| First Author | Chao YC | Year | 2015 |
| Journal | EMBO J | Volume | 34 |
| Issue | 3 | Pages | 294-306 |
| PubMed ID | 25452496 | Mgi Jnum | J:218251 |
| Mgi Id | MGI:5617081 | Doi | 10.15252/embj.201489652 |
| Citation | Chao YC, et al. (2015) Receptor guanylyl cyclase-G is a novel thermosensory protein activated by cool temperatures. EMBO J 34(3):294-306 |
| abstractText | 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. |
