Details
Original language | English |
---|---|
Pages (from-to) | 345-351 |
Number of pages | 7 |
Journal | Nature plants |
Volume | 4 |
Issue number | 6 |
Early online date | 7 May 2018 |
Publication status | Published - Jun 2018 |
Abstract
The leucine-rich repeat receptor kinase (LRR-RK) BRASSINOSTEROID INSENSITIVE 1 (BRI1) requires a shape-complementary SOMATIC EMBRYOGENESIS RECEPTOR KINASE (SERK) co-receptor for brassinosteroid sensing and receptor activation 1 . Interface mutations that weaken the interaction between receptor and co-receptor in vitro reduce brassinosteroid signalling responses 2 . The SERK3 elongated (elg) allele 3-5 maps to the complex interface and shows enhanced brassinosteroid signalling, 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 BRI1-ASSOCIATED-KINASE1 INTERACTING KINASE (BIR) receptor pseudokinases, negative regulators of LRR-RK signalling 6 . 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 signalling complex formation is negatively regulated by BIR receptor ectodomains.
ASJC Scopus subject areas
- Agricultural and Biological Sciences(all)
- Plant Science
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In: Nature plants, Vol. 4, No. 6, 06.2018, p. 345-351.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Mechanistic analysis of the SERK3 elongated allele defines a role for BIR ectodomains in brassinosteroid signaling
AU - Hohmann, Ulrich
AU - Nicolet, Joël
AU - Moretti, Andrea
AU - Hothorn, Ludwig A.
AU - Hothorn, Michael
N1 - Publisher Copyright: © 2018 The Author(s).
PY - 2018/6
Y1 - 2018/6
N2 - The leucine-rich repeat receptor kinase (LRR-RK) BRASSINOSTEROID INSENSITIVE 1 (BRI1) requires a shape-complementary SOMATIC EMBRYOGENESIS RECEPTOR KINASE (SERK) co-receptor for brassinosteroid sensing and receptor activation 1 . Interface mutations that weaken the interaction between receptor and co-receptor in vitro reduce brassinosteroid signalling responses 2 . The SERK3 elongated (elg) allele 3-5 maps to the complex interface and shows enhanced brassinosteroid signalling, 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 BRI1-ASSOCIATED-KINASE1 INTERACTING KINASE (BIR) receptor pseudokinases, negative regulators of LRR-RK signalling 6 . 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 signalling complex formation is negatively regulated by BIR receptor ectodomains.
AB - The leucine-rich repeat receptor kinase (LRR-RK) BRASSINOSTEROID INSENSITIVE 1 (BRI1) requires a shape-complementary SOMATIC EMBRYOGENESIS RECEPTOR KINASE (SERK) co-receptor for brassinosteroid sensing and receptor activation 1 . Interface mutations that weaken the interaction between receptor and co-receptor in vitro reduce brassinosteroid signalling responses 2 . The SERK3 elongated (elg) allele 3-5 maps to the complex interface and shows enhanced brassinosteroid signalling, 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 BRI1-ASSOCIATED-KINASE1 INTERACTING KINASE (BIR) receptor pseudokinases, negative regulators of LRR-RK signalling 6 . 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 signalling complex formation is negatively regulated by BIR receptor ectodomains.
UR - http://www.scopus.com/inward/record.url?scp=85046546455&partnerID=8YFLogxK
U2 - 10.1101/257543
DO - 10.1101/257543
M3 - Article
C2 - 29735985
AN - SCOPUS:85046546455
VL - 4
SP - 345
EP - 351
JO - Nature plants
JF - Nature plants
SN - 2055-0278
IS - 6
ER -