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Related Experiment Videos

Bestrophin interacts physically and functionally with protein phosphatase 2A.

Lihua Y Marmorstein1, Precious J McLaughlin, J Brett Stanton

  • 1Department of Ophthalmic Research, Cole Eye Institute, The Cleveland Clinic Foundation, 9500 Euclid Avenue, Cleveland, OH 44195, USA.

The Journal of Biological Chemistry
|June 12, 2002
PubMed
Summary
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Bestrophin, a protein linked to Best macular dystrophy, interacts with protein phosphatase 2A (PP2A). This interaction suggests bestrophin is regulated by phosphorylation, impacting retinal function.

Area of Science:

  • Ophthalmology
  • Cell Biology
  • Molecular Biology

Background:

  • Bestrophin is a basolateral plasma membrane protein in retinal pigment epithelial cells (RPE).
  • Mutations in the VMD2 gene encoding bestrophin cause Best macular dystrophy, characterized by an abnormal electrooculogram light peak.
  • Bestrophin's role as a chloride channel in generating the electrooculogram light peak has been proposed.

Purpose of the Study:

  • To investigate the function and regulation of bestrophin.
  • To identify proteins interacting with bestrophin in RPE cells.
  • To elucidate the role of phosphorylation in bestrophin's function.

Main Methods:

  • Immunoaffinity purification of the bestrophin complex from RPE lysates.
  • Matrix-assisted laser desorption ionization time-of-flight mass spectrometry to identify complex members.

Related Experiment Videos

  • Reciprocal immunoprecipitation and pulldown assays to confirm protein-protein interactions.
  • In vitro dephosphorylation assays using purified PP2A.

    • Main Results:

    • Bestrophin and the beta-catalytic subunit of protein phosphatase 2A (PP2A) were identified as components of the bestrophin complex.
    • Protein-protein interaction between bestrophin and PP2A subunits (PP2Ac and PR65) was confirmed.
    • Bestrophin phosphorylation, sensitive to okadaic acid, was observed in RPE-J cells and dephosphorylated by purified PP2A in vitro.

    Conclusions:

    • Bestrophin is part of a signal transduction pathway modulating the electrooculogram light peak.
    • Bestrophin function is regulated by phosphorylation.
    • Protein phosphatase 2A (PP2A) regulates bestrophin phosphorylation, suggesting a novel regulatory mechanism in RPE cells.