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Guanine nucleotide dependent and independent reconstitution of G‐proteins with adenylate cyclase: stimulation or attenuation of the enzyme by Gi α subunits
Author(s) -
Newton Dianne L.,
Klee Werner A.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80407-a
Subject(s) - adenylate kinase , cyclase , gtp' , g protein , enzyme , biochemistry , gtp binding protein regulators , adenylate cyclase toxin , g alpha subunit , nucleotide , phospholipid , stimulation , gi alpha subunit , chemistry , biology , protein subunit , membrane , pertussis toxin , signal transduction , endocrinology , gene
The α subunits of five members of the Gi family of bovine brain proteins were reconstituted with adenylate cyclase in phospholipid vesicles. Our results support both the views that much of the inhibition of the enzyme by Gi is due to the action of its liberated βγ subunits, and that the α subunits themselves interact with the enzyme. Inhibition of basal or Gs‐stimulated adenylate cyclase activity is small or undetectable by a subunits of Go, Go ∗ and Gi‐2B. On the other hand, adenylate cyclase activity is stimulated by the α subunits of Gi‐1 and Gi‐2A. The G proteins act in the absence of added GTP when reconstituted with phospholipids of low but not high fluidity.