Source:http://linkedlifedata.com/resource/pubmed/id/15150092
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
2004-5-19
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pubmed:abstractText |
hSNF5/INI1, which encodes a component of the ATP-dependent chromatin remodeling hSWI-SNF complex, is a tumor suppressor gene mutated in malignant rhabdoid tumors. We have developed a tetracycline-based hSNF5/INI1-inducible system in a hSNF5/INI1-deficient malignant rhabdoid tumor cell line and studied time course variation of 22,000 genes/expressed sequence tags upon hSNF5/INI1 induction. A total of 482 responsive genes were identified and further clustered into 9 groups of coregulated genes. Among genes with early and strong inductions, the use of a fusion protein with the hormone-binding domain of the estrogen receptor enabled the identification of a subset of direct targets regulated independently of de novo protein synthesis. We show that the G(1) arrest induced by hSNF5/INI1 is reversible and associated with the down-regulation of components of the DNA replication complex. We also identify an unsuspected role of hSNF5/INI1 in cytoskeleton organization. Indeed, induction of hSNF5/INI1 induces dramatic modifications of the cell shape including complete disruption of the actin stress fiber network and disappearance of focal adhesions associated with up-regulation of genes involved in the organization of the actin cytoskeleton. We document a strong decrease of Rho activity upon hSNF5/INI1 expression, suggesting that the regulation of this activity constitutes a crucial step of the hSNF5/INI1-induced reorganization of the actin network. This study identifies hSNF5/INI1 target genes and provides evidence that hSNF5/INI1 may modulate the cell cycle control and cytoskeleton organization through the regulation of the retinoblastoma protein-E2F and Rho pathways.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SMARCB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/rho GTP-Binding Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0008-5472
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
64
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3406-13
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15150092-Actins,
pubmed-meshheading:15150092-Amino Acid Sequence,
pubmed-meshheading:15150092-Cell Division,
pubmed-meshheading:15150092-Cell Line, Tumor,
pubmed-meshheading:15150092-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:15150092-Cytoskeleton,
pubmed-meshheading:15150092-DNA-Binding Proteins,
pubmed-meshheading:15150092-Gene Expression Profiling,
pubmed-meshheading:15150092-Genes, Tumor Suppressor,
pubmed-meshheading:15150092-Humans,
pubmed-meshheading:15150092-Molecular Sequence Data,
pubmed-meshheading:15150092-Rhabdoid Tumor,
pubmed-meshheading:15150092-Transcription Factors,
pubmed-meshheading:15150092-rho GTP-Binding Proteins
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pubmed:year |
2004
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pubmed:articleTitle |
The tumor suppressor hSNF5/INI1 modulates cell growth and actin cytoskeleton organization.
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pubmed:affiliation |
INSERM U509, Laboratoire de Pathologie Moléculaire des Cancers, Institut Curie, Paris, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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