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J Biol Chem. 2015 Oct 30;290(44):26437-44. doi: 10.1074/jbc.R115.653675. Epub 2015 Sep 9.

Using protein motion to read, write, and erase ubiquitin signals.

Author information

1
From the Innovative Genomics Initiative, University of California, Berkeley, California 94702 Aaron.Phillips@stjude.org.
2
From the Innovative Genomics Initiative, University of California, Berkeley, California 94702 jcorn@berkeley.edu.

Abstract

Eukaryotes use a tiny protein called ubiquitin to send a variety of signals, most often by post-translationally attaching ubiquitins to substrate proteins and to each other, thereby forming polyubiquitin chains. A combination of biophysical, biochemical, and biological studies has shown that complex macromolecular dynamics are central to many aspects of ubiquitin signaling. This review focuses on how equilibrium fluctuations and coordinated motions of ubiquitin itself, the ubiquitin conjugation machinery, and deubiquitinating enzymes enable activity and regulation on many levels, with implications for how such a tiny protein can send so many signals.

KEYWORDS:

biophysics; deubiquitylation (deubiquitination); structural biology; ubiquitin; ubiquitylation (ubiquitination)

PMID:
26354440
PMCID:
PMC4646302
DOI:
10.1074/jbc.R115.653675
[Indexed for MEDLINE]
Free PMC Article

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