结核分枝杆菌中蛋白质酪氨酸磷酸酶A活性的磷酸化调控
Phosphorylation control of protein tyrosine phosphatase A activity in Mycobacterium tuberculosis.
作者信息
Zhou Peifu, Li Wu, Wong Dennis, Xie Jianping, Av-Gay Yossef
机构信息
Department of Medicine, Division of Infectious Diseases, University of British Columbia, Vancouver, BC V5Z 3J5, Canada; Institute of Modern Biopharmaceuticals, State Key Laboratory Breeding Base of Eco-environment and Bio-resource of the Three Gorges Area, Key Laboratory of Eco-environment of Three Gorges Reservoir, Ministry of Education, School of Life Sciences, Southwest University, Chongqing 400715, China; Institute of Ethnic-minority Medicine, School of Chemistry & Environmental Science, Guizhou Minzu University, Guiyang 550025, China.
Institute of Modern Biopharmaceuticals, State Key Laboratory Breeding Base of Eco-environment and Bio-resource of the Three Gorges Area, Key Laboratory of Eco-environment of Three Gorges Reservoir, Ministry of Education, School of Life Sciences, Southwest University, Chongqing 400715, China.
出版信息
FEBS Lett. 2015 Jan 30;589(3):326-31. doi: 10.1016/j.febslet.2014.12.015. Epub 2014 Dec 20.
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.
蛋白酪氨酸磷酸酶A（PtpA）已被证明在结核分枝杆菌（Mtb）感染人类巨噬细胞过程中起关键作用。蛋白酪氨酸激酶A（PtkA）是首个被证明可使PtpA磷酸化的蛋白酪氨酸激酶。在此，我们发现PtkA介导的PtpA在酪氨酸128和酪氨酸129位点的磷酸化增强了PtpA的磷酸酶活性。此外，体外蛋白质-蛋白质相互作用试验表明，PtpA可被几种类真核丝氨酸/苏氨酸蛋白激酶磷酸化，如蛋白激酶A（PknA）。研究发现PknA通过苏氨酸45位点的磷酸化来调节PtpA的磷酸酶活性。这些结果表明，两个独立的蛋白激酶家族成员可调节Mtb中PtpA的活性。
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