期刊
EMBO JOURNAL
卷 34, 期 3, 页码 294-306出版社
WILEY
DOI: 10.15252/embj.201489652
关键词
cyclic guanosine monophosphate; chemosensory; Grueneberg ganglion; transmembrane guanylyl cyclase GC-G; ultrasound vocalization
资金
- Neuroscience Program in Academia Sinica
- National Science Council, Taiwan [NSC-97-2320-B-001-009-MY3]
- Deutsche Forschungsgemeinschaft [Br712/24-1]
- Bundesministerium fur Bildung und Forschung [01PL11003]
- Taiwan Mouse Clinic - National Research Program for Biopharmaceuticals (NRPB) at the National Science Council (NSC) of Taiwan [NSC 102-2325-B-001-042]
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.
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