Intramolecular Crosstalk between Catalytic Activities of Receptor Kinases

Handle URI:
http://hdl.handle.net/10754/627011
Title:
Intramolecular Crosstalk between Catalytic Activities of Receptor Kinases
Authors:
Kwezi, Lusisizwe; Wheeler, Janet I; Marondedze, Claudius ( 0000-0002-2113-904X ) ; Gehring, Christoph A. ( 0000-0003-4355-4591 ) ; Irving, Helen R
Abstract:
Signal 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.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division
Citation:
Kwezi 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.
Publisher:
Informa UK Limited
Journal:
Plant Signaling & Behavior
Issue Date:
22-Jan-2018
DOI:
10.1080/15592324.2018.1430544
Type:
Article
ISSN:
1559-2324
Sponsors:
Funding 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).
Additional Links:
http://www.tandfonline.com/doi/full/10.1080/15592324.2018.1430544
Appears in Collections:
Articles; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorKwezi, Lusisizween
dc.contributor.authorWheeler, Janet Ien
dc.contributor.authorMarondedze, Claudiusen
dc.contributor.authorGehring, Christoph A.en
dc.contributor.authorIrving, Helen Ren
dc.date.accessioned2018-02-01T11:45:54Z-
dc.date.available2018-02-01T11:45:54Z-
dc.date.issued2018-01-22en
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.en
dc.identifier.issn1559-2324en
dc.identifier.doi10.1080/15592324.2018.1430544en
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.en
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).en
dc.publisherInforma UK Limiteden
dc.relation.urlhttp://www.tandfonline.com/doi/full/10.1080/15592324.2018.1430544en
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.en
dc.subjectAuto-regulationen
dc.subjectbrassinosteroid receptor (BRI1)en
dc.subjectcyclic GMPen
dc.subjectintramolecular crosstalken
dc.subjectphytosulfokine receptor 1 (PSKR1)en
dc.subjectPeP1 receptor (PEPR1)en
dc.subjectphosphorylationen
dc.subjectreceptor kinaseen
dc.subjectsignal transductionen
dc.titleIntramolecular Crosstalk between Catalytic Activities of Receptor Kinasesen
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.identifier.journalPlant Signaling & Behavioren
dc.eprint.versionPost-printen
dc.contributor.institutionCouncil For Scientific and Industrial Research, Biosciences, Brummeria, Pretoria 0001, South Africaen
dc.contributor.institutionMonash Institute of Pharmaceutical Sciences, Monash University, Melbourne, VIC 3052 Australiaen
dc.contributor.institutionAgriBio, La Trobe University, Bundoora, VIC 3086, Australiaen
dc.contributor.institutionLaboratoire de Physiologie Cellulaire et Végétale, Université Grenoble Alpes, CEA/DRF/BIG, INRA UMR1417, CNRS UMR5168, 38054 Grenoble Cedex 9, Franceen
dc.contributor.institutionLa Trobe Institute for Molecular Science, La Trobe University, PO Box 199, Bendigo VIC 3552, Australiaen
kaust.authorMarondedze, Claudiusen
kaust.authorGehring, Christoph A.en
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