is a complex machinery responsible for protein degradation and recycle. Although playing a vital role in protein turnover and maintaining cellular homeostasis, the regulation of this machinery was largely understudied. In an effort to expand our knowledge of regulators of proteasome function, 'General' Guo carried out a kinome-wide screen and identified a previously unrecognized proteasome kinase (DYRK2), which directly phosphorylates the proteasome at Rpt3 subunit at a conserved Thr25. Importantly, Thr25 phosphorylation is essential for enhanced substrate translocation and degradation by the proteasome leading to regulation of cell proliferation, mitosis and enhanced tumor burden in a mouse xenograft model. The paper has been published in Nature Cell Biology. Jack was very happy with the outcome and congratulated Guo on the fine achievement. The paper has been co-authored by the laboratories of Dr. Jing Yang of UCSD and Dr. Lan Huang of UC Irvine. Guo, who recently moved to Zhejiang University, Hangzhou, China to start his own lab seemed quite relieved, 'Well, what can i say? It's great to see it in print, although we all knew it's an interesting story and I could only wish that it had been accepted earlier!'. Congratulations to 'General' Guo and colleagues! To check out Guo's paper, please follow the link