Faculty Opinions recommendation of BRI1/BAK1, a receptor kinase pair mediating brassinosteroid signaling.

Author(s):  
Martin Parniske
2020 ◽  
Vol 21 (12) ◽  
pp. 4340 ◽  
Author(s):  
Juan Mao ◽  
Jianming Li

Brassinosteroids (BRs) are important plant growth hormones that regulate a wide range of plant growth and developmental processes. The BR signals are perceived by two cell surface-localized receptor kinases, Brassinosteroid-Insensitive1 (BRI1) and BRI1-Associated receptor Kinase (BAK1), and reach the nucleus through two master transcription factors, bri1-EMS suppressor1 (BES1) and Brassinazole-resistant1 (BZR1). The intracellular transmission of the BR signals from BRI1/BAK1 to BES1/BZR1 is inhibited by a constitutively active kinase Brassinosteroid-Insensitive2 (BIN2) that phosphorylates and negatively regulates BES1/BZR1. Since their initial discoveries, further studies have revealed a plethora of biochemical and cellular mechanisms that regulate their protein abundance, subcellular localizations, and signaling activities. In this review, we provide a critical analysis of the current literature concerning activation, inactivation, and other regulatory mechanisms of three key kinases of the BR signaling cascade, BRI1, BAK1, and BIN2, and discuss some unresolved controversies and outstanding questions that require further investigation.


Cell ◽  
2002 ◽  
Vol 110 (2) ◽  
pp. 203-212 ◽  
Author(s):  
Kyoung Hee Nam ◽  
Jianming Li

2018 ◽  
Author(s):  
Ulrich Hohmann ◽  
Joël Nicolet ◽  
Andrea Moretti ◽  
Ludwig A. Hothorn ◽  
Michael Hothorn

AbstractThe leucine-rich repeat receptor kinase (LRR-RK) BRI1 requires a shape-complementary SERK co-receptor for brassinosteroid sensing and receptor activation. Interface mutations that weaken the interaction between receptor and co-receptor in vitro reduce brassinosteroid signaling responses. The SERK3 elongated (elg) allele maps to the complex interface and shows enhanced brassinosteroid signaling, but surprisingly no tighter binding to the BRI1 ectodomain in vitro. Here, we report that rather than promoting the interaction with BRI1, the elg mutation disrupts the ability of the co-receptor to interact with the ectodomains of BIR receptor pseudokinases, negative regulators of LRR-RK signaling. A conserved lateral surface patch in BIR LRR domains is required for targeting SERK co-receptors and the elg allele maps to the core of the complex interface in a 1.25 Å BIR3 - SERK1 structure. Collectively, our structural, quantitative biochemical and genetic analyses suggest that brassinosteroid signaling complex formation is negatively regulated by BIR receptor ectodomains.


2016 ◽  
Vol 9 (4) ◽  
pp. 593-600 ◽  
Author(s):  
Juthamas Chaiwanon ◽  
Veder J. Garcia ◽  
Heather Cartwright ◽  
Ying Sun ◽  
Zhi-Yong Wang

2008 ◽  
Vol 15 (2) ◽  
pp. 220-235 ◽  
Author(s):  
Xiaofeng Wang ◽  
Uma Kota ◽  
Kai He ◽  
Kevin Blackburn ◽  
Jia Li ◽  
...  

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