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ADENOVIRAL E1A-ASSOCIATED PROTEIN P300 AS A FUNCTIONAL HOMOLOG OF THE TRANSCRIPTIONAL COACTIVATOR CBP
Author(s): LUNDBLAD JR, KWOK RPS, LAURANCE ME, HARTER ML, GOODMAN RH
Source: NATURE    Volume: 374    Issue: 6517    Pages: 85-88    Published: MAR 2 1995  
Times Cited: 464     References: 21     
Abstract: THE 265K nuclear protein CBP was initially identified as a coactivator for the protein kinase A (PKA)-phosphorylated form of the transcription factor CREB(1). The domains in CBP that are involved in CREB binding and transcriptional activation are highly related to the adenoviral E1A-associated cellular protein p300 (refs 2, 3), and to two hypothetical proteins from Caenorhabditis elegans, R10E11.1 and K03H1.10 (refs 4 and 5, respectively), whose functions are unknown. Here, we show that CBP and p300 have similar binding affinity for the PKA-phosphorylated form of CREB, and that p300 can substitute for CBP in potentiating CREB-activated gene expression. We find that E1A binds to CBP through a domain conserved with p300 acid represses the CREB-dependent co-activator functions of both CBP and p300. Our results indicate that the gene repression and cell immortalization functions associated with E1A involve the inactivation of a family of related proteins that normally participate in second-messenger-regulated gene expression.
Document Type: Article
Language: English
Addresses:
1. OREGON HLTH SCI UNIV, VOLLUM INST, PORTLAND, OR 97201 USA
2. CLEVELAND CLIN, RES INST, DEPT MOLEC BIOL, CLEVELAND, OH 44195 USA
Publisher: MACMILLAN MAGAZINES LTD, 4 LITTLE ESSEX STREET, LONDON, ENGLAND WC2R 3LF
Subject Category: Multidisciplinary Sciences
IDS Number: QK079
ISSN: 0028-0836
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