Receptor guanylyl cyclase-G is a novel thermosensory protein activated by cool temperatures

Ying Chi Chao, Chih Cheng Chen, Yuh Charn Lin, Heinz Breer, Joerg Fleischer, Ruey Bing Yang

Research output: Contribution to journalArticlepeer-review

36 Citations (Scopus)


Transmembrane guanylyl cyclases (GCs), with activity regulated by peptide ligands and/or calcium-binding proteins, are essential for various physiological and sensory processes. The mode of activation of the GC subtype GC-G, which is expressed in neurons of the Grueneberg ganglion that respond to cool temperatures, has been elusive. In searching for appropriate stimuli to activate GC-G, we found that its enzymatic activity is directly stimulated by cool temperatures. In this context, it was observed that dimerization/oligomerization of GC-G, a process generally considered as critical for enzymatic activity of GCs, is strongly enhanced by coolness. Moreover, heterologous expression of GC-G in cultured cells rendered these cells responsive to coolness; thus, the protein might be a sensor for cool temperatures. This concept is supported by the observation of substantially reduced coolness-induced response of Grueneberg ganglion neurons and coolness-evoked ultrasonic vocalization in GC-G-deficient mouse pups. GC-G may be a novel thermosensory protein with functional implications for the Grueneberg ganglion, a sensory organ responding to cool temperatures.

Original languageEnglish
Pages (from-to)294-306
Number of pages13
JournalEMBO Journal
Issue number3
Publication statusPublished - Feb 3 2015


  • chemosensory
  • cyclic guanosine monophosphate
  • Grueneberg ganglion
  • transmembrane guanylyl cyclase GC-G
  • ultrasound vocalization

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)


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