Calcium is the switch in the moonlighting dual function of the ligand-activated receptor kinase phytosulfokine receptor 1

Handle URI:
http://hdl.handle.net/10754/334974
Title:
Calcium is the switch in the moonlighting dual function of the ligand-activated receptor kinase phytosulfokine receptor 1
Authors:
Muleya, Victor; Wheeler, Janet I; Ruzvidzo, Oziniel; Freihat, Lubna; Manallack, David T; Gehring, Christoph A. ( 0000-0003-4355-4591 ) ; Irving, Helen R
Abstract:
Background: A number of receptor kinases contain guanylate cyclase (GC) catalytic centres encapsulated in the cytosolic kinase domain. A prototypical example is the phytosulfokine receptor 1 (PSKR1) that is involved in regulating growth responses in plants. PSKR1 contains both kinase and GC activities however the underlying mechanisms regulating the dual functions have remained elusive. Findings: Here, we confirm the dual activity of the cytoplasmic domain of the PSKR1 receptor. We show that mutations within the guanylate cyclase centre modulate the GC activity while not affecting the kinase catalytic activity. Using physiologically relevant Ca2+ levels, we demonstrate that its GC activity is enhanced over two-fold by Ca2+ in a concentration-dependent manner. Conversely, increasing Ca2+ levels inhibits kinase activity up to 500-fold at 100 nM Ca2+. Conclusions: Changes in calcium at physiological levels can regulate the kinase and GC activities of PSKR1. We therefore propose a functional model of how calcium acts as a bimodal switch between kinase and GC activity in PSKR1 that could be relevant to other members of this novel class of ligand-activated receptor kinases.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division
Citation:
Calcium is the switch in the moonlighting dual function of the ligand-activated receptor kinase phytosulfokine receptor 1 2014, 12 (1):60 Cell Communication and Signaling
Publisher:
Springer Nature
Journal:
Cell Communication and Signaling
Issue Date:
23-Sep-2014
DOI:
10.1186/s12964-014-0060-z
PubMed ID:
25245092
PubMed Central ID:
PMC4180545
Type:
Article
ISSN:
1478-811X
Additional Links:
http://www.biosignaling.com/content/12/1/60
Appears in Collections:
Articles; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorMuleya, Victoren
dc.contributor.authorWheeler, Janet Ien
dc.contributor.authorRuzvidzo, Ozinielen
dc.contributor.authorFreihat, Lubnaen
dc.contributor.authorManallack, David Ten
dc.contributor.authorGehring, Christoph A.en
dc.contributor.authorIrving, Helen Ren
dc.date.accessioned2014-11-16T12:04:49Zen
dc.date.available2014-11-16T12:04:49Zen
dc.date.issued2014-09-23en
dc.identifier.citationCalcium is the switch in the moonlighting dual function of the ligand-activated receptor kinase phytosulfokine receptor 1 2014, 12 (1):60 Cell Communication and Signalingen
dc.identifier.issn1478-811Xen
dc.identifier.pmid25245092en
dc.identifier.doi10.1186/s12964-014-0060-zen
dc.identifier.urihttp://hdl.handle.net/10754/334974en
dc.description.abstractBackground: A number of receptor kinases contain guanylate cyclase (GC) catalytic centres encapsulated in the cytosolic kinase domain. A prototypical example is the phytosulfokine receptor 1 (PSKR1) that is involved in regulating growth responses in plants. PSKR1 contains both kinase and GC activities however the underlying mechanisms regulating the dual functions have remained elusive. Findings: Here, we confirm the dual activity of the cytoplasmic domain of the PSKR1 receptor. We show that mutations within the guanylate cyclase centre modulate the GC activity while not affecting the kinase catalytic activity. Using physiologically relevant Ca2+ levels, we demonstrate that its GC activity is enhanced over two-fold by Ca2+ in a concentration-dependent manner. Conversely, increasing Ca2+ levels inhibits kinase activity up to 500-fold at 100 nM Ca2+. Conclusions: Changes in calcium at physiological levels can regulate the kinase and GC activities of PSKR1. We therefore propose a functional model of how calcium acts as a bimodal switch between kinase and GC activity in PSKR1 that could be relevant to other members of this novel class of ligand-activated receptor kinases.en
dc.language.isoenen
dc.publisherSpringer Natureen
dc.relation.urlhttp://www.biosignaling.com/content/12/1/60en
dc.rightsThis is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.en
dc.rights.urihttp://creativecommons.org/licenses/by/4.0en
dc.subjectCalciumen
dc.subjectGuanylate cyclaseen
dc.subjectKinaseen
dc.subjectPSKR1en
dc.titleCalcium is the switch in the moonlighting dual function of the ligand-activated receptor kinase phytosulfokine receptor 1en
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.identifier.journalCell Communication and Signalingen
dc.identifier.pmcidPMC4180545en
dc.eprint.versionPublisher's Version/PDFen
dc.contributor.institutionDepartment of Biological Sciences, North-West University, Private Bag X2046, Mmabatho 2735, South Africaen
dc.contributor.institutionMonash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville 3052, VIC, Australiaen
dc.contributor.affiliationKing Abdullah University of Science and Technology (KAUST)en
kaust.authorGehring, Christoph A.en

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