| pubmed-article:9412467 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9412467 | lifeskim:mentions | umls-concept:C0178719 | lld:lifeskim |
| pubmed-article:9412467 | lifeskim:mentions | umls-concept:C0010852 | lld:lifeskim |
| pubmed-article:9412467 | lifeskim:mentions | umls-concept:C0287990 | lld:lifeskim |
| pubmed-article:9412467 | lifeskim:mentions | umls-concept:C1414635 | lld:lifeskim |
| pubmed-article:9412467 | lifeskim:mentions | umls-concept:C1414637 | lld:lifeskim |
| pubmed-article:9412467 | lifeskim:mentions | umls-concept:C0439851 | lld:lifeskim |
| pubmed-article:9412467 | lifeskim:mentions | umls-concept:C1704259 | lld:lifeskim |
| pubmed-article:9412467 | lifeskim:mentions | umls-concept:C1705987 | lld:lifeskim |
| pubmed-article:9412467 | lifeskim:mentions | umls-concept:C0599896 | lld:lifeskim |
| pubmed-article:9412467 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
| pubmed-article:9412467 | lifeskim:mentions | umls-concept:C1552596 | lld:lifeskim |
| pubmed-article:9412467 | lifeskim:mentions | umls-concept:C1947931 | lld:lifeskim |
| pubmed-article:9412467 | lifeskim:mentions | umls-concept:C1709708 | lld:lifeskim |
| pubmed-article:9412467 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:9412467 | pubmed:dateCreated | 1998-2-5 | lld:pubmed |
| pubmed-article:9412467 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9412467 | pubmed:abstractText | Furin catalyzes the proteolytic maturation of many proproteins within the trans-Golgi network (TGN)/endosomal system. Furin's cytosolic domain (cd) directs both the compartmentalization to and transit between its manifold processing compartments (i.e., TGN/biosynthetic pathway, cell surface, and endosomes). Here we report the identification of the first furin cd sorting protein, ABP-280 (nonmuscle filamin), an actin gelation protein. The furin cd was used as bait in a yeast two-hybrid screen to identify ABP-280 as a furin-binding protein. Binding analyses in vitro and coimmunoprecipitation studies in vivo showed that furin and ABP-280 interact directly and that ABP-280 tethers furin molecules to the cell surface. Quantitative analysis of both ABP-280-deficient and genetically replete cells showed that ABP-280 modulates the rate of internalization of furin but not of the transferrin receptor, a cycling receptor. However, although ABP-280 directs the rate of furin internalization, the efficiency of sorting of the endoprotease from the cell surface to early endosomes is independent of expression of ABP-280. By contrast, efficient sorting of furin from early endosomes to the TGN requires expression of ABP-280. In addition, ABP-280 is also required for the correct localization of late endosomes (dextran bead uptake) and lysosomes (LAMP-1 staining), demonstrating a pleiotropic role for this actin binding protein in the organization of cellular compartments and directing protein traffic. Finally, and consistent with the trafficking studies on furin, we showed that ABP-280 modulates the processing of furin substrates in the endocytic but not the biosynthetic pathways. The novel roles of ABP-280 and the cytoskeleton in the sorting of furin in the TGN/ endosomal system and the formation of proprotein processing compartments are discussed. | lld:pubmed |
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