Home LiteratureArticle Details
PMID: 10446255 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

E2F/p107 and E2F/p130 complexes are regulated by C/EBPalpha in 3T3-L1 adipocytes.

Nucleic acids research ·Vol. 27 ·No. 17 ·1999-09-01 ·Pages 3621-30

Timchenko NA, Wilde M, Iakova P, Albrecht JH, Darlington GJ

Abstract

We have previously found that loss of C/EBPalpha in hepatocytes of newborn livers leads to increased proliferation, to a reduction in p21 protein levels and to an induction of S phase-specific E2F/p107 complexes. In this paper, we investigated C/EBPalpha-dependent regulation of E2F complexes in a well-characterized cell line, 3T3-L1, and in stable transformants that conditionally express C/EBPalpha. C/EBPalpha and C/EBPbeta proteins are induced in 3T3-L1 preadipocytes during differentiation with different kinetics and potentially may regulate E2F/Rb family complexes. In pre-differentiated cells, three E2F complexes are observed: cdk2/E2F/p107, E2F/p130 and E2F4. cdk2/E2F/p107 complexes are induced in nuclear extracts of 3T3-L1 cells during mitotic expansion, but are not detectable in nuclear extracts at later stages of 3T3-L1 differentiation. The reduction in E2F/p107 complexes is associated with elevation of C/EBPalpha, but is independent of C/EBPbeta expression. Bacterially expressed, purified His-C/EBPalpha is able to disrupt E2F/p107 complexes that are observed at earlier stages of 3T3-L1 differentiation. C/EBPbeta, however, does not disrupt E2F/p107 complexes. A short C/EBPalpha peptide with homology to E2F is sufficient to bring about the disruption of E2F/p107 complexes from 3T3-L1 cells in vitro. Induction of C/EBPalpha in stable 3T3-L1 clones revealed that C/EBPalpha causes disruption of p107/E2F complexes in these cells. In contrast, E2F/p130 complexes are induced in cells expressing C/EBPalpha. Our data suggest that induction of p130/E2F complexes by C/EBPalpha occurs via up-regulation of p21, which, in turn, leads to association with and inhibition of, cdk2 kinase activity. The reduction in cdk2 kinase activity correlates with alterations of p130 phosphorylation and with induction of p130/E2F complexes in 3T3-L1 stable clones. Our data suggest two pathways of C/EBPalpha-dependent regulation of E2F/Rb family complexes: disruption of S phase-specific E2F/p107 complexes and induction of E2F/p130 complexes.

MeSH Terms
3T3 Cells Adipocytes/metabolism Animals CCAAT-Enhancer-Binding Proteins CDC2-CDC28 Kinases Carrier Proteins Cell Cycle Proteins Cell Differentiation Cyclin E/metabolism Cyclin-Dependent Kinase 2 Cyclin-Dependent Kinases/metabolism DNA-Binding Proteins/metabolism E2F Transcription Factors E2F4 Transcription Factor Gene Expression Regulation Glutathione Transferase/metabolism Mice Nuclear Proteins/metabolism Phosphoproteins/metabolism Phosphorylation Protein Binding Protein Serine-Threonine Kinases/metabolism Proteins Proto-Oncogene Proteins p21(ras)/metabolism Recombinant Fusion Proteins/metabolism Retinoblastoma-Binding Protein 1 Retinoblastoma-Like Protein p107 Retinoblastoma-Like Protein p130 Time Factors Transcription Factor DP1 Transcription Factors/metabolism
Chemicals
Arid4a protein, mouse CCAAT-Enhancer-Binding Proteins Carrier Proteins Cell Cycle Proteins Cyclin E DNA-Binding Proteins E2F Transcription Factors E2F4 Transcription Factor E2f4 protein, mouse Nuclear Proteins Phosphoproteins Proteins Rbl1 protein, mouse Rbl2 protein, mouse Recombinant Fusion Proteins Retinoblastoma-Binding Protein 1 Retinoblastoma-Like Protein p107 Retinoblastoma-Like Protein p130 Transcription Factor DP1 Transcription Factors Glutathione Transferase Protein Serine-Threonine Kinases CDC2-CDC28 Kinases Cdk2 protein, mouse Cyclin-Dependent Kinase 2 Cyclin-Dependent Kinases Proto-Oncogene Proteins p21(ras)
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Timchenko N A
Huffington Center on Aging, Department of Pathology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA. [email protected]
Wilde M
Iakova P
Albrecht J H
Darlington G J
Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
1362-4962
Published
1999-09-01
Pages
3621-30
Language
English
Region
England
NLM ID
0411011
PMCID
PMC148609
Subset
IM
Grants
NIA NIH HHS · AG00766 · United States
NIDDK NIH HHS · DK45285 · United States
NIGMS NIH HHS · GM55188 · United States
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]