TI  -  SREBP  transcriptional activity is mediated through an interaction with the
       <prot><prot>CREB</prot>-binding protein</prot> .
PG  - 2903-11
AB  - The sterol regulatory element binding proteins (<prot>SREBP-1</prot> 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  <prot>SREBP-1</prot>  and  <prot>SREBP-2</prot> .
      Peptide sequencing and Western blot analysis established that the 265-kD
      protein was   <prot>CBP</prot> (<prot>CREB-binding protein</prot>)   a recently identified
      transcriptional coactivator. The putative activation domain of   SREBP   was
      shown to bind specifically to amino-terminal domains of recombinant  <prot>CBP</prot> 
      and  <prot>p300</prot> (a <prot>CBP</prot>-related protein) . Moreover, transfection studies
      demonstrated that <prot>CBP</prot> enhances the ability of SREBP to activate
      transcription of reporter genes in HeLa cells. Together, these data
      suggest that  <prot>CBP</prot>  mediates  SREBP  transcriptional activity, thus revealing a
      new step in the biochemical pathway regulating cholesterol metabolism.
AD  - Department of Molecular and Cell Biology, Howard Hughes Medical Institute,
