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Related Experiment Video

Updated: May 28, 2026

Electrophoretic Mobility Shift Assay (EMSA) for the Study of RNA-Protein Interactions: The IRE/IRP Example

Electrophoretic Mobility Shift Assay (EMSA) for the Study of RNA-Protein Interactions: The IRE/IRP Example

Published on: December 3, 2014

Sam68 interacts with IRS1.

R Quintana-Portillo¹, A Canfrán-Duque, T Issad

¹Department of Clinical Biochemistry, Virgen Macarena University Hospital, University of Seville, Spain.

Biochemical Pharmacology

|October 19, 2011

Summary

Sam68 protein interacts with IRS-1 in basal conditions. Insulin enhances this association, highlighting Sam68's role in early insulin receptor signaling.

Area of Science:

Cellular Biology
Molecular Signaling
Biochemistry

Background:

Sam68 (Src associated in mitosis) is an RNA-binding protein involved in linking cellular signaling to RNA processing.
Previous research indicated insulin promotes Sam68 cytoplasmic relocalization, associating it with signaling molecules and positively modulating insulin action.

Purpose of the Study:

To elucidate the role of Sam68 in the initial stages of insulin receptor (IR) signaling.
To investigate the interaction between Sam68 and IRS-1 under basal and insulin-stimulated conditions.

Main Methods:

Bioluminescence Resonance Energy Transfer (BRET) assays, including BRET saturation experiments.
Co-immunoprecipitation assays.
Utilized various Sam68 mutants to map interaction domains.

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A High Resolution Method to Monitor Phosphorylation-dependent Activation of IRF3

A High Resolution Method to Monitor Phosphorylation-dependent Activation of IRF3

Published on: January 24, 2016

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Last Updated: May 28, 2026

Electrophoretic Mobility Shift Assay (EMSA) for the Study of RNA-Protein Interactions: The IRE/IRP Example

Electrophoretic Mobility Shift Assay (EMSA) for the Study of RNA-Protein Interactions: The IRE/IRP Example

Published on: December 3, 2014

A High Resolution Method to Monitor Phosphorylation-dependent Activation of IRF3

A High Resolution Method to Monitor Phosphorylation-dependent Activation of IRF3

Published on: January 24, 2016

Main Results:

Demonstrated for the first time that Sam68 associates with IRS-1 in basal conditions.
Identified proline-rich domains (P0-P5) in Sam68 as important for IRS-1 binding affinity.
Showed that insulin significantly increases the binding affinity between Sam68 and IRS-1 in HEK-293 cells.

Conclusions:

Sam68 directly interacts with IRS-1 in basal conditions.
Insulin enhances the affinity of the Sam68-IRS-1 interaction, suggesting a role in early IR signal transduction.