To be (in a transcriptional complex) or not to be (promoting UBR5 ubiquitylation): That is an answer to how degradation controls gene expression

Laura A Hehl; Brenda A Schulman

doi:10.1016/j.molcel.2023.07.010

To be (in a transcriptional complex) or not to be (promoting UBR5 ubiquitylation): That is an answer to how degradation controls gene expression

Mol Cell. 2023 Aug 3;83(15):2616-2618. doi: 10.1016/j.molcel.2023.07.010.

Authors

Laura A Hehl¹, Brenda A Schulman²

Affiliations

¹ Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany; TUM School of Natural Sciences, Department of Chemistry, 85747 Garching, Germany.
² Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany; TUM School of Natural Sciences, Department of Chemistry, 85747 Garching, Germany. Electronic address: schulman@biochem.mpg.de.

PMID: 37541216
DOI: 10.1016/j.molcel.2023.07.010

Abstract

Tsai et al.¹ in this issue and Mark et al.² in Cell reveal how the E3 ligase UBR5 mediates broad regulation by selectively targeting agonist-bound nuclear hormone receptors, MYC, and other transcriptional regulators not incorporated into active gene expression complexes.

Publication types

Research Support, Non-U.S. Gov't
Comment

MeSH terms

Gene Expression
Ubiquitin-Protein Ligases* / genetics
Ubiquitin-Protein Ligases* / metabolism
Ubiquitination

Substances

Ubiquitin-Protein Ligases