PXD039877

PXD039877 is an original dataset announced via ProteomeXchange.

Title	Phosphorylation of RADICAL-INDUCED CELL DEATH1 by Photoregulatory Protein Kinases
Description	RADICAL-INDUCED CELL DEATH1 (RCD1) is a multidomain protein with intrinsically disordered regions (IDRs) separating its highly structured domains. RCD1 regulates plant development and stress tolerance by interacting with numerous transcription factors (TFs) through its C-terminal RST domain. It has been shown to interact in a non-RST-dependent manner with Photoregulatory Protein Kinases (PPKs). In Arabidopsis, this recently discovered family of protein kinases is comprised of four members that localize to nuclear bodies (NBs), subnuclear non-membrane bound complexes of mostly unknown function. PPK-dependent phosphorylation has been shown to target proteins for degradation, thereby playing an essential role in protein turnover. Mass spectrometric analysis of the in vitro phosphorylated GST-RCD1 revealed several PPK-dependent RCD1 phosphopeptides that were also identified in the in vivo pull-down experiments. Most of these phosphosites were clustered in the IDR2, the intrinsically disordered region between the WWE and PARP-like domains. Using transgenic lines expressing non-phosphorylatable version of RCD1 we showed that phosphorylation of the IDR2 is involved in the regulation of the RCD1 affecting its subnuclear distribution to NBs of different size and number. Moreover, phosphorylation of IDR2 facilitates degradation of RCD1 and possibly also its partner TFs. Thus, it is necessary for the function of RCD1 as a negative transcriptional co-regulator.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_08:45:06.827.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Julia Vainonen
SpeciesList	scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: 3702;
ModificationList	phosphorylated residue; acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2023-02-06 02:58:07	ID requested
1	2023-04-21 00:57:22	announced
⏵ 2	2023-11-14 08:45:07	announced	2023-11-14: Updated project metadata.

Vainonen JP, Gossens R, Krasensky-Wrzaczek J, De Masi R, Danciu I, Puukko T, Battchikova N, Jonak C, Wirthmueller L, Wrzaczek M, Shapiguzov A, Kangasj, ä, rvi J, Poly(ADP-ribose)-binding protein RCD1 is a plant PARylation reader regulated by Photoregulatory Protein Kinases. Commun Biol, 6(1):429(2023) [pubmed]

submitter keyword: PPK,Arabidopsis, RCD1, phosphorylation

Jaakko Kangasjärvi
contact affiliation	Organismal and Evolutionary Biology Research Programme, Faculty of Biological and Environmental Sciences, and Viikki Plant Science Center, University of Helsinki, Helsinki, Finland
contact email	jaakko.kangasjarvi@helsinki.fi
lab head
Julia Vainonen
contact affiliation	University of Helsinki
contact email	julia.vainonen@helsinki.fi
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2023/04/PXD039877

PRIDE project URI

• PRIDE
  1. PXD039877
     1. Label: PRIDE project
     2. Name: Phosphorylation of RADICAL-INDUCED CELL DEATH1 by Photoregulatory Protein Kinases