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PXD046004

PXD046004 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitlePhosphorylation Promotes DELLA Activity by Enhancing Its Binding to Histone H2A at Target Chromatin in Arabidopsis
DescriptionDELLA proteins are conserved master growth regulators that play a central role in controlling plant development in response to internal and environmental cues. DELLAs function as transcription regulators, which are recruited to target promoters by binding to transcription factors (TFs) and histone H2A via its GRAS domain. Recent studies showed that DELLA stability is regulated post-translationally via two mechanisms, phytohormone gibberellin-induced polyubiquitination for its rapid degradation, and Small Ubiquitin-like Modifier (SUMO)-conjugation to alter its accumulation. Moreover, DELLA activity is dynamically modulated by two distinct glycosylations: DELLA-TF interactions are enhanced by O-fucosylation, but inhibited by O-linked N-acetylglucosamine (O-GlcNAc) modification. However, the role of DELLA phosphorylation remains unclear. Here, we identified phosphorylation sites in REPRESSOR OF ga1-3 (RGA, an AtDELLA) purified from Arabidopsis by tandem mass spectrometry analysis, and showed that phosphorylation of the RGA LKS-peptide in the poly-S/T region enhances RGA-H2A interaction and RGA association with target promoters. Interestingly, phosphorylation does not affect RGA-TF interactions. Our study has uncovered that phosphorylation is a new regulatory mechanism of DELLA activity.
HostingRepositoryPRIDE
AnnounceDate2024-08-08
AnnouncementXMLSubmission_2024-08-08_10:13:05.955.xml
DigitalObjectIdentifierhttps://dx.doi.org/10.6019/PXD046004
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportSupported dataset by repository
PrimarySubmitterJeffrey Shabanowitz
SpeciesList scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: 3702;
ModificationListN-acetylhexosaminylated residue; fucosylated residue; phosphorylated residue; monohydroxylated residue; hexosylated residue; iodoacetamide derivatized residue
InstrumentOrbitrap Fusion
Dataset History
RevisionDatetimeStatusChangeLog Entry
02023-10-09 15:27:27ID requested
12024-08-08 10:13:06announced
Publication List
10.6019/PXD046004;
Keyword List
submitter keyword: RGA phosphorylation,Arabidopsis, DELLA
Contact List
Jeffrey Shabanowitz
contact affiliationDepartment of Chemistry,University of Virginia,Charlottesville, VA 22903 USA
contact emailjs4c@virginia.edu
lab head
Jeffrey Shabanowitz
contact affiliationUniversity of Virginia
contact emailjs4c@virginia.edu
dataset submitter
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Dataset FTP location
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