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PXD033120-1

PXD033120 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleThe protein phosphatase 2A holoenzyme is a key regulator of starch metabolism and bradyzoite differentiation in Toxoplasma gondii
DescriptionPhenotypic switching from tachyzoite to bradyzoite and vice versa is the fundamental mechanism underpinning the pathogenicity and adaptability of the protozoan parasite Toxoplasma gondii. Accumulation of cytoplasmic starch granules is a hallmark of the quiescent bradyzoite stage. The regulatory factors and mechanisms that contribute to amylopectin storage in bradyzoites remain incompletely known. Here, we show that T. gondii protein phosphatase 2A (PP2A) holoenzyme is composed of a catalytic subunit (PP2A-C), a structural subunit (PP2A-A) and a regulatory subunit (PP2A-B). Disruption of any of these subunits increased starch accumulation and disrupted the parasite differentiation. The putative PP2A holoenzyme substrates were identified by phosphoproteomics. PP2A contributes to the regulation of amylopectin metabolism via dephosphorylation of calcium-dependent protein kinase 2 at S679. Several putative PP2A substrates were found to play important roles in bradyzoite differentiation. Our findings establish PP2A as an integral component of the regulatory network mediating amylopectin metabolism and tachyzoite-bradyzoite transformation in T. gondii.
HostingRepositoryPRIDE
AnnounceDate2022-11-05
AnnouncementXMLSubmission_2022-11-05_05:55:43.505.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterJinLeiWang
SpeciesList scientific name: Toxoplasma gondii; NCBI TaxID: 5811;
ModificationListphosphorylated residue
InstrumentLTQ
Dataset History
RevisionDatetimeStatusChangeLog Entry
02022-04-08 13:38:32ID requested
12022-11-05 05:55:43announced
Publication List
Dataset with its publication pending
Keyword List
submitter keyword: PP2A holoenzyme,Toxoplasma gondii, differentiation, dephosphorylation., starch metabolism
Contact List
Xing-QuanZhu
contact affiliationState Key Laboratory of Veterinary Etiological Biology, Key Laboratory of Veterinary Parasitology of Gansu Province, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, Gansu Province 730046, PR China
contact emailxingquanzhu1@hotmail.com
lab head
JinLeiWang
contact affiliationLanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China.
contact emailwangjinlei90@126.com
dataset submitter
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Dataset FTP location
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