Sorting of Fas ligand to secretory lysosomes is regulated by mono-ubiquitylation and phosphorylation
Zuccato E, Blott E, Holt O, Sigismund S, Shaw M, Bossi G, Griffiths G. Sorting of Fas ligand to secretory lysosomes is regulated by mono-ubiquitylation and phosphorylation. Journal Of Cell Science 2006, 120: 191-199. PMID: 17164290, DOI: 10.1242/jcs.03315.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsEndosomesFas Ligand ProteinHeLa CellsHumansJurkat CellsLeukemia, Basophilic, AcuteLymphocyte Specific Protein Tyrosine Kinase p56(lck)LysosomesMolecular Sequence DataPhosphorylationProtein Structure, TertiaryProtein TransportProto-Oncogene ProteinsProto-Oncogene Proteins c-fynRatsSecretory VesiclesSignal Transductionsrc Homology Domainssrc-Family KinasesUbiquitinConceptsSecretory lysosomesMono-ubiquitylationMultivesicular bodiesProline-rich domainLyn tyrosine kinaseExosome-like vesiclesUbiquitin signalingCytoplasmic tailInner vesicleFas ligandPhosphorylationTyrosine kinaseFasLLysosomesControl entryFasL.LysineSortingUbiquitylationUbiquitinFynLynFASKinaseApoptosis
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