Autophagy is a process whose core machinery is highly conserved from yeast to higher eukaryotes and mammals. However it is becoming clear that multicellular organisms exhibit increased complexity of autophagic regulation and specialization of the non-core apparatus to perform a number of different roles. Using the yeast interaction network as a scaffold we identified the 14 novel human proteins as putative autophagy-associatd proteins. We confirmed one of these, the F-BAR protein FNBP1L,as being an ATG3 interactor. Using a functional siRNA approach we demonstrated that FNBP1L was essential for autophagy of internalized Salmonella Typhimurium, but dispensable for formation of classical autophagosomes. Our approach illustrates the level of conservation of the autophagy apparatus over large evolutionary distances, but also demonstrates that mammalian cells utilize different autophagy accessory molecules in specific contexts.
|Evidence ID||Analyze ID||Interactor||Interactor Systematic Name||Interactor||Interactor Systematic Name||Type||Assay||Annotation||Action||Modification||Phenotype||Source||Reference||Note|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Gene Ontology Term||Gene Ontology Term ID||Qualifier||Aspect||Method||Evidence||Source||Assigned On||Reference||Annotation Extension|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Phenotype||Experiment Type||Experiment Type Category||Mutant Information||Strain Background||Chemical||Details||Reference|
|Evidence ID||Analyze ID||Regulator||Regulator Systematic Name||Target||Target Systematic Name||Experiment||Conditions||Strain||Source||Reference|