TY - JOUR
AU - 
AB - Downloaded from genesdev.cshlp.org on December 18, 2021 - Published by Cold Spring Harbor Laboratory Press SREBP transcriptional activity is mediated through an interaction with the CREB-binding protein Jonathan D. Oliner, J. Michael Andresen, Stig K. Hansen, Sharleen Zhou, and Robert Tjian 1 Department of Molecular and Cell Biology, Howard Hughes Medical Institute, University of California, Berkeley, California 94720-3204 USA The sterol regulatory element binding proteins (SREBP-1 and -2) activate transcription of genes whose products are involved in the cellular uptake and synthesis of cholesterol. Although considerable effort has been exerted to define the events regulating the levels of active SREBP, little is known about the transcriptional cofactors mediating SREBP function. In an unbiased search for potential coactivators of SREBP, we isolated a protein of 265 kD from HeLa cells that directly bound SREBP-1 and SREBP-2. Peptide sequencing and Western blot analysis established that the 265-kD protein was CBP (CREB-binding protein), a recently identified transcriptional coactivator. The putative activation domain of SREBP was shown to bind specifically to amino-terminal domains of recombinant CBP and p300 (a CBP-related protein). Moreover, transfection studies demonstrated that CBP enhances the ability of SREBP to activate transcription of reporter genes in HeLa cells. Together, these 
TI - SREBP transcriptional activity is mediated through an interaction with the CREB-binding protein.
JF - Genes & Development
DO - 10.1101/gad.10.22.2903
DA - 1996-11-15
UR - https://www.deepdyve.com/lp/unpaywall/srebp-transcriptional-activity-is-mediated-through-an-interaction-with-1vCmh1D1kP
DP - DeepDyve
ER -