Mycobacterium tuberculosis hijacks ubiquitin to inhibit pyroptosis

Daniela S Krause; Ivan Dikic

doi:10.1016/j.molcel.2022.11.020

Mycobacterium tuberculosis hijacks ubiquitin to inhibit pyroptosis

Mol Cell. 2022 Dec 15;82(24):4588-4590. doi: 10.1016/j.molcel.2022.11.020.

Authors

Daniela S Krause¹, Ivan Dikic²

Affiliations

¹ Georg-Speyer-Haus, Institute for Tumor Biology and Experimental Therapy, Frankfurt am Main, Germany; Institute of Biochemistry II, Medical Faculty, Goethe-University, Frankfurt am Main, Germany; Institute of General Pharmacology and Toxicology, Goethe-University, Frankfurt am Main, Germany.
² Institute of Biochemistry II, Medical Faculty, Goethe-University, Frankfurt am Main, Germany; Buchmann Institute for Molecular Life Sciences, Frankfurt am Main, Germany; Max Planck Institute for Biophysics, Frankfurt am Main, Germany. Electronic address: dikic@biochem2.uni-frankfurt.de.

PMID: 36525954
DOI: 10.1016/j.molcel.2022.11.020

Abstract

Chai et al.¹ reveal that the eukaryotic-like effector protein PtpB from Mycobacterium tuberculosis (MTB) dephosphorylates phospholipid membrane proteins, which prevents membrane localization of cleaved gasdermin D, inhibiting pyroptosis and cytokine release by infected macrophages to enable MTB immune evasion.

Publication types

Research Support, Non-U.S. Gov't
Comment

MeSH terms

Cytokines / metabolism
Macrophages / metabolism
Mycobacterium tuberculosis* / metabolism
Pyroptosis
Ubiquitin / metabolism

Substances

Ubiquitin
Cytokines