TY - JOUR
T1 - Type-specific regulation of adenylyl cyclase by G protein βγ subunits
AU - Tang, Wei Jen
AU - Gilman, Alfred G.
PY - 1991
Y1 - 1991
N2 - Heterotrimeric guanine nucleotide-binding regulatory proteins (G proteins) dissociate into guanosine triphosphate (GTP)-bound α subunits and a complex of β and γ subunits after interaction with receptors. The GTP-α subunit complex activates appropriate effectors, such as adenylyl cyclase, retinal phosphodiesterase, phospholipase C, and ion channels. G protein βγ subunits have been found to have regulatory effects on certain types of adenylyl cyclase. In the presence of G8α, the α subunit of the G protein that activates adenylyl cyclase, one form of adenylyl cyclase was inhibited by βγ, some forms were activated by βγ, and some forms were not affected by βγ. These interactions suggest mechanisms for communication between distinct signal-transducing pathways.
AB - Heterotrimeric guanine nucleotide-binding regulatory proteins (G proteins) dissociate into guanosine triphosphate (GTP)-bound α subunits and a complex of β and γ subunits after interaction with receptors. The GTP-α subunit complex activates appropriate effectors, such as adenylyl cyclase, retinal phosphodiesterase, phospholipase C, and ion channels. G protein βγ subunits have been found to have regulatory effects on certain types of adenylyl cyclase. In the presence of G8α, the α subunit of the G protein that activates adenylyl cyclase, one form of adenylyl cyclase was inhibited by βγ, some forms were activated by βγ, and some forms were not affected by βγ. These interactions suggest mechanisms for communication between distinct signal-transducing pathways.
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U2 - 10.1126/science.1962211
DO - 10.1126/science.1962211
M3 - Article
C2 - 1962211
AN - SCOPUS:0026418426
SN - 0036-8075
VL - 254
SP - 1500
EP - 1503
JO - Science
JF - Science
IS - 5037
ER -