TY - JOUR
T1 - Plasma membrane calcium ATPase activity is regulated by actin oligomers through direct interaction
AU - Dalghi, Marianela G.
AU - Fernández, Marisa M.
AU - Ferreira-Gomes, Mariela
AU - Mangialavori, Irene C.
AU - Malchiodi, Emilio L.
AU - Strehler, Emanuel E.
AU - Rossi, Juan Pablo F.C.
PY - 2013/8/9
Y1 - 2013/8/9
N2 - 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.
AB - 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.
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U2 - 10.1074/jbc.M113.470542
DO - 10.1074/jbc.M113.470542
M3 - Article
C2 - 23803603
AN - SCOPUS:84881469078
SN - 0021-9258
VL - 288
SP - 23380
EP - 23393
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 32
ER -