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Title: Glucagon induces disaggregation of polymer-like structures of the. alpha. subunit of the stimulatory G protein in liver membranes

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America; (United States)
;  [1]
  1. National Inst. of Environmental Health Sciences, Research Triangle Park, NC (United States)

The hydrodynamic behavior of G{alpha}{sub s}, the {alpha} subunit of the stimulatory guanine nucleotide-binding regulatory protein (G protein), in octyl glucoside extracts of rat liver membranes was investigated. As was previously shown for G proteins similarly extracted from brain synaptoneurosomes, G{alpha}{sub s} behaved as polydisperse structures with S values higher than that of heterotrimeric G proteins. When G{alpha}{sub s} in its membrane-bound form was ({sup 32}P)ADP-ribosylated by cholera toxin and the treated membranes were extracted with octyl glucoside, > 35% of the labeled G{alpha}{sub s} was found in material that sedimented through sucrose gradients and contained relatively low levels of immunoreactive G{alpha}{sub s}. These finding suggest that the glucagon receptor selectivity interacts with polymer-like structures of G{alpha}{sub 2} and that activation by GTP({gamma}S) results in disaggregation. The role of the {beta} and {gamma} subunits of G proteins in the hormone-induced process is not clear since the polymer-like structures extracted with octyl glucoside are devoid of {beta} and {gamma} subunits.

OSTI ID:
5703207
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America; (United States), Vol. 88:16; ISSN 0027-8424
Country of Publication:
United States
Language:
English

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