G Protein Alpha Transducin
G protein alpha transducin was purified from bovine retinal extracts more than three decades ago. The discovery of transducin was the culmination of a series of findings that started in the mid-1970s (see Bourne 2006 for a recent review), beginning with the identification of the effector molecule cGMP phosphodiesterase (Bitensky et al. 1975). Shortly afterward, the presence of light-induced GTPase activity in rod outer segment extracts was described (Wheeler and Bitensky 1977). In 1978, activation of cGMP phosphodiesterase was shown to require activated rhodopsin and the presence of GTP (Yee and Liebman 1978). In 1979, a soluble guanine nucleotide binding protein with light-activated GTP–GDP exchange was purified (Godchaux and Zimmerman 1979). However, only two components, the a and β subunits, of the heterotrimeric G protein transducin were described. In 1981, the full heterotrimeric G protein was purified in Lubert...
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