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dc.contributor.authorKwezi, Lusisizwe
dc.contributor.authorWheeler, Janet I
dc.contributor.authorMarondedze, Claudius
dc.contributor.authorGehring, Christoph A
dc.contributor.authorIrving, Helen R
dc.date.accessioned2018-02-01T11:45:54Z
dc.date.available2018-02-01T11:45:54Z
dc.date.issued2018-02-15
dc.identifier.citationKwezi L, Wheeler JI, Marondedze C, Gehring C, Irving HR (2018) Intramolecular Crosstalk between Catalytic Activities of Receptor Kinases. Plant Signaling & Behavior: 00–00. Available: http://dx.doi.org/10.1080/15592324.2018.1430544.
dc.identifier.issn1559-2324
dc.identifier.pmid29355445
dc.identifier.doi10.1080/15592324.2018.1430544
dc.identifier.urihttp://hdl.handle.net/10754/627011
dc.description.abstractSignal modulation is important for the growth and development of plants and this process is mediated by a number of factors including physiological growth regulators and their associated signal transduction pathways. Protein kinases play a central role in signaling, including those involving pathogen response mechanisms. We previously demonstrated an active guanylate cyclase (GC) catalytic center in the brassinosteroid insensitive receptor (AtBRI1) within an active intracellular kinase domain resulting in dual enzymatic activity. Here we propose a novel type of receptor architecture that is characterized by a functional GC catalytic center nested in the cytosolic kinase domain enabling intramolecular crosstalk. This may be through a cGMP-AtBRI1 complex forming that may induce a negative feedback mechanism leading to desensitisation of the receptor, regulated through the cGMP production pathway. We further argue that the comparatively low but highly localized cGMP generated by the GC in response to a ligand is sufficient to modulate the kinase activity. This type of receptor therefore provides a molecular switch that directly and/or indirectly affects ligand dependent phosphorylation of downstream signaling cascades and suggests that subsequent signal transduction and modulation works in conjunction with the kinase in downstream signaling.
dc.description.sponsorshipFunding for this research was provided by the Australian Research Council's Discovery funding scheme (project numbers DP0878194 and DP110104164) and the National Research Foundation South Africa (grant numbers 78843; IRF2009021800047).
dc.publisherInforma UK Limited
dc.relation.urlhttp://www.tandfonline.com/doi/full/10.1080/15592324.2018.1430544
dc.rightsThis is an Accepted Manuscript of an article published by Taylor & Francis in Plant Signaling & Behavior on 22 Jan 2018, available online: http://wwww.tandfonline.com/10.1080/15592324.2018.1430544.
dc.subjectAuto-regulation
dc.subjectbrassinosteroid receptor (BRI1)
dc.subjectcyclic GMP
dc.subjectintramolecular crosstalk
dc.subjectphytosulfokine receptor 1 (PSKR1)
dc.subjectPeP1 receptor (PEPR1)
dc.subjectphosphorylation
dc.subjectreceptor kinase
dc.subjectsignal transduction
dc.titleIntramolecular Crosstalk between Catalytic Activities of Receptor Kinases
dc.typeArticle
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.contributor.departmentBioscience Program
dc.identifier.journalPlant Signaling & Behavior
dc.eprint.versionPost-print
dc.contributor.institutionCouncil For Scientific and Industrial Research, Biosciences, Brummeria, Pretoria 0001, South Africa
dc.contributor.institutionMonash Institute of Pharmaceutical Sciences, Monash University, Melbourne, VIC 3052 Australia
dc.contributor.institutionAgriBio, La Trobe University, Bundoora, VIC 3086, Australia
dc.contributor.institutionLaboratoire de Physiologie Cellulaire et Végétale, Université Grenoble Alpes, CEA/DRF/BIG, INRA UMR1417, CNRS UMR5168, 38054 Grenoble Cedex 9, France
dc.contributor.institutionLa Trobe Institute for Molecular Science, La Trobe University, PO Box 199, Bendigo VIC 3552, Australia
kaust.personMarondedze, Claudius
kaust.personGehring, Christoph A.
dc.date.published-online2018-02-15
dc.date.published-print2018-02


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