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Proper processing of a G protein γ subunit depends on complex formation with a β subunit
Author(s) -
Pronin Alexey N.,
Gautam Narasimhan
Publication year - 1993
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(93)80971-v
Subject(s) - protein subunit , specificity factor , gi alpha subunit , intracellular , gamma aminobutyric acid receptor subunit alpha 1 , cell fractionation , microbiology and biotechnology , scn3a , chemistry , biology , biochemistry , g alpha subunit , enzyme , gene , rna dependent rna polymerase , polymerase
G protein β and γ subunits function as a tightly associated complex. We show that complex formation with the β subunit is a critical step for post‐translational processing of a γ subunit. When expressed alone in a cell line, the γ3 subunit type is isoprenylated but degraded; co‐expression with theβ1 subunit type stabilizes the γ3 protein. Furthermore, our experiments with partial cell fractionation indicate that the γ3 protein is localized differently in the cell depending on whether or not it is bound to the β subunit. Binding of the γ subunit to the β subunit is thus one of the prerequisites for the appropriate intracellular localization of the βγ complex and potentially, for normal G‐protein function.