Published online 31 October 2005. doi:10.1083/jcb1713iti4
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 171, Number 3, 405-405
G proteins live in excess
On page 517, Elia et al. show how fly photoreceptors achieve their exquisite sensitivity to a single photon of light. The key is not the number of photoreceptor-activating proteins but the ratios of their components.
Photoreceptor sensitivity depends on extremely low levels of spontaneous activity in the dark. This activity, spontaneous or otherwise, depends on a G protein coupled to the rhodopsin receptor. Rhodopsin activation induces the G protein's
subunit to exchange its bound GDP for GTP, dissociate from its binding partner, ß
, and initiate downstream signaling. The group now finds that excess ß
ensures that
is not activated in the dark.
Wild-type photoreceptors had over twofold more ß
than
and low background activity. Mutants with less ß
had much more spontaneous activity. This defect was corrected by simultaneously reducing
levels in the mutant (thus restoring the ß
excess).
Spontaneous activity was actually higher in cells with moderate rather than extreme reduction in ß
. The authors explain this finding by showing that ß
was needed to bring
to the rhabdomere, from which
signals. Thus, in stronger ß
mutants, there was less
able to signal and hence less spontaneous activity.
The group must now determine how the excess ß
limits
activity. Perhaps it either accelerates GTP hydrolysis on
to block the downstream cascade or prevents the unsolicited exchange of GDP for GTP on
.
Nicole LeBrasseur
lebrasn{at}rockefeller.edu

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J. Cell Biol. 2005 171: 517-526.
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