Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 24
pubmed:dateCreated
2004-11-11
pubmed:abstractText
The SWI/SNF enzymes belong to a family of ATP-dependent chromatin remodeling enzymes that have been functionally implicated in gene regulation, development, differentiation and oncogenesis. BRG1, the catalytic core subunit of some of the SWI/SNF enzymes, can interact with known tumor suppressor proteins and can act as a tumor suppressor itself. We report that cells that inducibly express ATPase-deficient versions of BRG1 increase in cell volume, area of attachment and nuclear size upon expression of the mutant BRG1 protein. Examination of focal adhesions reveals qualitative changes in paxillin distribution but no difference in the actin cytoskeletal structure. Increases in cell size and shape correlate with over-expression of two integrins and the urokinase-type plasminogen activator receptor (uPAR), which is also involved in cell adhesion and is often over-expressed in metastatic cancer cells. These findings demonstrate that gene expression pathways affected by chromatin remodeling enzymes can regulate the physical dimensions of mammalian cell morphology.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Actins, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Chromatin, http://linkedlifedata.com/resource/pubmed/chemical/Collagen, http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary, http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases, http://linkedlifedata.com/resource/pubmed/chemical/Drug Combinations, http://linkedlifedata.com/resource/pubmed/chemical/Laminin, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/PLAUR protein, human, http://linkedlifedata.com/resource/pubmed/chemical/PXN protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Paxillin, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Plaur protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Proteoglycans, http://linkedlifedata.com/resource/pubmed/chemical/Pxn protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Urokinase Plasminogen..., http://linkedlifedata.com/resource/pubmed/chemical/SMARCA4 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Smarca4 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/matrigel
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9533
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
117
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5847-54
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:15537831-Humans, pubmed-meshheading:15537831-Animals, pubmed-meshheading:15537831-Mice, pubmed-meshheading:15537831-Collagen, pubmed-meshheading:15537831-Adenosine Triphosphatases, pubmed-meshheading:15537831-Mutation, pubmed-meshheading:15537831-Actins, pubmed-meshheading:15537831-Drug Combinations, pubmed-meshheading:15537831-Adenosine Triphosphate, pubmed-meshheading:15537831-Cell Nucleus, pubmed-meshheading:15537831-Neoplasm Metastasis, pubmed-meshheading:15537831-Time Factors, pubmed-meshheading:15537831-Cell Differentiation, pubmed-meshheading:15537831-Chromatin, pubmed-meshheading:15537831-RNA, Messenger, pubmed-meshheading:15537831-Protein Binding, pubmed-meshheading:15537831-Heterozygote, pubmed-meshheading:15537831-Cell Line, pubmed-meshheading:15537831-Dose-Response Relationship, Drug, pubmed-meshheading:15537831-Cell Adhesion, pubmed-meshheading:15537831-Nuclear Proteins, pubmed-meshheading:15537831-Cell Line, Tumor, pubmed-meshheading:15537831-Protein Structure, Tertiary, pubmed-meshheading:15537831-Cell Size, pubmed-meshheading:15537831-Phosphoproteins, pubmed-meshheading:15537831-Receptors, Cell Surface, pubmed-meshheading:15537831-Cytoskeleton, pubmed-meshheading:15537831-Gene Expression Regulation, pubmed-meshheading:15537831-Proteoglycans, pubmed-meshheading:15537831-DNA, Complementary
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