Ester-linked ubiquitination by HOIL-1 controls immune signalling by shaping the linear ubiquitin landscape.

Pruneda, Jonathan N; Damgaard, Rune Busk

Pruneda, Jonathan N; Damgaard, Rune Busk.

Afiliación

Pruneda JN; Department of Molecular Microbiology & Immunology, Oregon Health & Science University, Portland, OR, USA.
Damgaard RB; Department of Biotechnology and Biomedicine, Technical University of Denmark, Lyngby, Denmark.

FEBS J ; 288(20): 5903-5908, 2021 10.

Article en En | MEDLINE | ID: mdl-34322999

RESUMEN

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.

Asunto(s)

Ésteres; Ubiquitina; Transducción de Señal; Ubiquitina/metabolismo; Ubiquitina-Proteína Ligasas/metabolismo; Ubiquitinación

Palabras clave

HOIL-1; LUBAC; immune signalling; inflammation; ubiquitin

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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ubiquitina / Ésteres Idioma: En Revista: FEBS J Asunto de la revista: BIOQUIMICA Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido

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