| pubmed-article:16027725 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16027725 | lifeskim:mentions | umls-concept:C0040690 | lld:lifeskim |
| pubmed-article:16027725 | lifeskim:mentions | umls-concept:C1333282 | lld:lifeskim |
| pubmed-article:16027725 | lifeskim:mentions | umls-concept:C1426328 | lld:lifeskim |
| pubmed-article:16027725 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:16027725 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:16027725 | pubmed:issue | 54 | lld:pubmed |
| pubmed-article:16027725 | pubmed:dateCreated | 2005-12-2 | lld:pubmed |
| pubmed-article:16027725 | pubmed:abstractText | Disruption of components in the transforming growth factor-beta (TGF-beta) signalling cascade is a common occurrence in human cancers. TGF-beta pathway activation is accomplished via serine/threonine kinase receptors and intracellular Smad transcription factors. A key regulatory step involves specific ubiquitination by Smurfs that mediate the proteasomal degradation of Smads and/or receptors. Here, we report a novel interaction between Smads and ubiquitin C-terminal hydrolase UCH37, a deubiquitinating enzyme that could potentially reverse Smurf-mediated ubiquitination. In GST pull down experiments, UCH37 bound weakly to Smad2 and Smad3, and bound very strongly to Smad7 in a region that is distinct from the -PY- motif in Smad7 that interacts with Smurf ubiquitin ligases. Endogenous Smad7 and UCH37 formed a stable complex in U4A/JAK1 cells, and FLAG-Smad7 co-immunoprecipitated with HA-UCH37 in transfected HEK-293 cells. In addition, we show that UCH37 can deubiquitinate and stabilize the type I TGF-beta receptor. Furthermore, overexpression of UCH37 upregulates TGF-beta-dependent transcription, and this effect is reversed in cells subject to RNAi-mediated knockdown of endogenous UCH37. These findings support a new role for deubiquitinating enzymes in the control of the TGF-beta signalling pathway, and provide a novel molecular target for the design of inhibitors with therapeutic potential in cancer. | lld:pubmed |
| pubmed-article:16027725 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16027725 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16027725 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16027725 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16027725 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16027725 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:16027725 | pubmed:issn | 0950-9232 | lld:pubmed |
| pubmed-article:16027725 | pubmed:author | pubmed-author:WicksStephen... | lld:pubmed |
| pubmed-article:16027725 | pubmed:author | pubmed-author:ChantryAndrew... | lld:pubmed |
| pubmed-article:16027725 | pubmed:author | pubmed-author:SongLingL | lld:pubmed |
| pubmed-article:16027725 | pubmed:author | pubmed-author:CohenRobert... | lld:pubmed |
| pubmed-article:16027725 | pubmed:author | pubmed-author:DijkePeter... | lld:pubmed |
| pubmed-article:16027725 | pubmed:author | pubmed-author:HarosKatherin... | lld:pubmed |
| pubmed-article:16027725 | pubmed:author | pubmed-author:MaillardMarjo... | lld:pubmed |
| pubmed-article:16027725 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16027725 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:16027725 | pubmed:volume | 24 | lld:pubmed |
| pubmed-article:16027725 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16027725 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16027725 | pubmed:pagination | 8080-4 | lld:pubmed |
| pubmed-article:16027725 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:16027725 | pubmed:meshHeading | pubmed-meshheading:16027725... | lld:pubmed |
| pubmed-article:16027725 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16027725 | pubmed:articleTitle | The deubiquitinating enzyme UCH37 interacts with Smads and regulates TGF-beta signalling. | lld:pubmed |
| pubmed-article:16027725 | pubmed:affiliation | School of Biological Sciences, University of East Anglia, Earlham Road, Norwich Norfolk NR4 7TJ, UK. | lld:pubmed |
| pubmed-article:16027725 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16027725 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16027725 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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