Selective regulation of the chitin‐induced defense response by the Arabidopsis receptor‐like cytoplasmic kinase PBL27. (23rd May 2014)

• Record Type: Journal Article
• Authors: Shinya, Tomonori; Yamaguchi, Koji; Desaki, Yoshitake; Yamada, Kenta; Narisawa, Tomoko; Kobayashi, Yoshihiro; Maeda, Kanako; Suzuki, Maruya; Tanimoto, Takumi; Takeda, Jun; Nakashima, Masato; Funama, Ryota; Narusaka, Mari; Narusaka, Yoshihiro; Kaku, Hanae; Kawasaki, Tsutomu; Shibuya, Naoto
• Is Part Of: Plant journal. Volume 79:Number 1(2014:Jul.)
• Page Start: 56
• Page End: 66
• Publication Date: 2014-05-23
• Subjects: Plant molecular biology -- Periodicals; Plant cells and tissues -- Periodicals; Botany -- Periodicals; 580
• DOI: 10.1111/tpj.12535
• Languages: English
• ISSNs: 0960-7412

Abstract

<abstract abstract-type="main" id="tpj12535-abs-0001"> <title>Summary</title> <p>Recognition of microbe‐associated molecular patterns (MAMPs) initiates pattern‐triggered immunity in host plants. Pattern recognition receptors (PRRs) and receptor‐like cytoplasmic kinases (RLCKs) are the major components required for sensing and transduction of these molecular patterns. However, the regulation of RLCKs by PRRs and their specificity remain obscure. In this study we show that PBL27, an Arabidopsis ortholog of OsRLCK185, is an immediate downstream component of the chitin receptor CERK1 and contributes to the regulation of chitin‐induced immunity in Arabidopsis. Knockout of PBL27 resulted in the suppression of several chitin‐induced defense responses, including the activation of MPK3/6 and callose deposition as well as in disease resistance against fungal and bacterial infections. On the other hand, the contribution of PBL27 to flg22 signaling appears to be very limited, suggesting that PBL27 selectively regulates defense signaling downstream of specific PRR complexes. <italic>In vitro</italic> phosphorylation experiments showed that CERK1 preferentially phosphorylated PBL27 in comparison to BIK1, whereas phosphorylation of PBL27 by BAK1 was very low compared with that of BIK1. Thus, the substrate specificity of the signaling receptor‐like kinases, CERK1 and BAK1, may determine the preference of downstream RLCKs.</p> </abstract>