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结核分枝杆菌通过PtpA蛋白依赖性去磷酸化宿主GSK3α来促进巨噬细胞的抗凋亡活性。

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

作者信息

Poirier Valérie, Bach Horacio, Av-Gay Yossef

机构信息

From the Division of Infectious Diseases, Department of Medicine, University of British Columbia, Vancouver, British Columbia V6H 3Z6, Canada.

From the Division of Infectious Diseases, Department of Medicine, University of British Columbia, Vancouver, British Columbia V6H 3Z6, Canada

出版信息

J Biol Chem. 2014 Oct 17;289(42):29376-85. doi: 10.1074/jbc.M114.582502. Epub 2014 Sep 3.

DOI:10.1074/jbc.M114.582502
PMID:25187516
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4200286/
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.

摘要

结核分枝杆菌酪氨酸磷酸酶PtpA可抑制巨噬细胞中清除入侵病原体所需的两个关键细胞事件，即吞噬体酸化和成熟。激酶组分析显示，结核分枝杆菌感染后，巨噬细胞蛋白质的磷酸化状态发生了多种依赖于PtpA的变化。在这些蛋白质中，我们发现PtpA使GSK3α的酪氨酸（Tyr279）去磷酸化，这导致GSK3α抗凋亡活性的调节，从而在感染早期促进病原体存活。

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本文引用的文献

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Mycobacterium tuberculosis protein tyrosine phosphatase (PtpA) excludes host vacuolar-H+-ATPase to inhibit phagosome acidification.结核分枝杆菌蛋白酪氨酸磷酸酶（PtpA）排除宿主液泡型 H+-ATP 酶以抑制吞噬体酸化。
Proc Natl Acad Sci U S A. 2011 Nov 29;108(48):19371-6. doi: 10.1073/pnas.1109201108. Epub 2011 Nov 15.
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