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CELL BIOLOGY AND SIGNAL TRANSDUCTION

Interaction of Calmodulin, a Sorting Nexin and Kinase-Associated Protein Phosphatase with the Brassica oleracea S Locus Receptor Kinase

Reproduction et Développement des Plantes, Unité Mixte de Recherche 5667, Centre National de la Recherche Scientifique-Institut National de la Recherche Agronomique-Ecole Normale Supérieure de Lyon-Université Claude Bernard Lyon, Ecole Normale Supérieure de Lyon, 46 Allée d'Italie, 69364 Lyon cedex 07, France

Recognition of self-pollen during the self-incompatibility response in Brassica oleracea is mediated by the binding of a secreted peptide (the S locus cysteine-rich protein) to the S locus receptor kinase (SRK), a member of the plant receptor kinase (PRK) superfamily. Here, we describe the characterization of three proteins that interact with the cytosolic kinase domain of SRK. A B. oleracea homolog of Arabidopsis kinase-associated protein phosphatase was shown to interact with and dephosphorylate SRK and was itself phosphorylated by SRK. Yeast (Saccharomyces cerevisiae) two-hybrid screens identified two additional interactors, calmodulin and a sorting nexin, both of which have been implicated in receptor kinase down-regulation in animals. A calmodulin-binding site was identified in sub-domain VIa of the SRK kinase domain. The binding site is conserved and functional in several other members of the PRK family. The sorting nexin also interacted with diverse members of the PRK family, suggesting that all three of the interacting proteins described here may play a general role in signal transduction by this family of proteins.

¹ Present address: Swann Building, Institute of Cell and Molecular Biology, King's Buildings, University of Edinburgh, Mayfield Road, Edinburgh EH9 3JR, UK.

² Present address: Unité Mixte de Recherche 7139, Centre National de la Recherche Scientifique-Goëmar-Université Paris 6, Station Biologique, Place Georges Teissier, BP 74, 29682 Roscoff Cedex, France

^* Corresponding author; e-mail cock{at}sb-roscoff.fr; fax 33–2–9829–2324.

Received March 19, 2003; returned for revision April 15, 2003; accepted June 23, 2003.

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