| pubmed-article:18319303 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18319303 | lifeskim:mentions | umls-concept:C0030211 | lld:lifeskim |
| pubmed-article:18319303 | lifeskim:mentions | umls-concept:C0042172 | lld:lifeskim |
| pubmed-article:18319303 | lifeskim:mentions | umls-concept:C0001511 | lld:lifeskim |
| pubmed-article:18319303 | lifeskim:mentions | umls-concept:C0751984 | lld:lifeskim |
| pubmed-article:18319303 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:18319303 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:18319303 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:18319303 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:18319303 | lifeskim:mentions | umls-concept:C0332453 | lld:lifeskim |
| pubmed-article:18319303 | pubmed:issue | Pt 7 | lld:pubmed |
| pubmed-article:18319303 | pubmed:dateCreated | 2008-3-20 | lld:pubmed |
| pubmed-article:18319303 | pubmed:abstractText | E-cadherin cell-cell adhesion plays a major role in the maintenance of the morphology and function of epithelial tissues. Modulation of E-cadherin function is an important process in morphogenesis and tumour de-differentiation. We have previously shown that constitutively active Rac1 induces the disassembly of E-cadherin complexes from junctions in human keratinocytes. Here, we compare this activity in three members of the Rac subfamily (Rac1, Rac3 and Rac1b) and investigate the molecular mechanisms underlying Rac1-induced destabilization of junctions. We demonstrate that Rac3 shares with Rac1 the ability to interfere with cadherin-mediated adhesion. Rac1b is an alternative splice variant of Rac1 but, surprisingly, Rac1b cannot induce junction disassembly. Thus, Rac family members differ on their potential to perturb keratinocyte cell-cell contacts. The mechanism through which Rac promotes disassembly of cadherin-dependent adhesion does not involve an increase in contractility. Instead, activation of the Rac target PAK1 is necessary for destabilization of cell-cell contacts. Inhibition of PAK1 by dominant-negative constructs or depletion of endogenous PAK1 by RNA interference efficiently blocked Rac1-induced perturbation of junctions. Interestingly, PAK1 cannot be activated by Rac1b, suggesting that this may contribute to the inability of Rac1b to disrupt cell-cell contacts in keratinocytes. As PAK1 also plays a crucial role in lamellipodia formation, our data indicate that PAK1 is at the interface between junction destabilization and increased motility during morphogenetic events. | lld:pubmed |
| pubmed-article:18319303 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18319303 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18319303 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18319303 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18319303 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18319303 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18319303 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18319303 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18319303 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18319303 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18319303 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18319303 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:18319303 | pubmed:issn | 0021-9533 | lld:pubmed |
| pubmed-article:18319303 | pubmed:author | pubmed-author:KnausUlla GUG | lld:pubmed |
| pubmed-article:18319303 | pubmed:author | pubmed-author:BragaVania... | lld:pubmed |
| pubmed-article:18319303 | pubmed:author | pubmed-author:LozanoEncarna... | lld:pubmed |
| pubmed-article:18319303 | pubmed:author | pubmed-author:SmolarczykKat... | lld:pubmed |
| pubmed-article:18319303 | pubmed:author | pubmed-author:FrasaMarieke... | lld:pubmed |
| pubmed-article:18319303 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18319303 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:18319303 | pubmed:volume | 121 | lld:pubmed |
| pubmed-article:18319303 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18319303 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18319303 | pubmed:pagination | 933-8 | lld:pubmed |
| pubmed-article:18319303 | pubmed:meshHeading | pubmed-meshheading:18319303... | lld:pubmed |
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| pubmed-article:18319303 | pubmed:meshHeading | pubmed-meshheading:18319303... | lld:pubmed |
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| pubmed-article:18319303 | pubmed:meshHeading | pubmed-meshheading:18319303... | lld:pubmed |
| pubmed-article:18319303 | pubmed:meshHeading | pubmed-meshheading:18319303... | lld:pubmed |
| pubmed-article:18319303 | pubmed:meshHeading | pubmed-meshheading:18319303... | lld:pubmed |
| pubmed-article:18319303 | pubmed:meshHeading | pubmed-meshheading:18319303... | lld:pubmed |
| pubmed-article:18319303 | pubmed:meshHeading | pubmed-meshheading:18319303... | lld:pubmed |
| pubmed-article:18319303 | pubmed:meshHeading | pubmed-meshheading:18319303... | lld:pubmed |
| pubmed-article:18319303 | pubmed:meshHeading | pubmed-meshheading:18319303... | lld:pubmed |
| pubmed-article:18319303 | pubmed:meshHeading | pubmed-meshheading:18319303... | lld:pubmed |
| pubmed-article:18319303 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18319303 | pubmed:articleTitle | PAK is required for the disruption of E-cadherin adhesion by the small GTPase Rac. | lld:pubmed |
| pubmed-article:18319303 | pubmed:affiliation | Molecular Medicine Section, NHLI, Faculty of Medicine, Imperial College London, London, SW7 2AZ, UK. v.braga@imperial.ac.uk | lld:pubmed |
| pubmed-article:18319303 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18319303 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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