A CBP integrator complex mediates translational activation and AP-1 inhibition by nuclear receptors

Article Abstract:

Research indicates that CREB (cAMP Response Element-Binding Protein)-binding protein (CBP) is an inhibiting factor in the process of genetic regulation. CBP interacts with phosphorylated CREB together with the protein p600. The CBP/p600 complex activates the transduction of various signals in the nucleus. This is achieved by the process of ligand-binding in the receptors of DNA. CBP also serves as an integrator that controls the signals necessary to initiate various metabolic activities making it a SRC-1 derivative.

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A corepressor/coactivator exchange complex required for transcriptional activation by nuclear receptors and other regulated transcription factors

Article Abstract:

The transcriptional activation mediated by liganded nuclear receptors unexpectedly requires the actions of two highly related F box/WD-40-containing factors, TBL1 and TBLR1. The role of TBLR1 and TBL1 in cofactor exchange appears to also operate for c-Jun and NF(kappa)B and is therefore likely to be a prototypic of similar mechanisms for other signal-dependent transcription factors.

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Activating the PARP-1 sensor component of the groucho/TLE1 corepressor complex mediates a CaMKinase II delta-dependent neurogenic gene activation pathway

Article Abstract:

Tests were conducted to know more about a pathway in which the induction of CaMKIIdelta triggers a sudden switch in the function of the HES1 transcription factor. It was found that the CaMKIIdelta mediates necessary phosphorylation of HES1 to allow neurogenic gene activation.

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