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Related Experiment Video

Updated: Jul 6, 2026

Identification of Protein Interaction Partners in Mammalian Cells Using SILAC-immunoprecipitation Quantitative Proteomics

Identification of Protein Interaction Partners in Mammalian Cells Using SILAC-immunoprecipitation Quantitative Proteomics

Published on: July 6, 2014

Mapping the integrin-linked kinase interactome using SILAC.

Iveta Dobreva¹, Andrew Fielding, Leonard J Foster

¹Department of Cancer Genetics, British Columbia Cancer Research Centre, 675 West 10th Avenue, V5Z 1L3, Vancouver, BC, Canada.

Journal of Proteome Research

|March 11, 2008

Summary

This summary is machine-generated.

This study identifies new proteins that interact with integrin-linked kinase (ILK), revealing how ILK controls cell signaling. These findings enhance our understanding of ILK

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Identification of Protein Interaction Partners in Mammalian Cells Using SILAC-immunoprecipitation Quantitative Proteomics

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Published on: July 6, 2014

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Published on: November 18, 2014

Area of Science:

Cell Biology
Molecular Biology
Proteomics

Background:

Integrin-linked kinase (ILK) is crucial for regulating cell functions like migration and survival.
The precise mechanisms by which ILK integrates and controls complex cellular signals remain unclear.
A comprehensive analysis of ILK-protein interactions is needed to understand ILK-dependent signal transduction.

Purpose of the Study:

To identify novel ILK-interacting proteins using a quantitative proteomics approach.
To gain insights into the complex network of ILK-dependent signaling pathways.
To elucidate the molecular mechanisms underlying ILK's regulatory functions.

Main Methods:

Stable Isotope Labeling with Amino acids in cell culture (SILAC)-based proteomics.
Immunoprecipitation of ILK followed by mass spectrometry.
Co-immunoprecipitation/Western blot and colocalization experiments for validation.

Main Results:

Identified 752 proteins interacting with ILK, with 24 novel partners showing significant enrichment.
Discovered interactions with Rictor, tubulin, RuvB-like 1 and 2, HAX-1, T-complex protein 1 subunits, and IQ-GAP1.
Demonstrated that ILK can form distinct protein complexes and regulates RuvB-like 1/tubulin interaction.

Conclusions:

Quantitative proteomics successfully identified novel ILK-binding proteins.
These findings provide new insights into the molecular mechanisms of ILK-dependent signal transduction.
ILK's ability to form distinct complexes and regulate protein interactions highlights its versatile role in cellular processes.