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Published on December 24, 2008; 10.1104/pp.108.128298

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Received August 20, 2008
Accepted December 18, 2008

A Rice Kinase-Protein Interaction Map

Xiaodong Ding , Todd Richter , Mei Chen , Hiroaki Fujii , Young Su Seo , Mingtang Xie , Xianwu Zheng , Siddhartha Kanrar , Rebecca A. Stevenson , Christopher Dardick , Ying Li , Hao Jiang , Yan Zhang , Fahong Yu , Laura E. Bartley , Mawsheng Chern , Rebecca Bart , Xiuhua Chen , Lihuang Zhu , William G. Farmerie , Michael Gribskov , Jian-Kang Zhu , Michael E. Fromm , Pamela C. Ronald , and Wen-Yuan Song *

Department of Plant Pathology, University of Florida, Gainesville, FL 32611, USA; Department of Plant Pathology, University of California, Davis, CA 95616, USA; Plant Science Initiative, University of Nebraska, Lincoln, NE 68588, USA; Botany and Plant Sciences, University of California, Riverside, CA 92521, USA; USDA-ARS, Appalachian Fruit Research Station, Kearneysville, West Virginia, 25430, USA; Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA; Interdisciplinary Center for Biotechnology Research, University of Florida, Gainesville, FL 32611, USA; Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China

* Corresponding author; email: wsong{at}.ifas.ufl.edu.

Plants uniquely contain large numbers of protein kinases and, for the vast majority of the 1429 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 subfamiles 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.






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