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Mycobacterium tuberculosis promotes anti-apoptotic activity of the macrophage by PtpA protein-dependent dephosphorylation of host GSK3?.

ABSTRACT: Mycobacterium tuberculosis tyrosine phosphatase PtpA inhibits two key cellular events in macrophages required for the elimination of invading organisms, phagosome acidification, and maturation. Kinome analysis revealed multiple PtpA-dependent changes to the phosphorylation status of macrophage proteins upon M. tuberculosis infection. Among those proteins we show that PtpA dephosphorylates GSK3? on amino acid Tyr(279), which leads to modulation of GSK3? anti-apoptotic activity, promoting pathogen survival early during infection.

SUBMITTER: Poirier V

PROVIDER: S-EPMC4200286 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature

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Mycobacterium tuberculosis promotes anti-apoptotic activity of the macrophage by PtpA protein-dependent dephosphorylation of host GSK3α.

Poirier Valérie V Bach Horacio H Av-Gay Yossef Y

The Journal of biological chemistry 20140903 42

Mycobacterium tuberculosis tyrosine phosphatase PtpA inhibits two key cellular events in macrophages required for the elimination of invading organisms, phagosome acidification, and maturation. Kinome analysis revealed multiple PtpA-dependent changes to the phosphorylation status of macrophage proteins upon M. tuberculosis infection. Among those proteins we show that PtpA dephosphorylates GSK3α on amino acid Tyr(279), which leads to modulation of GSK3α anti-apoptotic activity, promoting pathogen ...[more]

PMID: 25187516

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