Literature DB >> 25187516

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

Valérie Poirier1, Horacio Bach1, Yossef Av-Gay2.   

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 GSK3α on amino acid Tyr(279), which leads to modulation of GSK3α anti-apoptotic activity, promoting pathogen survival early during infection.
© 2014 by The American Society for Biochemistry and Molecular Biology, Inc.

Entities:  

Keywords:  Apoptosis; Macrophage; Mycobacterium tuberculosis; Protein-tyrosine Phosphatase (Tyrosine Phosphatase); Signal Transduction

Mesh：

Substances：

Year:  2014        PMID： 25187516      PMCID： PMC4200286          DOI： 10.1074/jbc.M114.582502

Source DB:  PubMed          Journal:  J Biol Chem        ISSN： 0021-9258            Impact factor:   5.157


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