Regulation of Arabidopsis defense responses against Spodoptera littoralisby CPK-mediated calcium signaling

BMC Plant Biology

Research Article

Yaeta Endo¹  Tatsuya Sawasaki¹  Junji Takabayashi²  Hirotaka Takahashi³  Stefano Quadro⁴  Wilhelm Boland⁴  Gen-ichiro Arimura⁵  Atsushi Muroi⁵  Chidananda Nagamangala Kanchiswamy⁶  Nobuaki Ishihama⁷  Hirofumi Yoshioka⁷  Simone Bossi⁸  Massimo E Maffei⁸  Simon Atsbaha Zebelo⁸  Cinzia Bertea⁸ 

[1]Cell-free Science and Technology Research Center, Ehime University, 790-8577, Matsuyama, Japan

[2]Center for Ecological Research, Kyoto University, 520-2113, Otsu, Japan

[3]Current Address:Department of Microbiology, Yong Loo Lin School of Medicine, National University of Singapore, 117597, Singapore, Singapore

[4]Cell-free Science and Technology Research Center, Ehime University, 790-8577, Matsuyama, Japan

[5]Department of Bioorganic Chemistry, Max Planck Institute for Chemical Ecology, 07745, Germany

[6]Global COE Program: Evolution and Biodiversity, Graduate School of Science, Kyoto University, 606-8502, Kyoto, Japan

[7]Center for Ecological Research, Kyoto University, 520-2113, Otsu, Japan

[8]Global COE Program: Evolution and Biodiversity, Graduate School of Science, Kyoto University, 606-8502, Kyoto, Japan

[9]Center for Ecological Research, Kyoto University, 520-2113, Otsu, Japan

[10]Plant Physiology Unit, Department of Plant Biology and Innovation Centre, University of Turin, 10135, Turin, Italy

[11]Graduate School of Bioagricultural Sciences, Nagoya University, 464-8601, Nagoya, Japan

[12]Plant Physiology Unit, Department of Plant Biology and Innovation Centre, University of Turin, 10135, Turin, Italy

关键词: Jasmonic Acid;    Ethephon;    Heat Shock Factor;    BAPTA;    Onion Peel;   

DOI  :  10.1186/1471-2229-10-97

 received in 2010-01-07, accepted in 2010-05-26,  发布年份 2010

来源: Springer

【 摘 要 】

BackgroundPlant Ca2+ signals are involved in a wide array of intracellular signaling pathways after pest invasion. Ca2+-binding sensory proteins such as Ca2+-dependent protein kinases (CPKs) have been predicted to mediate the signaling following Ca2+ influx after insect herbivory. However, until now this prediction was not testable.ResultsTo investigate the roles CPKs play in a herbivore response-signaling pathway, we screened the characteristics of Arabidopsis CPK mutants damaged by a feeding generalist herbivore, Spodoptera littoralis. Following insect attack, the cpk3 and cpk13 mutants showed lower transcript levels of plant defensin gene PDF1.2 compared to wild-type plants. The CPK cascade was not directly linked to the herbivory-induced signaling pathways that were mediated by defense-related phytohormones such as jasmonic acid and ethylene. CPK3 was also suggested to be involved in a negative feedback regulation of the cytosolic Ca2+ levels after herbivory and wounding damage. In vitro kinase assays of CPK3 protein with a suite of substrates demonstrated that the protein phosphorylates transcription factors (including ERF1, HsfB2a and CZF1/ZFAR1) in the presence of Ca2+. CPK13 strongly phosphorylated only HsfB2a, irrespective of the presence of Ca2+. Furthermore, in vivo agroinfiltration assays showed that CPK3-or CPK13-derived phosphorylation of a heat shock factor (HsfB2a) promotes PDF1.2 transcriptional activation in the defense response.ConclusionsThese results reveal the involvement of two Arabidopsis CPKs (CPK3 and CPK13) in the herbivory-induced signaling network via HsfB2a-mediated regulation of the defense-related transcriptional machinery. This cascade is not involved in the phytohormone-related signaling pathways, but rather directly impacts transcription factors for defense responses.

【 授权许可】

Unknown   
© Kanchiswamy et al; licensee BioMed Central Ltd. 2010. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.