Ski-interacting protein, a bifunctional nuclear receptor coregulator that interacts with N-CoR/SMRT and p300.

Ski-interacting protein (SKIP), a vitamin D receptor (VDR) coactivator, also functions as a repressor in Notch signalling in association with the corepressor SMRT. Here we show that SKIP bifunctionally modulates (activates or represses) Retinoid-X receptor (RXR)- and VDR-dependent gene transcription in a cell line-specific manner, with activation in CV-1 and ...
repression in P19 cells. The coactivator function of SKIP in these cells appeared to correlate with the relative level and ratio of expression of N-CoR and p300, with greater SKIP activation in higher p300-expressing and lower N-CoR-expressing cell-lines. C-terminal deletion of SKIP (delta334-536 aa) was associated with strong activation in both CV-1 and P19 cells. The corepressors N-CoR and SMRT and the coregulator p300 interacted with SKIP through the same N-terminal region (1-200 aa). Overall these results suggest that transcriptional action of SKIP may depend on distinct functional domains and cell line-specific interactions with both corepressors and coactivators.
Mesh Terms:
Acetyltransferases, Animals, COS Cells, Cell Cycle Proteins, Cell Line, Cercopithecus aethiops, DNA-Binding Proteins, Gene Expression, Histone Acetyltransferases, Mice, NIH 3T3 Cells, Nuclear Proteins, Nuclear Receptor Co-Repressor 2, Receptors, Calcitriol, Receptors, Cytoplasmic and Nuclear, Receptors, Retinoic Acid, Recombinant Fusion Proteins, Repressor Proteins, Retinoid X Receptors, Sequence Deletion, Transcription Factors, Transcription, Genetic, Transcriptional Activation, p300-CBP Transcription Factors
Biochem. Biophys. Res. Commun.
Date: Mar. 19, 2004
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