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PMID: 2165866 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

A novel function of the transforming domain of E1a: repression of AP-1 activity.

Cell ·Vol. 62 ·No. 3 ·1990-08-10 ·Pages 527-38

Offringa R, Gebel S, van Dam H, Timmers M, Smits A, Zwart R, Stein B, Bos JL, van der Eb A, Herrlich P

Abstract

Adenovirus E1a represses transcription of the collagenase gene via the phorbol ester-responsive element (collTRE). The mechanism involves inhibition of the trans-activating function of the transcription factor AP-1 without reduction of its synthesis and without any apparent change in DNA binding or composition. The ability of E1a to downmodulate AP-1 is a unique property among dominant oncogenes. This repression depends on conserved region 1, one of the transforming domains of E1a, indicating that it is an integral feature of adenovirus transformation.

MeSH Terms
Adenovirus Early Proteins Animals Base Sequence Cell Line DNA-Binding Proteins/metabolism Enzyme Repression Gene Expression Regulation, Enzymologic HeLa Cells/enzymology Humans Microbial Collagenase/biosynthesis,genetics Molecular Sequence Data Oncogene Proteins, Viral/metabolism Plasmids Promoter Regions, Genetic Protein-Tyrosine Kinases/metabolism Proto-Oncogene Proteins c-jun Receptors, Glucocorticoid/genetics Transcription Factors/metabolism Transcription, Genetic Transfection
Chemicals
Adenovirus Early Proteins DNA-Binding Proteins Oncogene Proteins, Viral Proto-Oncogene Proteins c-jun Receptors, Glucocorticoid Transcription Factors Protein-Tyrosine Kinases Microbial Collagenase
Authors & Affiliations
10 authors, click to expand affiliations / ORCID
Offringa R
Sylvius Laboratories, Laboratory for Molecular Carcinogenesis, University of Leiden, The Netherlands.
Gebel S
van Dam H
Timmers M
Smits A
Zwart R
Stein B
Bos J L
van der Eb A
Herrlich P
Article Info
Journal
Cell
Abbr.
Cell
ISSN
0092-8674
DOI
10.1016/0092-8674(90)90017-9
Published
1990-08-10
Pages
527-38
Language
English
Region
United States
NLM ID
0413066
Subset
IM
External Links
PubMed source DOI: 10.1016/0092-8674(90)90017-9 View journal details
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