Proteomics

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Phosphoproteomic analysis of signaling downstream of p85β

ABSTRACT: p85β is a regulatory subunit of phosphatidylinositol 3-kinase. The signaling mechanism of p85β is poorly understood. Quantitative mass spectrometry-based phosphoproteomic analysis was therefore performed to reveal proteins with an altered phosphorylation status upon PIK3R2 depletion in ovarian cancer cell line SKOV3. This profiling yielded 90 unique altered phosphopeptides, mapping to 29 and 45 proteins whose levels were downregulated or upregulated at P<0.05 by PIK3R2-specific siRNA, respectively. We observed significant enrichment of proteins in ubiquitin-mediated proteolysis and autophagy regulation, suggesting a role of p85β in regulating these cellular processes.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Ovary

DISEASE(S): Malignant Neoplasm Of Ovary

SUBMITTER: Lydia Cheung  

LAB HEAD: Dr CHEUNG, Lydia Wai Ting

PROVIDER: PXD018449 | Pride | 2020-05-08

REPOSITORIES: Pride

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Action DRS
DMSO_NS_2.raw Raw
DMSO_NS_2_total.raw Raw
DMSO_Si_2.raw Raw
DMSO_Si_2_total.raw Raw
PhosphoSTYSites.txt Txt
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Publications

PIK3R2 encodes the p85β regulatory subunit of phosphatidylinositol 3-kinase and is frequently amplified in cancers. The signaling mechanism and therapeutic implication of p85β are poorly understood. Here we report that p85β upregulates the protein level of the receptor tyrosine kinase AXL to induce oncogenic signaling in ovarian cancer. p85β activates p110 activity and AKT-independent PDK1/SGK3 signaling to promote tumorigenic phenotypes, which are all abolished upon inhibition of AXL. At the mo  ...[more]

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