Evidence that a Gq-protein mediates excitatory odor transduction in lobster olfactory receptor neurons

• Published in: Chemical senses Vol. 20; no. 5; p. 489
• Main Authors: Fadool, D A, Estey, S J, Ache, B W
• Format: Journal Article
• Language: English
• Published: England 01.10.1995
• Subjects: Amino Acid Sequence; Animals; Blotting, Western; Culture Techniques; Dendrites - metabolism; Dendrites - physiology; Electrophoresis, Polyacrylamide Gel; Electrophysiology; GTP-Binding Proteins - isolation & purification; GTP-Binding Proteins - metabolism; GTP-Binding Proteins - physiology; Molecular Sequence Data; Nephropidae - physiology; Olfactory Receptor Neurons - metabolism; Olfactory Receptor Neurons - physiology; Patch-Clamp Techniques; Sense Organs - cytology; Signal Transduction - physiology; Smell - physiology
• ISSN: 0379-864X
• DOI: 10.1093/chemse/20.5.489

Non-hydrolysable analogs of GTP and GDP alter odor-evoked inward and outward currents in voltage-clamped cultured lobster olfactory receptor neurons. Currents of both polarities are pertussis and cholera toxin-insensitive. Antibodies directed against the alpha subunits of G(olf), G(o), G11, an internal Gq sequence, the common carboxyl terminal sequence of Gq and G11 (anti-Gq/11), and the transducin beta subunit, fail to perturb the outward current, but anti-G(o) and anti-Gq/11 selectively block the inward current. Anti-Gq/11 immunolabels a band of approximately 45 kDa by Western blot analysis, but the anti-G(o) immunolabeling is non-specific. These results suggest that the excitatory olfactory signalling pathway that leads to an odor-evoked inward current may be coupled via a member of the Gq family, while the odor-evoked outward current is transduced by a different G protein.