Moonlighting kinases with guanylate cyclase activity can tune regulatory signal networks

Helen R. Irving, Lusisizwe Kwezi, Janet I. Wheeler, Chris Gehring

Research output: Contribution to journalArticlepeer-review

32 Scopus citations


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.

Original languageEnglish (US)
JournalPlant Signaling and Behavior
Issue number2
StatePublished - Feb 2012


  • Brassinosteroid receptor (BRI1)
  • Cyclic GMP (cGMP)
  • Guanylate cyclase
  • Phytosulfokine
  • Phytosulfokine receptor (PSKR)

ASJC Scopus subject areas

  • Plant Science


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