Regulation of ubiquitin and ubiquitin-like modifiers by phosphorylation.

Regulation of ubiquitin and ubiquitin-like modifiers by phosphorylation.
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DOI:
10.1111/febs.16101
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发表时间:
2022-08
期刊:
The FEBS journal
影响因子:
--
通讯作者:
MacGurn JA
MacGurn JA
中科院分区:
其他
文献类型:
--
作者:
Hepowit NL;Kolbe CC;Zelle SR;Latz E;MacGurn JA

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The regulatory influence of ubiquitin is vast, encompassing all cellular processes, by virtue of its central roles in protein degradation, membrane trafficking, and cell signaling. But how does ubiquitin, a 76 amino acid peptide, carry out such diverse, complex functions in eukaryotic cells? Part of the answer is rooted in the high degree of complexity associated with ubiquitin polymers, which can be “read” and processed differently depending on topology and cellular context. However, recent evidence indicates that post-translational modifications on ubiquitin itself enhance the complexity of the ubiquitin code. Here, we review recent discoveries related to the regulation of the ubiquitin code by phosphorylation. We summarize what is currently known about phosphorylation of ubiquitin at Ser65, Ser57 and Thr12, and we discuss the potential for phospho-regulation of ubiquitin at other sites. We also discuss accumulating evidence that ubiquitin-like modifiers, such as SUMO, are likewise regulated by phosphorylation. A complete understanding of these regulatory codes and their complex lexicon will require dissection of mechanisms that govern phosphorylation of ubiquitin and ubiquitin-like proteins, particularly in the context of cellular stress and disease.
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