GTP‐binding proteins in human platelet membranes serving as the specific substrate of islet‐activating protein, pertussis toxin

@article{Nagata1988GTPbindingPI,
  title={GTP‐binding proteins in human platelet membranes serving as the specific substrate of islet‐activating protein, pertussis toxin},
  author={Koh-ichi Nagata and Toshiaki Katada and Masahiro Tohkin and Hiroshi Itoh and Yoshito Kaziro and Michio Ui and Yoshinori Nozawa},
  journal={FEBS Letters},
  year={1988},
  volume={237}
}
30 Citations
Identification of the pertussis toxin-sensitive G proteins in platelets, megakaryocytes, and human erythroleukemia cells.
TLDR
The pertussis toxin substrates that have previously been detected in platelets and HEL cells are shown to be members of the Gi alpha family, all of which are candidates for interaction with receptors for thrombin and other agonists.
A low Mr GTP‐binding protein, Rapl, in human platelets: localization, translocation and phosphorylation by cyclic AMP‐dependent protein kinase
TLDR
The results strongly suggest that Rapl in plasma membranes and the protein on a‐granules are regulated by different mechanisms, and have different functions.
Evidence for the Presence of a Low Mr GTP-binding Protein, ram p25, in Human Platelet Membranes.
TLDR
The ram gene was isolated from a rat megakaryocyte cDNA library and encodes a GTP-binding protein that was observed to be present in membrane fractions of human platelets.
Purification and characterization of five different alpha subunits of guanine-nucleotide-binding proteins in bovine brain membranes. Their physiological properties concerning the activities of adenylate cyclase and atrial muscarinic K+ channels.
TLDR
The results suggest that alpha and beta gamma subunits might activate the K+ channels by mechanisms different from each other.
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References

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Two guanine nucleotide-binding proteins in rat brain serving as the specific substrate of islet-activating protein, pertussis toxin. Interaction of the alpha-subunits with beta gamma-subunits in development of their biological activities.
Two proteins serving as substrates for ADP-ribosylation catalyzed by islet-activating protein (IAP), pertussis toxin, and binding guanosine 5'-(3-O-thio)triphosphate (GTP gamma S) with high
Mechanisms for inhibition of the catalytic activity of adenylate cyclase by the guanine nucleotide-binding proteins serving as the substrate of islet-activating protein, pertussis toxin.
TLDR
The direct inhibition of the catalyst by beta gamma or GTP gamma S-bound alpha 41 is a likely mechanism involved in receptor-mediated inhibition of adenylate cyclase, in addition to the previously proposed indirect inhibition due to the reduction of the concentration of the active alpha-subunit of Ns by reassociation with beta gamma.
Primary structure of the α-subunit of transducin and its relationship to ras proteins
TLDR
The complementary DNA encoding the α-subunit of bovine retinal transducin is cloned and sequenced and from this the complete amino-acid sequence is deduced.
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