Proteomics

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Phosphorylation of RADICAL-INDUCED CELL DEATH1 by Photoregulatory Protein Kinases


ABSTRACT: 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.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

SUBMITTER: Julia Vainonen  

LAB HEAD: Jaakko Kangasjärvi

PROVIDER: PXD039877 | Pride | 2023-04-21

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
130411_JV3_IP.msf Msf
130411_JV3_IP.mzML Mzml
130411_JV3_IP.raw Raw
130411_JV4_IP.msf Msf
130411_JV4_IP.mzML Mzml
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Publications

Poly(ADP-ribose)-binding protein RCD1 is a plant PARylation reader regulated by Photoregulatory Protein Kinases.

Vainonen Julia P JP   Gossens Richard R   Krasensky-Wrzaczek Julia J   De Masi Raffaella R   Danciu Iulia I   Puukko Tuomas T   Battchikova Natalia N   Jonak Claudia C   Wirthmueller Lennart L   Wrzaczek Michael M   Shapiguzov Alexey A   Kangasjärvi Jaakko J  

Communications biology 20230419 1


Poly(ADP-ribosyl)ation (PARylation) is a reversible post-translational protein modification that has profound regulatory functions in metabolism, development and immunity, and is conserved throughout the eukaryotic lineage. Contrary to metazoa, many components and mechanistic details of PARylation have remained unidentified in plants. Here we present the transcriptional co-regulator RADICAL-INDUCED CELL DEATH1 (RCD1) as a plant PAR-reader. RCD1 is a multidomain protein with intrinsically disorde  ...[more]

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