Increased palmitoylation of the Gs protein alpha subunit after activation by the beta-adrenergic receptor or cholera toxin.

This publication has 22 references indexed in Scilit:

• The G protein .alpha.s subunit incorporates [3H]palmitic acid and mutation of cysteine-3 prevents this modification
  Biochemistry, 1993
• Structural elements of Gα subunits that interact with Gβγ, receptors, and effectors
  Cell, 1993
• Amino- and carboxy-terminal deletion mutants of Gs alpha are localized to the particulate fraction of transfected COS cells.
  The Journal of cell biology, 1992
• Insulin stimulates fatty acid acylation of adipocyte proteins
  Biochemical and Biophysical Research Communications, 1991
• Agonist-enhanced palmitoylation of platelet proteins
  Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1989
• Fatty Acylation of Proteins
  Annual Review of Cell Biology, 1988
• A mutation that prevents GTP-dependent activation of the α chain of Gs
  Nature, 1988
• G protein multiplicity in eukaryotic signal transduction systems
  Biochemistry, 1988
• Identification of receptor contact site involved in receptor–G protein coupling
  Nature, 1987
• Myristoylated alpha subunits of guanine nucleotide-binding regulatory proteins.
  Proceedings of the National Academy of Sciences, 1987