Cyclin E Associates with BAF155 and BRG1, Components of the Mammalian SWI-SNF Complex, and Alters the Ability of BRG1 To Induce Growth Arrest
- 1 February 1999
- journal article
- research article
- Published by Taylor & Francis in Molecular and Cellular Biology
- Vol. 19 (2), 1460-1469
- https://doi.org/10.1128/mcb.19.2.1460
Abstract
SWI-SNF complexes have been implicated in transcriptional regulation by chromatin remodeling. We have identified an interaction between two components of the mammalian SWI-SNF complex and cyclin E, an essential cell cycle regulatory protein required for G1/S transition. BRG1 and BAF155, mammalian homologs of yeast SWI2 and SWI3, respectively, are found in cyclin E complexes and are phosphorylated by cyclin E-associated kinase activity. In this report, we show that overexpression of BRG1 causes growth arrest and induction of senescence-associated β-galactosidase activity, which can be overcome by cyclin E. Our results suggest that cyclin E may modulate the activity of the SWI-SNF apparatus to maintain the chromatin in a transcriptionally permissive state.Keywords
This publication has 70 references indexed in Scilit:
- Activated RSC–Nucleosome Complex and Persistently Altered Form of the NucleosomeCell, 1998
- Cyclin E-induced S phase without activation of the pRb/E2F pathway.Genes & Development, 1997
- Cancer Cell CyclesScience, 1996
- Principles of CDK regulationNature, 1995
- Cyclin dependent kinase regulationCurrent Opinion in Cell Biology, 1995
- Nucleosome disruption and enhancement of activator binding by a human SW1/SNF complexNature, 1994
- BRG1 contains a conserved domain of the SWI2/SNF2 family necessary for normal mitotic growth and transcriptionNature, 1993
- Direct binding of cyclin D to the retinoblastoma gene product (pRb) and pRb phosphorylation by the cyclin D-dependent kinase CDK4Genes & Development, 1993
- Interaction of p107 with Cyclin A Independent of Complex Formation with Viral OncoproteinsScience, 1992
- G1/S phosphorylation of the retinoblastoma protein is associated with an altered affinity for the nuclear compartmentCell, 1991