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Mycobacterium tuberculosis hijacks ubiquitin to inhibit pyroptosis

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Dikic,  Ivan       
Institute of Biochemistry II, Medical Faculty, Goethe-University, Frankfurt am Main, Germany;
Max Planck Fellow Group ER remodelling Group, Prof. Ivan Đikić, Max Planck Institute of Biophysics, Max Planck Society;
Buchmann Institute for Molecular Life Sciences, Frankfurt am Main, Germany;

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Citation

Krause, D. S., & Dikic, I. (2022). Mycobacterium tuberculosis hijacks ubiquitin to inhibit pyroptosis. Molecular Cell, 82(24), 4588-4590. doi:10.1016/j.molcel.2022.11.020.


Cite as: https://hdl.handle.net/21.11116/0000-000C-0764-C
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.