Divergent self-association properties of paralogous proteins TRIM2 and TRIM3 regulate their E3 ligase activity

Diego Esposito; Jane Dudley-Fraser; Acely Garza-Garcia; Katrin Rittinger

doi:10.1038/s41467-022-35300-7

Nature Communications (Dec 2022)

Divergent self-association properties of paralogous proteins TRIM2 and TRIM3 regulate their E3 ligase activity

Diego Esposito,
Jane Dudley-Fraser,
Acely Garza-Garcia,
Katrin Rittinger

Affiliations

Diego Esposito: Molecular Structure of Cell Signalling Laboratory, The Francis Crick Institute
Jane Dudley-Fraser: Molecular Structure of Cell Signalling Laboratory, The Francis Crick Institute
Acely Garza-Garcia: Mycobacterial Metabolism and Antibiotic Research Laboratory, The Francis Crick Institute
Katrin Rittinger: Molecular Structure of Cell Signalling Laboratory, The Francis Crick Institute

DOI: https://doi.org/10.1038/s41467-022-35300-7
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 14

Abstract

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TRIM E3 ligases are key regulators of numerous cellular functions, yet their mechanism of action remains poorly understood. Here, the authors show that paralogous TRIM2 and TRIM3 adopt different self-association and activity profiles but interact in cells to modulate their respective activities.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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