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PXD002756

PXD002756 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleProteomic and Phosphoproteomic Analyses Reveal Extensive Phosphorylation of Regulatory Proteins in Developing Rice Anthers
DescriptionAnther development, particularly around the time of meiosis, is extremely crucial for plant sexual reproduction. Meanwhile, cell-to-cell communication between somatic (especial tapetum) cells and meiocytes are important for both somatic anther development and meiosis. To investigate possible molecular mechanisms involved in protein activities during anther development, we applied high-resolution mass spectrometry-based proteomic and phosphoproteomic analyses for developing rice (Oryza sativa) anthers around the time of meiosis (RAM). In total, we identified 4,984 proteins and 3,203 phosphoproteins with 8,973 unique phosphorylation sites (p-sites). Among those detected here, 1,544 phosphoproteins are currently absent in the Plant Protein Phosphorylation DataBase (P3DB), substantially enriching plant phosphorylation information. Mapman enrichment analysis showed that “DNA repair”, “transcription regulation” and “signalling” related proteins were over-represented in the phosphorylated proteins. Ten genetically identified rice meiotic proteins were detected to be phosphorylated at a total of 25 p-sites; moreover more than 400 meiotically expressed proteins were revealed to be phosphorylated and their phosphorylation sites were precisely assigned. 163 putative secretory proteins, possibly functioning in cell-to-cell communication, are also phosphorylated. Furthermore, we showed that DNA synthesis, RNA splicing and RNA-directed DNA methylation pathways are extensively affected by phosphorylation. In addition, our data support forty-six kinase-substrate pairs predicted by the rice Kinase-Protein Interaction Map, with SnRK1 substrates highly enriched. Taken together, our data revealed extensive protein phosphorylation during anther development, suggesting an important post-translational modification mechanism for protein activity.
HostingRepositoryPRIDE
AnnounceDate2021-01-13
AnnouncementXMLSubmission_2021-01-13_08:58:49.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterJuanying Ye
SpeciesList scientific name: Rice(O. sativa); NCBI TaxID: 4530;
ModificationListphosphorylated residue
InstrumentLTQ Orbitrap Elite
Dataset History
RevisionDatetimeStatusChangeLog Entry
02015-08-18 01:28:25ID requested
12021-01-13 08:58:50announced
Publication List
Ye J, Zhang Z, Long H, Zhang Z, Hong Y, Zhang X, You C, Liang W, Ma H, Lu P, Proteomic and phosphoproteomic analyses reveal extensive phosphorylation of regulatory proteins in developing rice anthers. Plant J, 84(3):527-44(2015) [pubmed]
Keyword List
curator keyword: Biological
submitter keyword: Oryza sativa, mass spectrometry, phosphoproteomics, meiosis, anther development
Contact List
Hong Ma
contact affiliationState Key Laboratory of Genetic Engineering and Collaborative Innovation Center of Genetics and Development, Institute of Plant Biology, School of Life Sciences, Fudan University
contact emailhongma@fudan.edu.cn
lab head
Juanying Ye
contact affiliationFudan university
contact emailyejuanying@fudan.edu.cn
dataset submitter
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