Plasma membrane calcium ATPase activity is regulated by actin oligomers through direct interaction

Abstract

Background: Plasma membrane calcium ATPases interact dynamically with the submembrane actin cytoskeleton. Results: Biophysical and functional assays show that purified plasma membrane calcium ATPase binds to G-actin and is activated by short actin oligomers. Conclusion: Plasma membrane calcium ATPases are regulated by polymerizing actin independently of regulation by calmodulin. Significance: Dynamic actin participates in cytosolic Ca2+ homeostasis by regulating plasma membrane calcium ATPase activity. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.