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Abstract
The cyclic adenosine monophosphate response element-binding protein (CREB) is a transcription
factor that contributes to memory formation. The transcriptional activity of CREB
is induced by its phosphorylation at Ser-133 and subsequent interaction with the CREB-binding
protein (CBP)/p300. We designed and optimized firefly split luciferase probe proteins
that detect the interaction of the kinase-inducible domain (KID) of CREB and the KIX
domain of CBP/p300. The increase in the light intensity of the probe proteins results
from the phosphorylation of the responsible serine corresponding to Ser-133 of CREB.
Because these proteins have a high signal-to-noise ratio and are nontoxic, it has
become possible for the first time to carry out long-term measurement of KID-KIX interaction
in living cells. Furthermore, we examined the usefulness of the probe proteins for
future high-throughput cell-based drug screening and found several herbal extracts
that activated CREB.