Proteomics

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HeLa phosphoproteome regulated by PP2A related proteins

ABSTRACT: HeLa cells were treated with siRNAs of PP2A related proteins or with okadaic acid, in triplicates. Tryptic digests of extracted proteins were analyzed using a Q Exactive mass spectrometer, before and after TiO2 phosphopeptide enrichment. Data were searched with Mascot via Proteome Discoverer. For phosphorylation site localization, phosphoRS was enabled. In parallel, SpectraST searching was performed via Proteome Discoverer, against an in-house made spectral library of phosphopeptides simulated using SimPhospho software.

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Susumu Y. Imanishi 

PROVIDER: PXD016102 | JPOST Repository | Wed Feb 19 00:00:00 GMT 2020

REPOSITORIES: jPOST

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Action DRS
120424_14_PTPA_X_TiO2_45_10MS2_110min.raw Raw
120424_16_PTPA_Y_TiO2_45_10MS2_110min.raw Raw
120424_18_PTPA_Z_TiO2_45_10MS2_110min.raw Raw
120424_20_5C_X_TiO2_45_10MS2_110min.raw Raw
120424_22_5C_Y_TiO2_45_10MS2_110min.raw Raw
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Publications

Protein phosphatase 2A (PP2A) critically regulates cell signaling and is a human tumor suppressor. PP2A complexes are modulated by proteins such as cancerous inhibitor of protein phosphatase 2A (CIP2A), protein phosphatase methylesterase 1 (PME-1), and SET nuclear proto-oncogene (SET) that often are deregulated in cancers. However, how they impact cellular phosphorylation and how redundant they are in cellular regulation is poorly understood. Here, we conducted a systematic phosphoproteomics scr  ...[more]

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