Abstract
We find that half of the pertussis toxin-sensitive guanine nucleotide-binding protein (G protein) in the squid (Loligo pealei) giant axon is cytoplasmic and that this species of G protein is intermediate in size between the two forms present in axolemma. This G protein is transported toward synaptic terminals at 44 mm/day. Moreover, these data are consistent with there being two additional steps leading to the maturation of G proteins: (i) association with and transport on intracellular organelles and (ii) modification at the time of transfer to the plasmalemma resulting in a molecular weight shift. Since the other two components of G protein-mediated signal transduction pathways, receptors and effector enzymes, are known to be delivered to the synaptic terminals by fast axonal transport, our findings introduce the possibility that these three macromolecules are assembled as a complex in the cell body and delivered together to the plasma membrane of the axon and synaptic terminals.
MeSH Terms
Adenosine Diphosphate Ribose/metabolism
Animals
Axonal Transport
Axons/physiology,ultrastructure
Decapodiformes
GTP-Binding Proteins/metabolism
In Vitro Techniques
Kinetics
Models, Neurological
NAD/metabolism
Pertussis Toxin
Synapses/physiology
Temperature
Virulence Factors, Bordetella/pharmacology
Chemicals
Virulence Factors, Bordetella
NAD
Adenosine Diphosphate Ribose
Pertussis Toxin
GTP-Binding Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Vogel S S
Marine Biological Laboratory, Woods Hole, MA 02543.
Chin G J
Schwartz J H
Reese T S
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