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Plant Physiology Preview Published on July 30, 2008; 10.1104/pp.108.123216
Received May 22, 2008 The Arabidopsis SERK proteins serve brassinosteroid dependent and independent signaling pathways
Laboratory of Biochemistry, Wageningen University, Dreijenlaan 3, 6703 HA Wageningen, The Netherlands; Present address: VIB Department of Plant Systems Biology, Ghent University, Technologiepark 927, 9052 Ghent, Belgium; Institute of Plant Biochemistry, ZMBP, University of Tuebingen, Auf der Morgenstelle 5, 72076 Tuebingen, Germany; Present address: Max Planck Institute for Plant Breeding Research, Department for Plant-Microbe Interactions, Carl van Linne weg 10, 50829, Cologne, Germany * Corresponding author; email: catherine.albrecht{at}wur.nl.
The Arabidopsis SERK genes belong to a small family of 5 plant receptor kinases that are involved in at least 5 different signaling pathways. One member of this family, BAK1, also known as SERK3, is the co-receptor of the brassinolide perceiving receptor BRI1, a function that is BR dependent and partially redundant with SERK1. BAK1 (SERK3) alone controls plant innate immunity, is also the co-receptor of the flagellin receptor FLS2 and together with SERK4 can mediate cell death control, all three in a BR-independent fashion. SERK1 and SERK2 are essential for male microsporogenesis, again independent from BR. SERK5 does not appear to have any function under the conditions tested. Here we show that the different SERK members are only redundant in pairs while higher order mutant combinations only show additive phenotypes. Surprisingly, SERK members that are redundant within one are not redundant in another pathway. We also show that this evolution of functional pairs occurred by a change in protein function and not by differences in spatial expression. We propose that in plants closely related receptor kinases have a minimal homo- or heterodimeric configuration to achieve specificity.
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