| http://purl.uniprot.org/citations/22172677 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22172677 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22172677 | http://www.w3.org/2000/01/rdf-schema#comment | "Lysosomes move bidirectionally on microtubules, and this motility can be stimulated by overexpression of the small GTPase Arl8. By using affinity chromatography, we find that Arl8-GTP binds to the soluble protein SKIP (SifA and kinesin-interacting protein, aka PLEKHM2). SKIP was originally identified as a target of the Salmonella effector protein SifA and found to bind the light chain of kinesin-1 to activate the motor on the bacteria's replicative vacuole. We show that in uninfected cells both Arl8 and SKIP are required for lysosomes to distribute away from the microtubule-organizing center. We identify two kinesin light chain binding motifs in SKIP that are required for lysosomes to accumulate kinesin-1 and redistribute to the cell periphery. Thus, Arl8 binding to SKIP provides a link from lysosomal membranes to plus-end-directed motility. A splice variant of SKIP that lacks a light chain binding motif does not stimulate movement, suggesting fine-tuning by alternative splicing."xsd:string |
| http://purl.uniprot.org/citations/22172677 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.devcel.2011.10.007"xsd:string |
| http://purl.uniprot.org/citations/22172677 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.devcel.2011.10.007"xsd:string |
| http://purl.uniprot.org/citations/22172677 | http://purl.uniprot.org/core/author | "Munro S."xsd:string |
| http://purl.uniprot.org/citations/22172677 | http://purl.uniprot.org/core/author | "Munro S."xsd:string |
| http://purl.uniprot.org/citations/22172677 | http://purl.uniprot.org/core/author | "Rosa-Ferreira C."xsd:string |
| http://purl.uniprot.org/citations/22172677 | http://purl.uniprot.org/core/author | "Rosa-Ferreira C."xsd:string |
| http://purl.uniprot.org/citations/22172677 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/22172677 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/22172677 | http://purl.uniprot.org/core/name | "Dev. Cell"xsd:string |
| http://purl.uniprot.org/citations/22172677 | http://purl.uniprot.org/core/name | "Dev. Cell"xsd:string |
| http://purl.uniprot.org/citations/22172677 | http://purl.uniprot.org/core/pages | "1171-1178"xsd:string |
| http://purl.uniprot.org/citations/22172677 | http://purl.uniprot.org/core/pages | "1171-1178"xsd:string |
| http://purl.uniprot.org/citations/22172677 | http://purl.uniprot.org/core/title | "Arl8 and SKIP act together to link lysosomes to kinesin-1."xsd:string |
| http://purl.uniprot.org/citations/22172677 | http://purl.uniprot.org/core/title | "Arl8 and SKIP act together to link lysosomes to kinesin-1."xsd:string |
| http://purl.uniprot.org/citations/22172677 | http://purl.uniprot.org/core/volume | "21"xsd:string |
| http://purl.uniprot.org/citations/22172677 | http://purl.uniprot.org/core/volume | "21"xsd:string |
| http://purl.uniprot.org/citations/22172677 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/22172677 |
| http://purl.uniprot.org/citations/22172677 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/22172677 |
| http://purl.uniprot.org/citations/22172677 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/22172677 |
| http://purl.uniprot.org/citations/22172677 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/22172677 |
| http://purl.uniprot.org/uniprot/Q9H0B6 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/22172677 |
| http://purl.uniprot.org/uniprot/Q9NVJ2 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/22172677 |