The brassinosteroid receptor BRI1 can generate cGMP enabling cGMP-dependent downstream signaling
AuthorsWheeler, Janet I.
Wong, Aloysius Tze
Groen, Arnoud J.
Irving, Helen R.
Gehring, Christoph A
KAUST DepartmentBiological and Environmental Sciences and Engineering (BESE) Division
Analytical Chemistry Core Laboratory, King Abdullah University of Science and Technology, Thuwal, Kingdom of Saudi Arabia
Permanent link to this recordhttp://hdl.handle.net/10754/623663
MetadataShow full item record
AbstractThe brassinosteroid receptor BRASSINOSTEROID INSENSITIVE 1 (BRI1) is a member of the leucine rich repeat receptor like kinase family. The intracellular kinase domain of BRI1 is an active kinase and also encapsulates a guanylate cyclase catalytic centre. Using liquid chromatography tandem mass spectrometry, we confirmed that the recombinant cytoplasmic domain of BRI1 generates pmol amounts of cGMP per μg protein with a preference for magnesium over manganese as a co-factor. Importantly, a functional BRI1 kinase is essential for optimal cGMP generation. Therefore, the guanylate cyclase activity of BRI1 is modulated by the kinase while cGMP, the product of the guanylate cyclase, in turn inhibits BRI1 kinase activity. Furthermore, we show using Arabidopsis root cell cultures that cGMP rapidly potentiates phosphorylation of the downstream substrate BRASSINOSTEROID SIGNALING KINASE 1 (BSK1). Taken together, our results suggest that cGMP acts as a modulator that enhances downstream signaling while dampening signal generation from the receptor. This article is protected by copyright. All rights reserved.
CitationWheeler JI, Wong A, Marondedze C, Groen AJ, Kwezi L, et al. (2017) The brassinosteroid receptor BRI1 can generate cGMP enabling cGMP-dependent downstream signaling. The Plant Journal. Available: http://dx.doi.org/10.1111/tpj.13589.
SponsorsSupport from the Australian Research Council’s Discovery funding scheme (project numbers DP0878194 and DP110104164), the National Research Foundation South Africa (grant numbers 78843; IRF2009021800047) and La Trobe University School of Life Science Publication Booster Award is gratefully acknowledged. We also thank Dr Yu Hua Wang (Monash University) for preparing the G1073K mutant construct and Dr Victor Muleya (Monash University) for helpful discussions.
JournalThe Plant Journal
- Crystal structures of the phosphorylated BRI1 kinase domain and implications for brassinosteroid signal initiation.
- Authors: Bojar D, Martinez J, Santiago J, Rybin V, Bayliss R, Hothorn M
- Issue date: 2014 Apr
- Visualization of BRI1 and BAK1(SERK3) membrane receptor heterooligomers during brassinosteroid signaling.
- Authors: Bücherl CA, van Esse GW, Kruis A, Luchtenberg J, Westphal AH, Aker J, van Hoek A, Albrecht C, Borst JW, de Vries SC
- Issue date: 2013 Aug
- Identification and functional analysis of in vivo phosphorylation sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase.
- Authors: Wang X, Goshe MB, Soderblom EJ, Phinney BS, Kuchar JA, Li J, Asami T, Yoshida S, Huber SC, Clouse SD
- Issue date: 2005 Jun
- Tyrosine phosphorylation of the BRI1 receptor kinase emerges as a component of brassinosteroid signaling in Arabidopsis.
- Authors: Oh MH, Wang X, Kota U, Goshe MB, Clouse SD, Huber SC
- Issue date: 2009 Jan 13
- Ligand perception, activation, and early signaling of plant steroid receptor brassinosteroid insensitive 1.
- Authors: Jiang J, Zhang C, Wang X
- Issue date: 2013 Dec