Ramping up degradation for proliferation

Jon M Huibregtse; Andreas Matouschek

doi:10.1038/ncb3306

Ramping up degradation for proliferation

Nat Cell Biol. 2016 Feb;18(2):141-2. doi: 10.1038/ncb3306.

Authors

Jon M Huibregtse¹, Andreas Matouschek¹

Affiliation

¹ Department of Molecular Biosciences, The University of Texas at Austin, Austin, Texas 78712, USA.

PMID: 26820437
DOI: 10.1038/ncb3306

Abstract

The control of proteasome-mediated protein degradation is thought to occur mainly at the level of polyubiquitylation of the substrate. However, the proteasome can also be regulated directly, as now demonstrated by a study in which DYRK2-mediated phosphorylation of the 19S subunit Rpt3 is found to increase proteasome activity.

Publication types

Comment

MeSH terms

Animals
Breast Neoplasms / enzymology*
Cell Proliferation*
Cell Transformation, Neoplastic / metabolism*
Female
Humans
Proteasome Endopeptidase Complex / metabolism*
Protein Serine-Threonine Kinases / metabolism*
Protein-Tyrosine Kinases / metabolism*

Substances

Protein-Tyrosine Kinases
Protein Serine-Threonine Kinases
Proteasome Endopeptidase Complex