Format

Send to

Choose Destination
See comment in PubMed Commons below
Nat Rev Mol Cell Biol. 2012 Jul 23;13(8):508-23. doi: 10.1038/nrm3394.

Atypical ubiquitylation - the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages.

Author information

1
Medical Research Council (MRC) Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 0QH, UK.

Abstract

Ubiquitylation is one of the most abundant and versatile post-translational modifications (PTMs) in cells. Its versatility arises from the ability of ubiquitin to form eight structurally and functionally distinct polymers, in which ubiquitin moieties are linked via one of seven Lys residues or the amino terminus. Whereas the roles of Lys48- and Lys63-linked polyubiquitin in protein degradation and cellular signalling are well characterized, the functions of the remaining six 'atypical' ubiquitin chain types (linked via Lys6, Lys11, Lys27, Lys29, Lys33 and Met1) are less well defined. Recent developments provide insights into the mechanisms of ubiquitin chain assembly, recognition and hydrolysis and allow detailed analysis of the functions of atypical ubiquitin chains. The importance of Lys11 linkages and Met1 linkages in cell cycle regulation and nuclear factor-κB activation, respectively, highlight that the different ubiquitin chain types should be considered as functionally independent PTMs.

PMID:
22820888
DOI:
10.1038/nrm3394
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Nature Publishing Group
    Loading ...
    Support Center