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J. Biol. Chem., Vol. 279, Issue 49, 50643-50646, December 3, 2004

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Phosphorylation of Annexin I by TRPM7 Channel-Kinase^*

Maxim V. Dorovkov and Alexey G. Ryazanov

From the Department of Pharmacology, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854

TRPM7 is an unusual bifunctional molecule consisting of a TRP ion channel fused to a protein kinase domain. It has been shown that TRPM7 plays a key role in the regulation of intracellular magnesium homeostasis as well as in anoxic neuronal death. TRPM7 channel has been characterized using electrophysiological techniques; however, the function of the kinase domain is not known and endogenous substrates for the kinase have not been reported previously. Here we have identified annexin 1 as a substrate for TRPM7 kinase. Phosphorylation of annexin 1 by TRPM7 kinase is stimulated by Ca²⁺ and is dramatically increased in extracts from cells overexpressing TRPM7. Phosphorylation of annexin 1 by TRPM7 kinase occurs at a conserved serine residue (Ser⁵) located within the N-terminal amphipathic -helix of annexin 1. The N-terminal region plays a crucial role in interaction of annexin 1 with other proteins and membranes, and therefore, phosphorylation of annexin 1 at Ser⁵ by TRPM7 kinase may modulate function of annexin 1.

Received for publication, September 20, 2004 , and in revised form, October 12, 2004.

^* This work was supported by the National Institutes of Health Grants RO1 GM57300 and RO1 CA81102 (to A. G. R.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Pharmacology, UMDNJ-Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, NJ 08854. Tel.: 732-235-5526; Fax: 732-235-4073; E-mail: ryazanag{at}umdnj.edu.

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