SNX27-driven membrane localisation of OTULIN antagonises linear ubiquitination and NF-κB signalling activation.

ABSTRACT:

Background

Linear ubiquitination is a novel type of ubiquitination that plays important physiological roles in signalling pathways such as tumour necrosis factor (TNF) signalling. However, little is known about the regulatory mechanisms of linear ubiquitination, except the well-described enzymatic regulators E3 ligase linear ubiquitin chain assembly complex (LUBAC) and deubiquitinase OTULIN.

Results

Previously, we identified SNX27, a member of the sorting nexin family protein, as a selective linear ubiquitin chain interactor in mass spectrometry-based ubiquitin interaction screening. Here, we demonstrated that the interaction between the linear ubiquitin chain and SNX27 is mediated by the OTULIN. Furthermore, we found that SNX27 inhibits LUBAC-mediated linear ubiquitin chain

SUBMITTER: Shi R 

PROVIDER: S-EPMC8314547 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature