| pubmed-article:18653465 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18653465 | lifeskim:mentions | umls-concept:C0221908 | lld:lifeskim |
| pubmed-article:18653465 | lifeskim:mentions | umls-concept:C1412528 | lld:lifeskim |
| pubmed-article:18653465 | lifeskim:mentions | umls-concept:C0018296 | lld:lifeskim |
| pubmed-article:18653465 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:18653465 | lifeskim:mentions | umls-concept:C0812248 | lld:lifeskim |
| pubmed-article:18653465 | lifeskim:mentions | umls-concept:C1419227 | lld:lifeskim |
| pubmed-article:18653465 | lifeskim:mentions | umls-concept:C1538448 | lld:lifeskim |
| pubmed-article:18653465 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:18653465 | lifeskim:mentions | umls-concept:C0205144 | lld:lifeskim |
| pubmed-article:18653465 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:18653465 | pubmed:dateCreated | 2008-9-29 | lld:pubmed |
| pubmed-article:18653465 | pubmed:abstractText | Small GTPases control key cellular events, including formation of cell-cell junctions and gene expression, and are regulated by activating and inhibiting factors. Here, we characterize the junctional protein paracingulin as a novel regulator of the activity of two small GTPases, Rac1 and RhoA, through the functional interaction with their respective activators, Tiam1 and GEF-H1. In confluent epithelial monolayers, paracingulin depletion leads to increased RhoA activity and increased expression of mRNA for the tight junction protein claudin-2. During tight junction assembly by the calcium-switch, Rac1 shows two transient peaks of activity, at earlier (10-20 min) and later (3-8 h) time points. Paracingulin depletion reduces such peaks of Rac1 activation in a Tiam1-dependent manner, resulting in a delay in junction formation. Paracingulin physically interacts with GEF-H1 and Tiam1 in vivo and in vitro, and it is required for their efficient recruitment to junctions, based on immunofluorescence and biochemical experiments. Our results provide the first description of a junctional protein that interacts with GEFs for both Rac1 and RhoA, and identify a novel molecular mechanism whereby Rac1 is activated during junction formation. | lld:pubmed |
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| pubmed-article:18653465 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18653465 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18653465 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18653465 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18653465 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:18653465 | pubmed:issn | 1939-4586 | lld:pubmed |
| pubmed-article:18653465 | pubmed:author | pubmed-author:CitiSandraS | lld:pubmed |
| pubmed-article:18653465 | pubmed:author | pubmed-author:PaschoudSerge... | lld:pubmed |
| pubmed-article:18653465 | pubmed:author | pubmed-author:GuillemotLaur... | lld:pubmed |
| pubmed-article:18653465 | pubmed:author | pubmed-author:JondLionelL | lld:pubmed |
| pubmed-article:18653465 | pubmed:author | pubmed-author:FogliaAndreaA | lld:pubmed |
| pubmed-article:18653465 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18653465 | pubmed:volume | 19 | lld:pubmed |
| pubmed-article:18653465 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18653465 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18653465 | pubmed:pagination | 4442-53 | lld:pubmed |
| pubmed-article:18653465 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:18653465 | pubmed:meshHeading | pubmed-meshheading:18653465... | lld:pubmed |
| pubmed-article:18653465 | pubmed:meshHeading | pubmed-meshheading:18653465... | lld:pubmed |
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| pubmed-article:18653465 | pubmed:meshHeading | pubmed-meshheading:18653465... | lld:pubmed |
