| pubmed-article:20026655 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20026655 | lifeskim:mentions | umls-concept:C0001271 | lld:lifeskim |
| pubmed-article:20026655 | lifeskim:mentions | umls-concept:C0887838 | lld:lifeskim |
| pubmed-article:20026655 | lifeskim:mentions | umls-concept:C1423702 | lld:lifeskim |
| pubmed-article:20026655 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:20026655 | lifeskim:mentions | umls-concept:C1947906 | lld:lifeskim |
| pubmed-article:20026655 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:20026655 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:20026655 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:20026655 | lifeskim:mentions | umls-concept:C0056080 | lld:lifeskim |
| pubmed-article:20026655 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:20026655 | pubmed:dateCreated | 2009-12-29 | lld:pubmed |
| pubmed-article:20026655 | pubmed:abstractText | Knockdown of the actin-severing protein actin-depolymerizing factor (ADF)/cofilin inhibited export of an exogenously expressed soluble secretory protein from Golgi membranes in Drosophila melanogaster and mammalian tissue culture cells. A stable isotope labeling by amino acids in cell culture mass spectrometry-based protein profiling revealed that a large number of endogenous secretory proteins in mammalian cells were not secreted upon ADF/cofilin knockdown. Although many secretory proteins were retained, a Golgi-resident protein and a lysosomal hydrolase were aberrantly secreted upon ADF/cofilin knockdown. Overall, our findings indicate that inactivation of ADF/cofilin perturbed the sorting of a subset of both soluble and integral membrane proteins at the trans-Golgi network (TGN). We suggest that ADF/cofilin-dependent actin trimming generates a sorting domain at the TGN, which filters secretory cargo for export, and that uncontrolled growth of this domain causes missorting of proteins. This type of actin-dependent compartmentalization and filtering of secretory cargo at the TGN by ADF/cofilin could explain sorting of proteins that are destined to the cell surface. | lld:pubmed |
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| pubmed-article:20026655 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20026655 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20026655 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20026655 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:20026655 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20026655 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:20026655 | pubmed:issn | 1540-8140 | lld:pubmed |
| pubmed-article:20026655 | pubmed:author | pubmed-author:MalhotraVivek... | lld:pubmed |
| pubmed-article:20026655 | pubmed:author | pubmed-author:DuranJuan MJM | lld:pubmed |
| pubmed-article:20026655 | pubmed:author | pubmed-author:MolinaHenrikH | lld:pubmed |
| pubmed-article:20026655 | pubmed:author | pubmed-author:PolishchukRom... | lld:pubmed |
| pubmed-article:20026655 | pubmed:author | pubmed-author:AlleaumeAnne-... | lld:pubmed |
| pubmed-article:20026655 | pubmed:author | pubmed-author:von... | lld:pubmed |
| pubmed-article:20026655 | pubmed:author | pubmed-author:ForlanelliEle... | lld:pubmed |
| pubmed-article:20026655 | pubmed:author | pubmed-author:EgorovMikhail... | lld:pubmed |
| pubmed-article:20026655 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20026655 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:20026655 | pubmed:volume | 187 | lld:pubmed |
| pubmed-article:20026655 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20026655 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20026655 | pubmed:pagination | 1055-69 | lld:pubmed |
| pubmed-article:20026655 | pubmed:dateRevised | 2010-9-28 | lld:pubmed |
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