التفاصيل البيبلوغرافية
العنوان: |
Ester‐linked ubiquitination by HOIL‐1 controls immune signalling by shaping the linear ubiquitin landscape. |
المؤلفون: |
Pruneda, Jonathan N.1 (AUTHOR) pruneda@ohsu.edu, Damgaard, Rune Busk2 (AUTHOR) rudam@dtu.dk |
المصدر: |
FEBS Journal. Oct2021, Vol. 288 Issue 20, p5903-5908. 6p. |
مصطلحات موضوعية: |
*UBIQUITIN, *CELL communication, *CELL receptors, *T cells, *CYTOKINES |
مستخلص: |
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.15896Test. [ABSTRACT FROM AUTHOR] |
قاعدة البيانات: |
Academic Search Index |