Journal Article (Review Article) DZNE-2022-00142

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png
Regulation of ubiquitin and ubiquitin-like modifiers by phosphorylation.

 ;  ;  ;  ;

2021
Wiley-Blackwell Oxford [u.a.]

The FEBS journal 289(16), 4797-4810 () [10.1111/febs.16101]

This record in other databases:    

Please use a persistent id in citations: doi:

Abstract: 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 phosphoregulation 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.

Keyword(s): Phosphorylation (MeSH) ; Protein Processing, Post-Translational (MeSH) ; Ubiquitin: metabolism (MeSH) ; Ubiquitin-Protein Ligases: genetics (MeSH) ; Ubiquitins: metabolism (MeSH) ; mitophagy ; phosphorylation ; protein degradation ; proteostasis ; signaling ; stress responses ; ubiquitin

Classification:

Contributing Institute(s):
  1. Innate Immunity in Neurodegeneration (AG Latz ; AG Latz)
Research Program(s):
  1. 351 - Brain Function (POF4-351) (POF4-351)

Appears in the scientific report 2021
Database coverage:
Medline ; BIOSIS Previews ; Biological Abstracts ; Clarivate Analytics Master Journal List ; Current Contents - Life Sciences ; DEAL Wiley ; Ebsco Academic Search ; Essential Science Indicators ; IF >= 5 ; JCR ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection
Click to display QR Code for this record

The record appears in these collections:
Document types > Articles > Journal Article
Institute Collections > BN DZNE > BN DZNE-AG Latz
Public records
Publications Database

 Record created 2022-03-31, last modified 2024-02-20


Rate this document:

Rate this document:
1
2
3
 
(Not yet reviewed)