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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
PubMed

Insights

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.

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.

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