Rod photoreceptors of mammalian retinas contain a 33-kDa
phosphoprotein,
phosducin, which complexes with the beta, gamma-subunits of
transducin (T beta gamma). The level of
phosducin phosphorylation is modulated by light, suggesting that the
phosducin/T beta gamma complex has a pivotal role in light-regulated events that occur in photoreceptors. We have investigated, in developing mouse retinas, the age at which the complex is first detected and the subsequent accumulation of the
phosducin/T beta gamma complex during postnatal life. Western blot analysis detected immunoreactivity both for
phosducin and T beta in
retinal homogenates of 3-day-old mice. Thereafter, the level of immunoreactivity for both
proteins increased steadily, to reach adult levels in the next 2 postnatal weeks. Gel filtration analysis of extracts from immature mouse retina showed that
phosducin and T beta co-eluted, like the
phosducin/T beta gamma complex of adult retina, as a 77-kDa complex, indicating that the
phosducin/T beta gamma complex is formed when photoreceptors first synthesize the components of the complex. While the levels of the
phosducin/T beta gamma complex increased steadily during the first 2 postnatal weeks, the subunits of
transducin complex, T alpha together with additional amounts of T beta gamma, only started to appear around the 7-9th postnatal day, and the level of
transducin complex increased sharply at 11-14 days to reach adult levels that are similar to those of
phosducin/T beta gamma complex.(ABSTRACT TRUNCATED AT 250 WORDS)