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The protein phosphatase 2A holoenzyme is a key regulator of starch metabolism and bradyzoite differentiation in Toxoplasma gondii

Wang, Jin-Lei; Li, Ting-Ting; Elsheikha, Hany M.; Liang, Qin-Li; Zhang, Zhi-Wei; Wang, Meng; Sibley, L. David; Zhu, Xing-Quan

The protein phosphatase 2A holoenzyme is a key regulator of starch metabolism and bradyzoite differentiation in Toxoplasma gondii Thumbnail


Authors

Jin-Lei Wang

Ting-Ting Li

Qin-Li Liang

Zhi-Wei Zhang

Meng Wang

L. David Sibley

Xing-Quan Zhu



Abstract

Phenotypic switching between tachyzoite and bradyzoite is the fundamental mechanism underpinning the pathogenicity and adaptability of the protozoan parasite Toxoplasma gondii. Although accumulation of cytoplasmic starch granules is a hallmark of the quiescent bradyzoite stage, the regulatory factors and mechanisms contributing to amylopectin storage in bradyzoites are incompletely known. Here, we show that T. gondii protein phosphatase 2A (PP2A) holoenzyme is composed of a catalytic subunit PP2A-C, a scaffold subunit PP2A-A and a regulatory subunit PP2A-B. Disruption of any of these subunits increased starch accumulation and blocked the tachyzoite-to- bradyzoite differentiation. PP2A contributes to the regulation of amylopectin metabolism via dephosphorylation of calcium-dependent protein kinase 2 at S679. Phosphoproteomics identified several putative PP2A holoenzyme sub- strates that are involved in bradyzoite differentiation. Our findings provide novel insight into the role of PP2A as a key regulator of starch metabolism and bradyzoite differentiation in T. gondii.

Journal Article Type Article
Acceptance Date Nov 22, 2022
Online Publication Date Dec 8, 2022
Publication Date Dec 8, 2022
Deposit Date Dec 8, 2022
Publicly Available Date Dec 8, 2022
Journal Nature Communications
Electronic ISSN 2041-1723
Publisher Springer Science and Business Media LLC
Peer Reviewed Peer Reviewed
Volume 13
Issue 1
Article Number 7560
DOI https://doi.org/10.1038/s41467-022-35267-5
Keywords General Physics and Astronomy; General Biochemistry, Genetics and Molecular Biology; General Chemistry; Multidisciplinary
Public URL https://nottingham-repository.worktribe.com/output/14596517
Publisher URL https://www.nature.com/articles/s41467-022-35267-5
Additional Information Received: 30 March 2022; Accepted: 22 November 2022; First Online: 8 December 2022; : The authors declare no competing interests.

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