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rdf:type |
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lifeskim:mentions |
umls-concept:C0015744,
umls-concept:C0851285,
umls-concept:C1269955,
umls-concept:C1414047,
umls-concept:C1422475,
umls-concept:C1446409,
umls-concept:C1521816,
umls-concept:C1824154,
umls-concept:C1824843,
umls-concept:C2699153,
umls-concept:C2911691
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pubmed:issue |
12
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pubmed:dateCreated |
2007-6-18
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pubmed:abstractText |
The RhoA-effector Dia1 controls actin-dependent processes such as cytokinesis, SRF transcriptional activity, and cell motility. Dia1 polymerizes actin through its formin homology (FH) 2 domain. Here we show that Dia1 acts upstream of RhoA independently of its effects on actin assembly. Dia1 binds to the leukemia-associated Rho-GEF (LARG) through RhoA-dependent release of Dia1 autoinhibition. The FH2 domain stimulates the guanine nucleotide exchange activity of LARG in vitro. Our results reveal that Dia1 is necessary for LPA-stimulated Rho/ROCK signaling and bleb-associated cancer cell invasion. Thus, Dia1-dependent RhoA activation constitutes a positive feedback mechanism to modulate cell behavior.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17575049-10428028,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17575049-10681437,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17575049-11779461,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17575049-12021256,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17575049-12429848,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17575049-12635176,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17575049-12717816,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17575049-12732141,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17575049-12771155,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17575049-12778124,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17575049-12805219,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17575049-12844144,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17575049-12894246,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17575049-14712228,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17575049-14992721,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17575049-15006353,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17575049-15150101,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17575049-15488183,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17575049-15488184,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17575049-15591319,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17575049-15661538,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17575049-15689371,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17575049-16251183,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17575049-16292343,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17575049-16740473,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17575049-16890527,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17575049-17306570
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ARHGEF12 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/DIAPH1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Exchange Factors,
http://linkedlifedata.com/resource/pubmed/chemical/RHOA protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Lysophosphatidic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/rhoA GTP-Binding Protein
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0890-9369
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
21
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1478-83
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:17575049-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:17575049-Cell Line,
pubmed-meshheading:17575049-Cell Line, Tumor,
pubmed-meshheading:17575049-Feedback,
pubmed-meshheading:17575049-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:17575049-Humans,
pubmed-meshheading:17575049-Models, Biological,
pubmed-meshheading:17575049-Mutation,
pubmed-meshheading:17575049-Neoplasm Invasiveness,
pubmed-meshheading:17575049-RNA, Small Interfering,
pubmed-meshheading:17575049-Receptors, Lysophosphatidic Acid,
pubmed-meshheading:17575049-Signal Transduction,
pubmed-meshheading:17575049-rhoA GTP-Binding Protein
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pubmed:year |
2007
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pubmed:articleTitle |
Positive feedback between Dia1, LARG, and RhoA regulates cell morphology and invasion.
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pubmed:affiliation |
Institute of Pharmacology, University of Heidelberg, 69120 Heidelberg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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