Moonlighting kinases with guanylate cyclase activity can tune regulatory signal networks

Handle URI:
http://hdl.handle.net/10754/562082
Title:
Moonlighting kinases with guanylate cyclase activity can tune regulatory signal networks
Authors:
Irving, Helen R.; Kwezi, Lusisizwe; Wheeler, Janet I.; Gehring, Christoph A. ( 0000-0003-4355-4591 )
Abstract:
Guanylate cyclase (GC) catalyzes the formation of cGMP and it is only recently that such enzymes have been characterized in plants. One family of plant GCs contains the GC catalytic center encapsulated within the intracellular kinase domain of leucine rich repeat receptor like kinases such as the phytosulfokine and brassinosteroid receptors. In vitro studies show that both the kinase and GC domain have catalytic activity indicating that these kinase-GCs are examples of moonlighting proteins with dual catalytic function. The natural ligands for both receptors increase intracellular cGMP levels in isolated mesophyll protoplast assays suggesting that the GC activity is functionally relevant. cGMP production may have an autoregulatory role on receptor kinase activity and/or contribute to downstream cell expansion responses. We postulate that the receptors are members of a novel class of receptor kinases that contain functional moonlighting GC domains essential for complex signaling roles.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division; Bioscience Program; Molecular Signalling Group
Publisher:
Informa UK Limited
Journal:
Plant Signaling & Behavior
Issue Date:
Feb-2012
DOI:
10.4161/psb.18891
PubMed ID:
22353864
PubMed Central ID:
PMC3405710
Type:
Article
ISSN:
15592316
Additional Links:
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3405710
Appears in Collections:
Articles; Bioscience Program; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorIrving, Helen R.en
dc.contributor.authorKwezi, Lusisizween
dc.contributor.authorWheeler, Janet I.en
dc.contributor.authorGehring, Christoph A.en
dc.date.accessioned2015-08-03T09:44:23Zen
dc.date.available2015-08-03T09:44:23Zen
dc.date.issued2012-02en
dc.identifier.issn15592316en
dc.identifier.pmid22353864en
dc.identifier.doi10.4161/psb.18891en
dc.identifier.urihttp://hdl.handle.net/10754/562082en
dc.description.abstractGuanylate cyclase (GC) catalyzes the formation of cGMP and it is only recently that such enzymes have been characterized in plants. One family of plant GCs contains the GC catalytic center encapsulated within the intracellular kinase domain of leucine rich repeat receptor like kinases such as the phytosulfokine and brassinosteroid receptors. In vitro studies show that both the kinase and GC domain have catalytic activity indicating that these kinase-GCs are examples of moonlighting proteins with dual catalytic function. The natural ligands for both receptors increase intracellular cGMP levels in isolated mesophyll protoplast assays suggesting that the GC activity is functionally relevant. cGMP production may have an autoregulatory role on receptor kinase activity and/or contribute to downstream cell expansion responses. We postulate that the receptors are members of a novel class of receptor kinases that contain functional moonlighting GC domains essential for complex signaling roles.en
dc.publisherInforma UK Limiteden
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3405710en
dc.titleMoonlighting kinases with guanylate cyclase activity can tune regulatory signal networksen
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.contributor.departmentBioscience Programen
dc.contributor.departmentMolecular Signalling Groupen
dc.identifier.journalPlant Signaling & Behavioren
dc.identifier.pmcidPMC3405710en
dc.contributor.institutionMonash Institute of Pharmaceutical Sciences, Monash University, Parkville, Australiaen
dc.contributor.institutionDepartment of Biological Sciences, North-West University, Mmabatho, South Africaen
kaust.authorGehring, Christoph A.en

Related articles on PubMed

All Items in KAUST are protected by copyright, with all rights reserved, unless otherwise indicated.