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Updated: Feb 28, 2026

2 in 1: One-step Affinity Purification for the Parallel Analysis of Protein-Protein and Protein-Metabolite Complexes
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2 in 1: One-step Affinity Purification for the Parallel Analysis of Protein-Protein and Protein-Metabolite Complexes

Published on: August 6, 2018

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Dataset to delineate changes in association between Akt1 and its interacting partners as a function of active state

Nutan Gupta1, Shweta Duggal1, Noor Jailkhani1

  • 1International Centre for Genetic Engineering and Biotechnology (ICGEB), Aruna Asif Ali Marg, New Delhi 110067, India.

Data in Brief
|June 13, 2017
PubMed

Insights

This study explored the dynamic Akt1 interactome by comparing its native state to its inhibited form using SILAC and AP-MS. Findings reveal how Akt1 protein interactions change upon inhibition, offering insights for targeted cancer therapies.

Area of Science:

  • Molecular Biology
  • Proteomics
  • Cancer Research

Background:

  • The protein kinase Akt1 plays a crucial role in cell survival and is implicated in various human solid tumors.
  • Targeted therapies focusing on Akt1 are under development due to its significance in cancer progression.
  • Understanding the dynamic interactions of Akt1 is essential for comprehending its functional diversity and developing effective treatments.

Purpose of the Study:

  • To investigate the dynamic changes in the Akt1 interactome in response to its active state.
  • To delineate how Akt1 protein associations are altered upon inhibition of its active form.
  • To provide novel insights into the context-dependent nature of the Akt1 interactome.

Main Methods:

  • Utilized SILAC (Stable Isotope Labeling by Amino acids in Cell culture) for quantitative proteomic analysis.
  • Employed Affinity Purification coupled to Mass Spectrometry (AP-MS) to identify Akt1 interacting proteins.
  • Compared the Akt1 interactome in untreated HEK293 cells (light labeled) with cells treated with the allosteric inhibitor MK-2206 (heavy labeled).

Main Results:

  • Identified dynamic changes in protein associations with Akt1 based on its activation state.
  • Quantitatively assessed alterations in the Akt1 interactome upon inhibition with MK-2206.
  • Revealed context-specific interaction profiles of Akt1.

Conclusions:

  • The study provides a dynamic view of the Akt1 interactome, highlighting its context-dependent nature.
  • Understanding these dynamic interactome shifts can inform the development of targeted Akt1-based cancer therapies.
  • The findings contribute to a deeper comprehension of Akt1 signaling in cancer.
Keywords:
Affinity purificationAkt1InteractomeMass spectrometrySILAC

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