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Related Experiment Video

Updated: Jun 21, 2026

An Immunofluorescent Method for Characterization of Barrett’s Esophagus Cells

An Immunofluorescent Method for Characterization of Barrett’s Esophagus Cells

Published on: July 20, 2014

The PDZ protein MPP2 interacts with c-Src in epithelial cells.

Martin Baumgartner¹, Andreas Weiss, Thorsten Fritzius

¹Institute of Medical Virology, University of Zürich, Zürich, Switzerland. Martin.Baumgartner@mopa.unibe.ch

Experimental Cell Research

|August 12, 2009

Summary

Membrane Protein Palmitoylated 2 (MPP2) restricts Src activity by interacting with c-Src, a non-receptor tyrosine kinase. This interaction helps regulate cell morphology and suppress Src-driven cytoskeletal disorganization in epithelial cells.

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Methods to Study Mrp4-containing Macromolecular Complexes in the Regulation of Fibroblast Migration

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Published on: May 19, 2016

Area of Science:

Cellular Biology
Molecular Oncology
Biochemistry

Background:

c-Src, a non-receptor tyrosine kinase, regulates critical cellular processes like proliferation, migration, and invasion.
Protein-protein interactions, particularly with PDZ proteins, represent a novel mechanism for controlling c-Src activity.
The specific PDZ protein MPP2 and its functional role in regulating c-Src remain largely uncharacterized.

Purpose of the Study:

To identify and characterize PDZ proteins that interact with c-Src.
To elucidate the functional significance of the interaction between MPP2 and c-Src in controlling kinase activity and cellular morphology.

Main Methods:

PDZ domain array screening was employed to identify interacting PDZ proteins.
Co-localization studies using immunofluorescence microscopy were performed in MCF-10A cells.
Cellular kinase activity assays and actin cytoskeleton organization assessments were conducted.

Main Results:

The PDZ protein MPP2 was identified as an interactor of c-Src.
MPP2 associates with the cytoskeleton and co-localizes with microtubules and c-Src in epithelial cells.
MPP2 negatively regulates c-Src kinase activity and suppresses c-Src-dependent disruption of the cortical actin cytoskeleton.

Conclusions:

MPP2 interacts with c-Src to restrict its kinase activity.
The MPP2-c-Src interaction plays a crucial role in maintaining epithelial cell morphology.
MPP2 serves as a negative regulator of c-Src, impacting cellular functions and cytoskeletal organization.