A Billion Ubiquitin Variants to Probe and Modulate the UPS

Larissa A Canadeo; Jon M Huibregtse

doi:10.1016/j.molcel.2016.03.023

A Billion Ubiquitin Variants to Probe and Modulate the UPS

Mol Cell. 2016 Apr 7;62(1):2-4. doi: 10.1016/j.molcel.2016.03.023.

Authors

Larissa A Canadeo¹, Jon M Huibregtse²

Affiliations

¹ Department of Molecular Biosciences, University of Texas at Austin, Austin, TX 78712, USA.
² Department of Molecular Biosciences, University of Texas at Austin, Austin, TX 78712, USA. Electronic address: huibregtse@austin.utexas.edu.

PMID: 27058783
DOI: 10.1016/j.molcel.2016.03.023

Abstract

Low-affinity but highly specific protein-protein interactions abound within the ubiquitin-proteasome system (UPS). Selection for ubiquitin variants (UbVs) that bind tightly to HECT ubiquitin ligases proved remarkably useful for probing enzyme mechanism and modulating E3 activities in cells.

Publication types

Comment

MeSH terms

Humans
Proteasome Endopeptidase Complex / metabolism*
Ubiquitin / metabolism*
Ubiquitin-Protein Ligases / metabolism

Substances

Ubiquitin
Ubiquitin-Protein Ligases
Proteasome Endopeptidase Complex