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Updated: Oct 26, 2025

In Vitro Analysis of E3 Ubiquitin Ligase Function
Published on: May 14, 2021
Ester-linked ubiquitination by HOIL-1 controls immune signalling by shaping the linear ubiquitin landscape
Jonathan N Pruneda1, Rune Busk Damgaard2
1Department of Molecular Microbiology & Immunology, Oregon Health & Science University, Portland, OR, USA.
Abstract:
Ester-linked ubiquitination of serine or threonine residues - or even lipids - has emerged as a new regulatory earmark in cell signalling. Petrova et al. (2021) now reveal that ubiquitin esterification by the atypical ubiquitin ligase HOIL-1, a component of the LUBAC complex, is critical for proper formation of linear ubiquitin chains and control of immune signalling in T cells and macrophages. Surprisingly, ester-linked ubiquitination can either promote or inhibit linear ubiquitin conjugation and cytokine production depending on the receptor and immune cell engaged. Comment on: https://doi.org/10.1111/febs.15896.
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