Related Experiment Video
Updated: Aug 8, 2026

Quantifying Agonist Activity at G Protein-coupled Receptors
Published on: December 26, 2011
Subunit composition and functional properties of G-protein heterotrimers on rat chromaffin granules
Ingrid Pahner1, Markus Höltje, Sandra Winter
1Institut für Anatomie/Neurowissenschaftliches Zentrum der Charité, Humboldt Universität zu Berlin, Germany.
Abstract:
Heterotrimeric G-proteins at the plasma membrane serve as switches between heptahelical receptors and intracellular signal cascades. Likewise endomembrane associated G-proteins may transduce signals from intracellular compartments provided they consist of a functional trimer. Using quantitative immunoelectron microscopy we found heterotrimeric G-protein subunits Galpha2, Galpha(q/11), Gbeta2 and Gbeta5 to reside on secretory granules in chromaffin cells of rat adrenal glands. Thus rat chromaffin granules are equipped with functional G-proteins that consist of a specific alpha-, beta- and probably gamma-subunit combination. Serotonin uptake into a crude rat chromaffin granule preparation was inhibited by activated Galphao2 (10 nM) to nearly the same extent as by GMppNp (50 microM) whereas GDPbetaS was ineffective. The data support the idea that vesicular G-proteins directly regulate the transmitter content of secretory vesicles. In this respect Galphao2 appears to be the main regulator of vesicular momoamine transporter activity.
More Related Videos
Related Concept Videos
G-protein Coupled Receptors
GTPases and their Regulation
Large G-proteins, also known...
G Protein-coupled Receptors
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
Activation and Inactivation of G Proteins
G-Protein Gated Ion Channels
Sensory organs,...
Transducer Mechanism: G Protein–Coupled Receptors
GPCRs are also called heptahelical, 7TM, or...

