Proteomics

Dataset Information

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Identification of DDX6 ubiquitylated lysines in cAMP-stimulated cells. stimulation


ABSTRACT: DDX6 is an RNA helicase mostly located in the P-bodies, membrane-less organelles that play a fundamental role in the post-transcriptional regulation of gene expression. We found that stimulation of the G protein-coupled receptor (GPCR)-cAMP pathway induces a non-proteolytic polyubiquitylation of DDX6 mediated by the RING E3 ligase Praja2. To identify potential lysine residues of DDX6 accepting ubiquitin moieties mediated by Praja2, we performed a proteomic analysis on DDX6 purified from total lysates from cells treated with Forskolin, a diterpene that raises cAMP levels. The analysis identified K26 and K286 as ubiquitylated sites upon cAMP stimulation.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell

SUBMITTER: Luc Camoin  

LAB HEAD: Luc Camoin

PROVIDER: PXD054750 | Pride | 2025-05-26

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
DDX6_FSK_Rep1.raw Raw
DDX6_FSK_Rep2_20230420142346.raw Raw
DDX6_FSK_Rep3.raw Raw
DDX6_FSK_siPja2_Rep1.raw Raw
DDX6_FSK_siPja2_Rep2.raw Raw
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Publications


Glioblastoma multiforme (GBM) is the most lethal form of malignant brain tumor in adults. Dysregulation of protein synthesis contributes to cancer cell plasticity, driving GBM cell heterogeneity, metastatic behavior, and drug resistance. Understanding the complex network and signaling pathways governing protein translation, is therefore an important goal for GBM treatment. Here we identify a novel signaling network centered on the E3 ubiquitin ligase praja2 that controls protein translation in G  ...[more]

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