| pubmed-article:20580638 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20580638 | lifeskim:mentions | umls-concept:C0034802 | lld:lifeskim |
| pubmed-article:20580638 | lifeskim:mentions | umls-concept:C0376525 | lld:lifeskim |
| pubmed-article:20580638 | lifeskim:mentions | umls-concept:C0014139 | lld:lifeskim |
| pubmed-article:20580638 | lifeskim:mentions | umls-concept:C0071253 | lld:lifeskim |
| pubmed-article:20580638 | lifeskim:mentions | umls-concept:C0013126 | lld:lifeskim |
| pubmed-article:20580638 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:20580638 | lifeskim:mentions | umls-concept:C0598629 | lld:lifeskim |
| pubmed-article:20580638 | lifeskim:mentions | umls-concept:C1522138 | lld:lifeskim |
| pubmed-article:20580638 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
| pubmed-article:20580638 | pubmed:issue | 14 | lld:pubmed |
| pubmed-article:20580638 | pubmed:dateCreated | 2010-7-12 | lld:pubmed |
| pubmed-article:20580638 | pubmed:abstractText | Like many other receptor tyrosine kinases (RTKs), platelet-derived growth factor (PDGF) receptor beta (PDGFR-beta) is internalized and degraded in lysosomes in response to PDGF stimulation, which regulates many aspects of cell signalling. However, little is known about the regulation of PDGFR-beta endocytosis. Given that ligand binding is essential for the rapid internalization of RTKs, the events induced by the ligand binding likely contribute to the regulation of ligand-induced RTK internalization. These events include receptor dimerization, activation of intrinsic tyrosine kinase activity and autophosphorylation. In this communication, we examined the role of PDGFR-beta kinase activity, PDGFR-beta dimerization and PDGFR-beta C-terminal motifs in PDGF-induced PDGFR-beta internalization. We showed that inhibition of PDGFR-beta kinase activity by chemical inhibitor or mutation did not block PDGF-induced PDGFR-beta endocytosis, suggesting that the kinase activity is not essential. We further showed that dimerization of PDGFR-beta is essential and sufficient to drive PDGFR-beta internalization independent of PDGFR-beta kinase activation. Moreover, we showed that the previously reported 14 amino acid sequence 952-965 is required for PDGF-induced PDGFR-beta internalization. Most importantly, we showed that this PDGFR-beta internalization motif is exchangeable with the EGFR internalization motif (1005-1017) in mediating ligand-induced internalization of both PDGFR-beta and EGFR. This indicates a common mechanism for the internalization of both PDGFR-beta and EGFR. | lld:pubmed |
| pubmed-article:20580638 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20580638 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20580638 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20580638 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20580638 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20580638 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20580638 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20580638 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20580638 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20580638 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:20580638 | pubmed:issn | 1090-2422 | lld:pubmed |
| pubmed-article:20580638 | pubmed:author | pubmed-author:ChenXinmeiX | lld:pubmed |
| pubmed-article:20580638 | pubmed:author | pubmed-author:WangZhixiangZ | lld:pubmed |
| pubmed-article:20580638 | pubmed:author | pubmed-author:PaharaJustinJ | lld:pubmed |
| pubmed-article:20580638 | pubmed:author | pubmed-author:ShiHuaipingH | lld:pubmed |
| pubmed-article:20580638 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20580638 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:20580638 | pubmed:volume | 316 | lld:pubmed |
| pubmed-article:20580638 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20580638 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20580638 | pubmed:pagination | 2237-50 | lld:pubmed |
| pubmed-article:20580638 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:20580638 | pubmed:meshHeading | pubmed-meshheading:20580638... | lld:pubmed |
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| pubmed-article:20580638 | pubmed:meshHeading | pubmed-meshheading:20580638... | lld:pubmed |
| pubmed-article:20580638 | pubmed:meshHeading | pubmed-meshheading:20580638... | lld:pubmed |
| pubmed-article:20580638 | pubmed:meshHeading | pubmed-meshheading:20580638... | lld:pubmed |
| pubmed-article:20580638 | pubmed:meshHeading | pubmed-meshheading:20580638... | lld:pubmed |
| pubmed-article:20580638 | pubmed:meshHeading | pubmed-meshheading:20580638... | lld:pubmed |
| pubmed-article:20580638 | pubmed:meshHeading | pubmed-meshheading:20580638... | lld:pubmed |
| pubmed-article:20580638 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20580638 | pubmed:articleTitle | Dimerization drives PDGF receptor endocytosis through a C-terminal hydrophobic motif shared by EGF receptor. | lld:pubmed |
| pubmed-article:20580638 | pubmed:affiliation | Department of Cell Biology and Signal Transduction Research Group, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, Alberta, Canada T6G 2H7. | lld:pubmed |
| pubmed-article:20580638 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20580638 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:18596 | entrezgene:pubmed | pubmed-article:20580638 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:20580638 | lld:entrezgene |
