The GID ubiquitin ligase complex just reached the next level of complexity

Lisa Fechtner; Thorsten Pfirrmann

doi:10.1016/j.molcel.2021.05.003

The GID ubiquitin ligase complex just reached the next level of complexity

Mol Cell. 2021 Jun 3;81(11):2270-2272. doi: 10.1016/j.molcel.2021.05.003.

Authors

Lisa Fechtner¹, Thorsten Pfirrmann²

Affiliations

¹ Institute of Physiological Chemistry, Martin-Luther University Halle-Wittenberg, Halle, Germany.
² Institute of Physiological Chemistry, Martin-Luther University Halle-Wittenberg, Halle, Germany; Health and Medical University, Potsdam, Germany. Electronic address: thorsten.pfirrmann@health-and-medical-university.de.

PMID: 34087177
DOI: 10.1016/j.molcel.2021.05.003

Abstract

This issue of Molecular Cell features two publications that make striking discoveries concerning the GID ubiquitin ligase complex. Kong et al. (2021) describe a substrate recognition mechanism, expanding the set of GID complex substrates, whereas Sherpa et al. (2021) unravel the molecular mechanism by which the GID complex targets the quaternary structure of a substrate.

Publication types

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

MeSH terms

Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins*
Ubiquitin
Ubiquitin-Protein Ligases* / genetics

Substances

Saccharomyces cerevisiae Proteins
Ubiquitin
Ubiquitin-Protein Ligases