Mechanistic analysis of the SERK3 elongated allele defines a role for BIR ectodomains in brassinosteroid signaling

Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review

Autoren

  • Ulrich Hohmann
  • Joël Nicolet
  • Andrea Moretti
  • Ludwig A. Hothorn
  • Michael Hothorn

Organisationseinheiten

Externe Organisationen

  • Universität Genf
Forschungs-netzwerk anzeigen

Details

OriginalspracheEnglisch
Seiten (von - bis)345-351
Seitenumfang7
FachzeitschriftNature plants
Jahrgang4
Ausgabenummer6
Frühes Online-Datum7 Mai 2018
PublikationsstatusVeröffentlicht - Juni 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 Sachgebiete

Zitieren

Mechanistic analysis of the SERK3 elongated allele defines a role for BIR ectodomains in brassinosteroid signaling. / Hohmann, Ulrich; Nicolet, Joël; Moretti, Andrea et al.
in: Nature plants, Jahrgang 4, Nr. 6, 06.2018, S. 345-351.

Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review

Hohmann U, Nicolet J, Moretti A, Hothorn LA, Hothorn M. Mechanistic analysis of the SERK3 elongated allele defines a role for BIR ectodomains in brassinosteroid signaling. Nature plants. 2018 Jun;4(6):345-351. Epub 2018 Mai 7. doi: 10.1101/257543, 10.1038/s41477-018-0150-9, 10.1038/s41477-018-0244-4
Hohmann, Ulrich ; Nicolet, Joël ; Moretti, Andrea et al. / Mechanistic analysis of the SERK3 elongated allele defines a role for BIR ectodomains in brassinosteroid signaling. in: Nature plants. 2018 ; Jahrgang 4, Nr. 6. S. 345-351.
Download
@article{2cecce7f16a6466c9faf1f5f10a3393a,
title = "Mechanistic analysis of the SERK3 elongated allele defines a role for BIR ectodomains in brassinosteroid signaling",
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 {\AA} BIR3-SERK1 structure. Collectively, our structural, quantitative biochemical and genetic analyses suggest that brassinosteroid signalling complex formation is negatively regulated by BIR receptor ectodomains.",
author = "Ulrich Hohmann and Jo{\"e}l Nicolet and Andrea Moretti and Hothorn, {Ludwig A.} and Michael Hothorn",
note = "Publisher Copyright: {\textcopyright} 2018 The Author(s).",
year = "2018",
month = jun,
doi = "10.1101/257543",
language = "English",
volume = "4",
pages = "345--351",
journal = "Nature plants",
issn = "2055-0278",
publisher = "Nature Research",
number = "6",

}

Download

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 -