| pubmed-article:18554923 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18554923 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:18554923 | lifeskim:mentions | umls-concept:C0208355 | lld:lifeskim |
| pubmed-article:18554923 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:18554923 | lifeskim:mentions | umls-concept:C1709059 | lld:lifeskim |
| pubmed-article:18554923 | lifeskim:mentions | umls-concept:C0302891 | lld:lifeskim |
| pubmed-article:18554923 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:18554923 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:18554923 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:18554923 | pubmed:dateCreated | 2008-8-4 | lld:pubmed |
| pubmed-article:18554923 | pubmed:abstractText | The granulocyte colony-stimulating factor receptor (G-CSFR) is a critical regulator of granulopoiesis, but the mechanisms controlling its surface expression are poorly understood. Recent studies using transfected cell lines have suggested the activated G-CSFR is routed to the lysosome and not the proteasome. Here, we examined the role of the ubiquitin/proteasome system in regulating G-CSFR surface expression in both ts20 cells that have a temperature-sensitive E1 ubiquitin-activating enzyme and in primary human neutrophils. We show that the G-CSFR is constitutively ubiquitinated, which increases following ligand binding. In the absence of a functional E1 enzyme, ligand-induced internalization of the receptor is inhibited. Pre-treatment of ts20 transfectants with either chloroquine or MG132 inhibited ligand-induced G-CSFR degradation, suggesting a role for both lysosomes and proteasomes in regulating G-CSFR surface expression in this cell line. In neutrophils, inhibition of the proteasome but not the lysosome was found to inhibit internalization/degradation of the activated G-CSFR. Collectively, these data demonstrate the requirement for a functional ubiquitin/proteasome system in G-CSFR internalization and degradation. Our results suggest a prominent role for the proteasome in physiologic modulation of the G-CSFR, and provide further evidence for the importance of the ubiquitin/proteasome system in the initiation of negative signaling by cytokine receptors. | lld:pubmed |
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| pubmed-article:18554923 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18554923 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18554923 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18554923 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18554923 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:18554923 | pubmed:issn | 1096-0023 | lld:pubmed |
| pubmed-article:18554923 | pubmed:author | pubmed-author:AiJingJ | lld:pubmed |
| pubmed-article:18554923 | pubmed:author | pubmed-author:DruhanLawrenc... | lld:pubmed |
| pubmed-article:18554923 | pubmed:author | pubmed-author:AvalosBelinda... | lld:pubmed |
| pubmed-article:18554923 | pubmed:author | pubmed-author:HunterMelissa... | lld:pubmed |
| pubmed-article:18554923 | pubmed:author | pubmed-author:MassulloPamP | lld:pubmed |
| pubmed-article:18554923 | pubmed:author | pubmed-author:Kindwall-Kell... | lld:pubmed |
| pubmed-article:18554923 | pubmed:author | pubmed-author:LovelandMegan... | lld:pubmed |
| pubmed-article:18554923 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18554923 | pubmed:volume | 43 | lld:pubmed |
| pubmed-article:18554923 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18554923 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18554923 | pubmed:pagination | 114-23 | lld:pubmed |
| pubmed-article:18554923 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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