Journal
SCIENCE
Volume 308, Issue 5730, Pages 1931-1934Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1109886
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Funding
- NEI NIH HHS [R01 EY006837, R01 EY006837-18, R01 EY014596, R01 EY014596-03, R37 EY006837-15S1, R01 EY014596-01, R01 EY006837-17, R37 EY006837, R01 EY006837-16A1, R01 EY014596-02, R37 EY006837-15] Funding Source: Medline
- NIDCD NIH HHS [R01 DC006904, DC06904, R01 DC006904-01] Funding Source: Medline
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Signaling by heterotrimeric GTP-binding proteins (G proteins) drives numerous cellular processes. The number of G protein molecules activated by a single membrane receptor is a determinant of signal amplification, although in most cases this parameter remains unknown. In retinal rod photoreceptors, a long-lived photoisomerized rhodopsin molecule activates many G protein molecules (transducins), yielding substantial amplification and a large elementary (single-photon) response, before rhodopsin activity is terminated. Here we report that the elementary response in olfactory transduction is extremely small. A ligand-bound odorant receptor has a low probability of activating even one G protein molecule because the odorant dwell-time is very brief. Thus, signal amplification in olfactory transduction appears fundamentally different from that of phototransduction.
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