PXD011089-1

PXD011089 is an original dataset announced via ProteomeXchange.

Title	Proximity assay of p38alpha MAPK reveals alternative splicing regulatory mechanism in cardiomyocyte.
Description	The mitogen-activated protein kinase (MAPK) p38 signaling pathway is essential for normal heart function. However, p38 also contributes to heart failure pathogenesis by affecting heart contractility and cardiomyocyte survival. To unravel the complex cardiac role of p38, we report the interactome of p38α and p38γ, the two well expressed isoforms in the heart, obtained via an APEX proximity assay performed in cultured neonatal rat ventricular myocytes. The p38α and p38γ have distinct interactomes in cardiomyocytes for both studied states; basal and activated by an osmotic stress. Interestingly, the activated p38α interactome contains many spliceosome implicated RNA-binding proteins. The serine/arginine-rich splicing factor 3 (SRSF3) is of particular interest and its interaction with p38α was validated by co-immunoprecipitation. p38 is sufficient to partially relocate nuclear SRSF3 to cytoplasm. The alternative splicing function of SRSF3 is also modulated by the p38 pathway. Our findings reveal a novel set of proteins to investigate in order to decipher cardiac functions of the MAPK p38, as well as a specific regulation mechanism of SRSF3 by p38 in cardiomyocytes.
HostingRepository	PRIDE
AnnounceDate	2021-03-01
AnnouncementXML	Submission_2021-02-28_22:17:27.984.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Mannix Auger-Messier
SpeciesList	scientific name: Rattus norvegicus (Rat); NCBI TaxID: 10116;
ModificationList	biotinylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2018-09-14 01:40:37	ID requested
⏵ 1	2021-02-28 22:17:29	announced
2	2024-10-22 05:19:32	announced	2024-10-22: Updated project metadata.

Dumont AA, Dumont L, Berthiaume J, Auger-Messier M, MAPK proximity assay reveals a regulatory mechanism of alternative splicing in cardiomyocytes. Biochim Biophys Acta Mol Cell Res, 1866(12):118557(2019) [pubmed]

curator keyword: Biological

submitter keyword: cardiomyocyte, p38 MAPK, SRSF3, splicing

Mannix Auger-Messier
contact affiliation	Département de médecine – Service de cardiologie, CRCHUS, FMSS, Université de Sherbrooke, Sherbrooke, QC, Canada
contact email	Mannix.Auger-Messier@USherbrooke.ca
lab head
Mannix Auger-Messier
contact affiliation	Université de Sherbrooke
contact email	Mannix.Auger-Messier@USherbrooke.ca
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD011089
     1. Label: PRIDE project
     2. Name: Proximity assay of p38alpha MAPK reveals alternative splicing regulatory mechanism in cardiomyocyte.