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Receptor serine/threonine protein kinases in signalling: analysis of the erecta receptor‐like kinase of Arabidopsis thaliana
Author(s) -
Lease Kevin A.,
Lau Nelson Y.,
Schuster Robert A.,
Torii Keiko U.,
Walker John C.
Publication year - 2001
Publication title -
new phytologist
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.742
H-Index - 244
eISSN - 1469-8137
pISSN - 0028-646X
DOI - 10.1046/j.1469-8137.2001.00150.x
Subject(s) - biology , protein kinase domain , leucine rich repeat , kinase , akt3 , sh3 domain , arabidopsis thaliana , protein kinase a , c raf , serine , arabidopsis , map2k7 , genetics , microbiology and biotechnology , threonine , gene , biochemistry , phosphorylation , mitogen activated protein kinase kinase , cyclin dependent kinase 2 , proto oncogene tyrosine protein kinase src , mutant
Summary The Arabidopsis ERECTA (ER) gene regulates elongation of above‐ground organs. ER encodes a member of the leucine‐rich repeats–receptor‐like protein kinases (LRR–RLK) gene family, with the predicted protein containing a signal peptide, 20 leucine‐rich repeats in the extracellular domain, a transmembrane domain, and a cytoplasmic serine/threonine protein kinase domain. The structural features of the predicted ER protein suggest its role in cell–cell signalling is through phosphorylating serine/threonine residues. Consistent with this hypothesis, in vitro protein kinase analysis indicates that ER is a functional serine/threonine protein kinase. Furthermore, a large‐scale genetic screen was conducted to analyse new mutations in the erecta gene; 16 new er alleles were isolated, all of which were recessive. Here we present the identification of molecular lesions of seven alleles of er , which suggests the hypothesis that ERECTA might employ a mode of action distinct from other RLKs such as Xa21 or CLAVATA1, which function in disease resistance and developmental pathways, respectively.