PMID- 10097092
OWN - NLM
STAT- MEDLINE
DCOM- 19990512
LR  - 20230331
IS  - 0027-8424 (Print)
IS  - 1091-6490 (Electronic)
IS  - 0027-8424 (Linking)
VI  - 96
IP  - 7
DP  - 1999 Mar 30
TI  - Factor-specific modulation of CREB-binding protein acetyltransferase activity.
PG  - 3652-7
AB  - CREB-binding proteins (CBP) and p300 are essential transcriptional coactivators 
      for a large number of regulated DNA-binding transcription factors, including 
      CREB, nuclear receptors, and STATs. CBP and p300 function in part by mediating 
      the assembly of multiprotein complexes that contain additional cofactors such as 
      p300/CBP interacting protein (p/CIP), a member of the p160/SRC family of 
      coactivators, and the p300/CBP associated factor p/CAF. In addition to serving as 
      molecular scaffolds, CBP and p300 each possess intrinsic acetyltransferase 
      activities that are required for their function as coactivators. Here we report 
      that the adenovirus E1A protein inhibits the acetyltransferase activity of CBP on 
      binding to the C/H3 domain, whereas binding of CREB, or a CREB/E1A fusion protein 
      to the KIX domain, fails to inhibit CBP acetyltransferase activity. Surprisingly, 
      p/CIP can either inhibit or stimulate CBP acetyltransferase activity depending on 
      the specific substrate evaluated and the functional domains present in the p/CIP 
      protein. While the CBP interaction domain of p/CIP inhibits acetylation of 
      histones H3, H4, or high mobility group by CBP, it enhances acetylation of other 
      substrates, such as Pit-1. These observations suggest that the acetyltransferase 
      activities of CBP/p300 and p/CAF can be differentially modulated by factors 
      binding to distinct regions of CBP/p300. Because these interactions are likely to 
      result in differential effects on the coactivator functions of CBP/p300 for 
      different classes of transcription factors, regulation of CBP/p300 
      acetyltransferase activity may represent a mechanism for integration of diverse 
      signaling pathways.
FAU - Perissi, V
AU  - Perissi V
AD  - Howard Hughes Medical Institute, University of California at San Diego, La Jolla, 
      CA 92093-0648, USA.
FAU - Dasen, J S
AU  - Dasen JS
FAU - Kurokawa, R
AU  - Kurokawa R
FAU - Wang, Z
AU  - Wang Z
FAU - Korzus, E
AU  - Korzus E
FAU - Rose, D W
AU  - Rose DW
FAU - Glass, C K
AU  - Glass CK
FAU - Rosenfeld, M G
AU  - Rosenfeld MG
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Adenovirus E1A Proteins)
RN  - 0 (Cyclic AMP Response Element-Binding Protein)
RN  - 0 (Histones)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Trans-Activators)
RN  - EC 2.3.1.- (Acetyltransferases)
RN  - EC 2.3.1.48 (CREB-Binding Protein)
RN  - EC 2.3.1.48 (Crebbp protein, rat)
SB  - IM
MH  - Acetylation
MH  - Acetyltransferases/*metabolism
MH  - Adenovirus E1A Proteins/*metabolism
MH  - Animals
MH  - Binding Sites
MH  - CREB-Binding Protein
MH  - Cell Line
MH  - Cyclic AMP Response Element-Binding Protein/metabolism
MH  - Fibroblasts
MH  - Histones/metabolism
MH  - Kinetics
MH  - Nuclear Proteins/*metabolism
MH  - Rats
MH  - Recombinant Fusion Proteins/biosynthesis
MH  - Recombinant Proteins/metabolism
MH  - Substrate Specificity
MH  - Trans-Activators/*metabolism
MH  - Transfection
PMC - PMC22349
EDAT- 1999/03/31 00:00
MHDA- 1999/03/31 00:01
PMCR- 1999/09/30
CRDT- 1999/03/31 00:00
PHST- 1999/03/31 00:00 [pubmed]
PHST- 1999/03/31 00:01 [medline]
PHST- 1999/03/31 00:00 [entrez]
PHST- 1999/09/30 00:00 [pmc-release]
AID - 0472 [pii]
AID - 10.1073/pnas.96.7.3652 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1999 Mar 30;96(7):3652-7. doi: 10.1073/pnas.96.7.3652.