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Published on June 13, 2008; 10.1104/pp.108.123380

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Received May 22, 2008
Accepted June 8, 2008

Interactions between the S-Domain receptor kinases and AtPUB-ARM E3 ubiquitin ligases suggest a conserved signaling pathway in Arabidopsis

Marcus A. Samuel , Yashwanti Mudgil , Jennifer N. Salt , Fred Delmas , Shaliny Ramachandran , Andrea Chilelli , and Daphne R. Goring *

Department of Cell and Systems Biology, University of Toronto, Toronto, Ontario, Canada M5S 3B2

* Corresponding author; email: d.goring{at}utoronto.ca.

The Arabidopsis genome encompasses multiple receptor kinase families with highly variable extracellular domains. Despite their large numbers, the various ligands and the downstream interacting partners for these kinases have been deciphered only for a few members. One such member, the S Receptor Kinase (SRK), is known to mediate the self-incompatibility (SI) response in Brassica. SRK has been shown to interact and phosphorylate a U-box/ARM-repeat-containing E3 ligase, ARC1, which in turn acts as a positive regulator of the self-incompatibility response. In an effort to identify conserved signaling pathways in Arabidopsis, we performed yeast two-hybrid analyses of various S-Domain receptor kinase family members with representative Arabidopsis U-box/ARM-repeat (AtPUB-ARM) E3 ligases. The kinase domains from S-Domain receptor kinases were found to interact with ARM repeat domains from AtPUB-ARM proteins. These kinase domains along with MLPK (M-locus protein kinase), a positive regulator of SI response, were also able to phosphorylate the ARM repeat domains in in vitro phosphorylation assays. Subcellular localization patterns were investigated using transient expression assays in tobacco BY-2 cells, and changes were detected in the presence of interacting kinases. Finally, potential links to the involvement of these interacting modules to the hormone, abscisic acid (ABA), were investigated. Interestingly, AtPUB9 displayed a redistribution to the plasma membrane of BY-2 cells when either treated with ABA or co-expressed with the active kinase domain of ARK1. As well, T-DNA insertion mutants for ARK1 and AtPUB9 lines were altered in their ABA sensitivity during germination and acted at or upstream of ABI3, indicating a potential involvement of these proteins in ABA responses.




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