Moonlighting kinases with guanylate cyclase activity can tune regulatory signal networks
KAUST DepartmentBiological and Environmental Sciences and Engineering (BESE) Division
Molecular Signalling Group
Online Publication Date2014-10-28
Print Publication Date2012-02
Permanent link to this recordhttp://hdl.handle.net/10754/562082
MetadataShow full item record
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.
PublisherInforma UK Limited
JournalPlant Signaling & Behavior
PubMed Central IDPMC3405710
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