Tag you're it: A phosphatase inhibitor changes the fate of intracellular mycobacteria

Charul Jani; Amy K Barczak

doi:10.1016/j.chembiol.2022.06.008

Tag you're it: A phosphatase inhibitor changes the fate of intracellular mycobacteria

Cell Chem Biol. 2022 Jul 21;29(7):1065-1067. doi: 10.1016/j.chembiol.2022.06.008.

Authors

Charul Jani¹, Amy K Barczak²

Affiliations

¹ The Ragon Institute of MGH, MIT and Harvard, Cambridge, MA, USA.
² The Ragon Institute of MGH, MIT and Harvard, Cambridge, MA, USA; Division of Infectious Diseases, Massachusetts General Hospital, Boston, MA, USA; Department of Medicine, Harvard Medical School, Boston, MA, USA. Electronic address: abarczak@mgh.harvard.edu.

PMID: 35868234
DOI: 10.1016/j.chembiol.2022.06.008

Abstract

In this issue of Cell Chemical Biology, Berton and colleagues describe a small-molecule inhibitor of the metal-dependent phosphatase PPM1A that enhances phosphorylation of the autophagy adapter p62. Inhibiting PPM1A results in enhanced clearance of Mycobacterium tuberculosis-infected macrophages, pointing to phosphatases as potential targets for host-directed therapies for tuberculosis.

Publication types

Research Support, N.I.H., Extramural
Comment

MeSH terms

Autophagy
Humans
Macrophages / microbiology
Mycobacterium tuberculosis*
Phosphoric Monoester Hydrolases
Protein Phosphatase 2C
Tuberculosis* / drug therapy

Substances

PPM1A protein, human
Protein Phosphatase 2C
Phosphoric Monoester Hydrolases

Abstract

Publication types

MeSH terms

Substances

Grants and funding