PMID: 2504150Jun 15, 1989Paper

Persistent activation of the alpha subunit of Gs promotes its removal from the plasma membrane

The Biochemical Journal
G Milligan, C G Unson

Abstract

As assessed both by cholera-toxin-catalysed ADP-ribosylation and by immunoblotting with an anti-peptide antiserum raised against the C-terminal decapeptide of forms of Gs alpha (the alpha subunit of the stimulatory guanine nucleotide-binding protein), rat glioma C6 BU1 cells express two forms of Gs alpha: a major 44 kDa form and a much less prevalent 42 kDa form. We examined the effects of guanine nucleotides on the interaction of the 44 kDa form with the plasma membrane. Incubation of membranes of C6 BU1 cells with poorly hydrolysed analogues of GTP, but not with analogues of either ATP or GDP, caused the release of this Gs alpha from the membrane fraction. Release of Gs alpha was observed within 5 min, and continued throughout the incubation period. After treatment with guanosine 5'-[beta gamma-imido]triphosphate for 60 min, some 75% of this polypeptide had been released from its site of membrane attachment. These experiments demonstrate that Gs alpha need not remain associated invariantly with the plasma membrane.

Citations

Jul 1, 1991·Journal of Neurochemistry·M McLaughlinJ T Knowler
Dec 1, 1994·Journal of Bone and Mineral Research : the Official Journal of the American Society for Bone and Mineral Research·M RansjöO Ljunggren
Apr 13, 1999·The American Journal of Physiology·J M ArthurJ R Raymond
Jan 22, 1992·Biochemical Pharmacology·J R Jasper, P A Insel
Sep 1, 1990·Biochimica Et Biophysica Acta·L KhachatrianB F Dickey
Jan 11, 1994·Biochimica Et Biophysica Acta·C J ClarkJ M Connell
Aug 12, 1992·Biochimica Et Biophysica Acta·D Gingras, R Béliveau
Jul 24, 2002·Biochemistry·Manimekalai M ThiyagarajanPhilip B Wedegaertner

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