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Phosphorylation control of protein tyrosine phosphatase A activity in Mycobacterium tuberculosis
Author(s) -
Zhou Peifu,
Li Wu,
Wong Dennis,
Xie Jianping,
Av-Gay Yossef
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.12.015
Subject(s) - protein tyrosine phosphatase , mycobacterium tuberculosis , phosphorylation , phosphatase , chemistry , tyrosine , microbiology and biotechnology , biochemistry , tuberculosis , biology , medicine , pathology
Protein tyrosine phosphatase A (PtpA) has been shown to play a key role in human macrophage infection by Mycobacterium tuberculosis ( Mtb ). Protein tyrosine kinase A (PtkA) was the first protein tyrosine kinase shown to phosphorylate PtpA. Here, we found that PtkA‐mediated phosphorylation of PtPA on Tyr‐128 and Tyr‐129 enhances the PtPA phosphatase activity. Moreover, ex‐vivo protein–protein interaction assays showed that PtpA can be phosphorylated by several eukaryotic‐like Ser/Thr protein kinases, such as protein kinase A (PknA). PknA was found to regulate PtpA phosphatase activity through Thr‐45 phosphorylation. These results indicate that members of two independent families of protein kinases tune PtpA activity in Mtb .