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Originally published as MBC in Press, 10.1091/mbc.E02-09-0591 on March 20, 2003

Vol. 14, Issue 7, 2935-2945, July 2003

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Essential role of Ca2+/Calmodulin in Early Endosome Antigen-1 Localization

Deirdre C. Lawe *, Nachida Sitouah *, Susan Hayes {dagger}, Anil Chawla * {ddagger}, Joseph V. Virbasius * {ddagger}, Richard Tuft §, Kevin Fogarty §, Lawrence Lifshitz §, David Lambright * {dagger} {ddagger}, and Silvia Corvera * {dagger} ||

* Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, Massachusetts 10615; {dagger} Interdisciplinary Graduate Program, University of Massachusetts Medical School, Worcester, Massachusetts 10615; {ddagger} Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts 10615; and § Department of Physiology, University of Massachusetts Medical School, Worcester, Massachusetts 10615

Submitted September 14, 2002; Revised February 14, 2003; Accepted February 15, 2003
Monitoring Editor: Keith Mostov

Ca2+ is an essential requirement in membrane fusion, acting through binding proteins such as calmodulin (CaM). Ca2+/CaM is required for early endosome fusion in vitro, however, the molecular basis for this requirement is unknown. An additional requirement for endosome fusion is the protein Early Endosome Antigen 1 (EEA1), and its recruitment to the endosome depends on phosphatidylinositol 3-phosphate [PI(3)P] and the Rab5 GTPase. Herein, we demonstrate that inhibition of Ca2+/CaM, by using either chemical inhibitors or specific antibodies directed to CaM, results in a profound inhibition of EEA1 binding to endosomal membranes both in live cells and in vitro. The concentration of Ca2+/CaM inhibitors required for a full dissociation of EEA1 from endosomal membranes had no effect on the activity of phosphatidylinositol 3-kinases or on endogenous levels of PI(3)P. However, the interaction of EEA1 with liposomes containing PI(3)P was decreased by Ca2+/CaM inhibitors. Thus, Ca2+/CaM seems to be required for the stable interaction of EEA1 with endosomal PI(3)P, perhaps by directly or indirectly stabilizing the quaternary organization of the C-terminal FYVE domain of EEA1. This requirement is likely to underlie at least in part the essential role of Ca2+/CaM in endosome fusion.

The online version of this article contains video material for some figures. Online version is available at silvia.corvera{at}umassmed.edu.

|| Corresponding author. E-mail address: silvia.corvera{at}umassmed.edu.




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