Phosphorylation of annexin I by TRPM7 channel-kinase - PubMed (original) (raw)

. 2004 Dec 3;279(49):50643-6.

doi: 10.1074/jbc.C400441200. Epub 2004 Oct 12.

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• PMID: 15485879
• DOI: 10.1074/jbc.C400441200

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Phosphorylation of annexin I by TRPM7 channel-kinase

Maxim V Dorovkov et al. J Biol Chem. 2004.

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Abstract

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 alpha-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.

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