| pubmed-article:10679008 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10679008 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:10679008 | lifeskim:mentions | umls-concept:C1334090 | lld:lifeskim |
| pubmed-article:10679008 | lifeskim:mentions | umls-concept:C1166848 | lld:lifeskim |
| pubmed-article:10679008 | lifeskim:mentions | umls-concept:C0058836 | lld:lifeskim |
| pubmed-article:10679008 | lifeskim:mentions | umls-concept:C0599896 | lld:lifeskim |
| pubmed-article:10679008 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:10679008 | pubmed:dateCreated | 2000-3-22 | lld:pubmed |
| pubmed-article:10679008 | pubmed:abstractText | It is well established that dynamin is involved in clathrin-dependent endocytosis, but relatively little is known about possible intracellular functions of this GTPase. Using confocal imaging, we found that endogenous dynamin was associated with the plasma membrane, the trans-Golgi network, and a perinuclear cluster of cation-independent mannose 6-phosphate receptor (CI-MPR)-containing structures. By electron microscopy (EM), it was shown that these structures were late endosomes and that the endogenous dynamin was preferentially localized to tubulo-vesicular appendices on these late endosomes. Upon induction of the dominant-negative dynK44A mutant, confocal microscopy demonstrated a redistribution of the CI-MPR in mutant-expressing cells. Quantitative EM analysis of the ratio of CI-MPR to lysosome-associated membrane protein-1 in endosome profiles revealed a higher colocalization of the two markers in dynK44A-expressing cells than in control cells. Western blot analysis showed that dynK44A-expressing cells had an increased cellular procathepsin D content. Finally, EM revealed that in dynK44A-expressing cells, endosomal tubules containing CI-MPR were formed. These results are in contrast to recent reports that dynamin-2 is exclusively associated with endocytic structures at the plasma membrane. They suggest instead that endogenous dynamin also plays an important role in the molecular machinery behind the recycling of the CI-MPR from endosomes to the trans-Golgi network, and we propose that dynamin is required for the final scission of vesicles budding from endosome tubules. | lld:pubmed |
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| pubmed-article:10679008 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10679008 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10679008 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10679008 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10679008 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10679008 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:10679008 | pubmed:issn | 1059-1524 | lld:pubmed |
| pubmed-article:10679008 | pubmed:author | pubmed-author:SandvigKK | lld:pubmed |
| pubmed-article:10679008 | pubmed:author | pubmed-author:van DeursBB | lld:pubmed |
| pubmed-article:10679008 | pubmed:author | pubmed-author:LlorenteAA | lld:pubmed |
| pubmed-article:10679008 | pubmed:author | pubmed-author:CourtoyP JPJ | lld:pubmed |
| pubmed-article:10679008 | pubmed:author | pubmed-author:VilhardtFF | lld:pubmed |
| pubmed-article:10679008 | pubmed:author | pubmed-author:NicozianiPP | lld:pubmed |
| pubmed-article:10679008 | pubmed:author | pubmed-author:HiloutLL | lld:pubmed |
| pubmed-article:10679008 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10679008 | pubmed:volume | 11 | lld:pubmed |
| pubmed-article:10679008 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10679008 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10679008 | pubmed:pagination | 481-95 | lld:pubmed |
