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Advanced filters: Author: Juraj Ahel Clear advanced filters

ATP functions as a pathogen-associated molecular pattern to activate the E3 ubiquitin ligase RNF213

RNF213 is an E3 ligase with ATPase activity. Here, the authors show that RNF213 is activated by ATP binding and senses cellular energy states, and reveal a transthiolation mechanism induced by immune signals through ATP increase in macrophages.

Juraj Ahel
Arda Balci
Adam J. Fletcher
ResearchOpen Access13 May 2025
Nature Communications

Volume: 16, P: 1-19
HUWE1 employs a giant substrate-binding ring to feed and regulate its HECT E3 domain

The full-length structure of HUWE1 reveals the bipartite organization of a giant E3 ubiquitin ligase, comprising a catalytic HECT domain and a large, ring-shaped scaffold that provides docking sites for various substrates and regulates E3 activity.

Daniel B. Grabarczyk
Olga A. Petrova
Tim Clausen
Research22 Jul 2021
Nature Chemical Biology

Volume: 17, P: 1084-1092

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ATP functions as a pathogen-associated molecular pattern to activate the E3 ubiquitin ligase RNF213

HUWE1 employs a giant substrate-binding ring to feed and regulate its HECT E3 domain

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