PXD048869 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Phosphorylation of the compartmentalized PKA substrate TAF15 regulates RNA-Protein interactions |
Description | Spatiotemporal-controlled second messengers alter molecular interactions of central signaling nodes for ensuring physiological signal transmission. One prototypical second messenger molecule which modulates kinase signal transmission is the cyclic-adenosine monophosphate (cAMP). The main proteinogenic cellular effectors of cAMP are compartmentalized protein kinase A (PKA) complexes. Their cell-type specific compositions precisely coordinate substrate phosphorylation and proper signal propagation which is indispensable for numerous cell-type specific functions. Here we present evidence that TAF15, which is implicated in the etiology of amyotrophic lateral sclerosis, represents a novel nuclear PKA substrate. In cross-linking and immunoprecipitation experiments (iCLIP) we showed that TAF15 phosphorylation alters the binding to target transcripts related to mRNA maturation, splicing and protein-binding related functions. TAF15 appears to be one of multiple PKA substrates that undergo RNA-binding dynamics upon phosphorylation. We observed that the activation of the cAMP-PKA signaling axis caused a change in the composition of a collection of RNA species that interact with TAF15. This observation appears to be a broader principle in the regulation of molecular interactions, as we identified a significant enrichment of RNA-binding proteins within endogenous PKA complexes. We assume that phosphorylation of RNA-binding domains adds another layer of regulation to binary protein-RNAs interactions with consequences to RNA features including binding specificities, localization, abundance and composition. |
HostingRepository | PRIDE |
AnnounceDate | 2024-04-04 |
AnnouncementXML | Submission_2024-04-04_02:22:40.284.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Omar Torres |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | phosphorylated residue; monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | Q Exactive HF |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2024-01-25 02:21:30 | ID requested | |
⏵ 1 | 2024-04-04 02:22:40 | announced | |
Publication List
Keyword List
submitter keyword: cAMP, TAF15,PKA, phosphorylation, RNA |
Contact List
Eduard Stefan |
contact affiliation | 1-Tyrolean Cancer Research Institute (TKFI), Innrain 66, A-6020 Innsbruck, Austria 2-Institute of Molecular Biology and Center for Molecular Biosciences, University of Innsbruck, Technikerstrasse 25, A-6020 Innsbruck, Austria. |
contact email | eduard.stefan@uibk.ac.at |
lab head | |
Omar Torres |
contact affiliation | Institute Medical Biochemistry, Medical University Innsbruck, Innrain 80-82, A-6020, Innsbruck, Austria |
contact email | omar.torres-quesada@i-med.ac.at |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD048869
- Label: PRIDE project
- Name: Phosphorylation of the compartmentalized PKA substrate TAF15 regulates RNA-Protein interactions