http://purl.uniprot.org/citations/17272273 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/17272273 | http://www.w3.org/2000/01/rdf-schema#comment | "Transforming growth factor-beta (TGF-beta) signaling is facilitated by scaffold proteins such as SARA (Smad anchor for receptor activation). Endofin, a member of the FYVE domain protein family, has been suggested to regulate membrane trafficking. In this study, we report that endofin functions as a scaffold protein to facilitate TGF-beta signaling. Overexpression of endofin FYVE domain-deletion mutants inhibited TGF-beta-induced expression of CAGA-luciferase. Knockdown of endogenous endofin expression by RNA interference specifically led to reduction of the transcriptional responses of TGF-beta, but had no effect on BMP- or Wnt1-induced reporter expression. Furthermore, in endofin small interfering RNA-expressing stable cells, TGF-beta-mediated expression of plasminogen activator inhibitor-1 and p21(Cip1) was significantly reduced, and TGF-beta-promoted apoptosis was also impaired. We further showed that endofin could interact with Smad4 and TGF-beta type I receptors. Reduction of endogenous endofin expression resulted in a decrease of TGF-beta-induced Smad2 phosphorylation and Smad2-Smad4 complex formation. Together, our findings suggest that endofin facilitates TGF-beta signaling as a scaffold protein to promote the R-Smad-Smad4 complex formation by bringing Smad4 to the proximity of the receptor complex."xsd:string |
http://purl.uniprot.org/citations/17272273 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m611704200"xsd:string |
http://purl.uniprot.org/citations/17272273 | http://purl.uniprot.org/core/author | "Ma J."xsd:string |
http://purl.uniprot.org/citations/17272273 | http://purl.uniprot.org/core/author | "Lu Z."xsd:string |
http://purl.uniprot.org/citations/17272273 | http://purl.uniprot.org/core/author | "Wang Z."xsd:string |
http://purl.uniprot.org/citations/17272273 | http://purl.uniprot.org/core/author | "Zhang L."xsd:string |
http://purl.uniprot.org/citations/17272273 | http://purl.uniprot.org/core/author | "Chen Y.G."xsd:string |
http://purl.uniprot.org/citations/17272273 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
http://purl.uniprot.org/citations/17272273 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
http://purl.uniprot.org/citations/17272273 | http://purl.uniprot.org/core/pages | "9688-9695"xsd:string |
http://purl.uniprot.org/citations/17272273 | http://purl.uniprot.org/core/title | "Endofin, a FYVE domain protein, interacts with Smad4 and facilitates transforming growth factor-beta signaling."xsd:string |
http://purl.uniprot.org/citations/17272273 | http://purl.uniprot.org/core/volume | "282"xsd:string |
http://purl.uniprot.org/citations/17272273 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17272273 |
http://purl.uniprot.org/citations/17272273 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/17272273 |
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