In:
Genes & Development, Cold Spring Harbor Laboratory, Vol. 12, No. 2 ( 1998-01-15), p. 233-245
Abstract:
Transcriptional activation of the c- jun gene is a critical event in the differentiation of F9 cells. In our previous studies we characterized an element [differentiation response element (DRE)] in the c- jun promoter that is both necessary and sufficient to confer the capacity for differentiation-dependent up-regulation. This element binds the differentiation regulatory factor (DRF) complex, of which one component is the adenovirus E1A-associated protein p300. We have now identified activation transcription factor-2 (ATF-2) as a DNA-binding subunit of the DRF complex. p300 and ATF-2 interact with each other in vivo and in vitro. The bromodomain and the C/H2 domain of p300 mediate the binding to ATF-2, which in turn requires a proline-rich region between amino acids 112 and 350 for its interaction with p300. The phosphorylation of the serine residue at position 121 of ATF-2 appears to be induced by protein kinase Cα (PKCα) after treatment of cells with retinoic acid (RA) or induction with E1A. In cotransfection assays, wild-type ATF-2 enhanced the transcription of an E2/tk–luciferase construct, in conjunction with p300–E2. However, a mutant form of ATF-2 with a mutation at position 121 (pCMVATF–2 Ser121–Ala ) did not. These results suggest that ATF-2 and p300 cooperate in the control of transcription by forming a protein complex that is responsive to differentiation-inducing signals, such as RA or E1A, and moreover, that the phosphorylation of ATF-2 by PKCα is probably a signaling event in the pathway that leads to the transactivation of the c- jun gene in F9 cells.
Type of Medium:
Online Resource
ISSN:
0890-9369
,
1549-5477
DOI:
10.1101/gad.12.2.233
Language:
English
Publisher:
Cold Spring Harbor Laboratory
Publication Date:
1998
detail.hit.zdb_id:
1467414-2
SSG:
12
