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Mol. Cells 2013; 35(1): 7-16

Published online December 21, 2012

https://doi.org/10.1007/s10059-013-2255-3

© The Korean Society for Molecular and Cellular Biology

Assessing the Diverse Functions of BAK1 and Its Homologs in Arabidopsis, beyond BR Signaling and PTI Responses

Beg Hab Kim, Sun Young Kim, and Kyoung Hee Nam*

Department of Biological Science, Sookmyung Women’s University, Seoul 140-742, Korea

Correspondence to : *Correspondence: khnam514@sookmyung.ac.kr

Received: October 2, 2012; Revised: November 9, 2012; Accepted: November 19, 2012

Abstract

Plants possess a variety of extracellular leucine-rich repeats receptor-like kinases (LRR-RLKs) to coordinate developmental programs with responses to environmental changes. Out of sixteen families of LRR-RLKs in Arabidopsis, the LRR-RLKII family consists of fourteen individual members, including five Arabidopsis thaliana somatic embryogenesis receptor kinases (AtSERKs). BAK1/AtSERK3 was first identified as a dual co-receptor of BRI1 and FLS2, mediating BR signaling and pathogen-associated molecular pattern (PAMP) triggered immunity (PTI), respectively. Since its identification, many researchers have attempted to elucidate the phosphorylation mechanisms between receptor complexes and identify additional components that interact with receptor complexes to transduce the signaling downstream. Relatively detailed early events in complex formation, phosphorylation sites on the BRI1/BAK1 complex and BAK1-interacting proteins, such as BIK1 and PUB13, have been identified. Small receptor complexes consisting of BAK1 and BIR1 or BAK1 and AtSERK4 regulate cell death during steady state conditions. Moreover, the redundant and distinct functions of AtSERK proteins and other members of the LRR-RLKII family have been revealed. This review focuses on the integration of the information from the most recent studies concerning BAK1 and its homologs.

Keywords AtSERK, BAK1, BAK1-interacting proteins, BR signaling, cell death, plant immunity

Article

Minireview

Mol. Cells 2013; 35(1): 7-16

Published online January 31, 2013 https://doi.org/10.1007/s10059-013-2255-3

Copyright © The Korean Society for Molecular and Cellular Biology.

Assessing the Diverse Functions of BAK1 and Its Homologs in Arabidopsis, beyond BR Signaling and PTI Responses

Beg Hab Kim, Sun Young Kim, and Kyoung Hee Nam*

Department of Biological Science, Sookmyung Women’s University, Seoul 140-742, Korea

Correspondence to:*Correspondence: khnam514@sookmyung.ac.kr

Received: October 2, 2012; Revised: November 9, 2012; Accepted: November 19, 2012

Abstract

Plants possess a variety of extracellular leucine-rich repeats receptor-like kinases (LRR-RLKs) to coordinate developmental programs with responses to environmental changes. Out of sixteen families of LRR-RLKs in Arabidopsis, the LRR-RLKII family consists of fourteen individual members, including five Arabidopsis thaliana somatic embryogenesis receptor kinases (AtSERKs). BAK1/AtSERK3 was first identified as a dual co-receptor of BRI1 and FLS2, mediating BR signaling and pathogen-associated molecular pattern (PAMP) triggered immunity (PTI), respectively. Since its identification, many researchers have attempted to elucidate the phosphorylation mechanisms between receptor complexes and identify additional components that interact with receptor complexes to transduce the signaling downstream. Relatively detailed early events in complex formation, phosphorylation sites on the BRI1/BAK1 complex and BAK1-interacting proteins, such as BIK1 and PUB13, have been identified. Small receptor complexes consisting of BAK1 and BIR1 or BAK1 and AtSERK4 regulate cell death during steady state conditions. Moreover, the redundant and distinct functions of AtSERK proteins and other members of the LRR-RLKII family have been revealed. This review focuses on the integration of the information from the most recent studies concerning BAK1 and its homologs.

Keywords: AtSERK, BAK1, BAK1-interacting proteins, BR signaling, cell death, plant immunity

Mol. Cells
May 31, 2023 Vol.46 No.5, pp. 259~328
COVER PICTURE
The alpha-helices in the lamin filaments are depicted as coils, with different subdomains distinguished by various colors. Coil 1a is represented by magenta, coil 1b by yellow, L2 by green, coil 2a by white, coil 2b by brown, stutter by cyan, coil 2c by dark blue, and the lamin Ig-like domain by grey. In the background, cells are displayed, with the cytosol depicted in green and the nucleus in blue (Ahn et al., pp. 309-318).

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