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First published online December 24, 2008; 10.1104/pp.108.128298 Plant Physiology 149:1478-1492 (2009) © 2009 American Society of Plant Biologists OPEN ACCESS ARTICLE
A Rice Kinase-Protein Interaction Map1,[W],[OA]Department of Plant Pathology (X.D., Y.Z., X.C., W.-Y.S.) and Interdisciplinary Center for Biotechnology Research (F.Y., W.G.F.), University of Florida, Gainesville, Florida 32611; Department of Plant Pathology, University of California, Davis, California 95616 (T.R., Y.S.S., L.E.B., M.C., R.B., P.C.R.); Plant Science Initiative, University of Nebraska, Lincoln, Nebraska 68588 (M.C., M.E.F.); Botany and Plant Sciences, University of California, Riverside, California 92521 (H.F., M.X., X.Z., S.K., R.A.S., J.-K.Z.); United States Department of Agriculture-Agricultural Research Service, Appalachian Fruit Research Station, Kearneysville, West Virginia 25430 (C.D.); Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907 (Y.L., H.J., M.G.); and Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China (L.Z.)
Plants uniquely contain large numbers of protein kinases, and for the vast majority of the 1,429 kinases predicted in the rice (Oryza sativa) genome, little is known of their functions. Genetic approaches often fail to produce observable phenotypes; thus, new strategies are needed to delineate kinase function. We previously developed a cost-effective high-throughput yeast two-hybrid system. Using this system, we have generated a protein interaction map of 116 representative rice kinases and 254 of their interacting proteins. Overall, the resulting interaction map supports a large number of known or predicted kinase-protein interactions from both plants and animals and reveals many new functional insights. Notably, we found a potential widespread role for E3 ubiquitin ligases in pathogen defense signaling mediated by receptor-like kinases, particularly by the kinases that may have evolved from recently expanded kinase subfamilies in rice. We anticipate that the data provided here will serve as a foundation for targeted functional studies in rice and other plants. The application of yeast two-hybrid and TAPtag analyses for large-scale plant protein interaction studies is also discussed.
1 This work was supported by the National Science Foundation (Plant Genome grant no. DBI–0217312). 2 Present address: Plant Biotech Institute, NRC, 110 Gymnasium Place, Saskatoon, Saskatchewan, Canada S7N 0W9. The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Wen-Yuan Song (wsong{at}ifas.ufl.edu). [W] The online version of this article contains Web-only data. [OA] Open Access articles can be viewed online without a subscription. www.plantphysiol.org/cgi/doi/10.1104/pp.108.128298 * Corresponding author; e-mail wsong{at}ifas.ufl.edu. Received August 20, 2008; accepted December 18, 2008; published December 24, 2008.
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