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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
10:17

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

2.9K

Quantitative phosphoproteomic analysis of the PI3K-regulated signaling network

Florian Gnad1, Jeffrey Wallin2, Kyle Edgar2

  • 1Department of Bioinformatics and Computational Biology, Genentech Inc, South San Francisco, CA, USA.

Proteomics
|June 11, 2016
PubMed

Insights

This study reveals new phosphorylation sites in cancer-related proteins by analyzing the PI3K pathway. These findings enhance our understanding of PI3K signaling in cell growth and proliferation.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cancer Research

Background:

  • The phosphoinositide 3-kinase (PI3K) pathway is frequently dysregulated in various cancers.
  • Understanding downstream signaling is crucial for elucidating cancer mechanisms.

Purpose of the Study:

  • To comprehensively map phosphorylation signaling events downstream of PI3K.
  • To identify novel PI3K-regulated proteins and phosphorylation sites involved in oncogenesis.

Main Methods:

  • Mass spectrometry-based phosphoproteomics was employed.
  • Isogenic cell models and targeted inhibitors were used to study PIK3CA activation/inhibition.
  • Quantitative analysis of phosphorylation site responses was performed.

Main Results:

  • 2509 phosphorylation sites on 1096 proteins were identified and quantified.
  • Significant phosphorylation changes were observed in proteins regulating cell growth and proliferation.
  • Many newly identified proteins were linked to PI3K signaling.

Conclusions:

  • This phosphoproteomic analysis expands the known landscape of PI3K signaling.
  • The findings provide new targets and insights into PI3K-driven oncogenic processes.
  • Updated PHOSIDA database and public data deposition facilitate further research.
Keywords:
Cell BiologyPHOSIDAPI3KPhosphoproteomicsSignaling

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