RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/16940348http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16940348http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16940348http://www.w3.org/2000/01/rdf-schema#comment"Autophagy, fundamentally a lysosomal degradation pathway, functions in cells during normal growth and certain pathological conditions, including starvation, to maintain homeostasis. Autophagosomes are formed through a mechanism that is not well understood, despite the identification of many genes required for autophagy. We have studied the mammalian homologue of Atg9p, a multi-spanning transmembrane protein essential in yeast for autophagy, to gain a better understanding of the function of this ubiquitious protein. We show that both the N- and C-termini of mammalian Atg9 (mAtg9) are cytosolic, and predict that mAtg9 spans the membrane six times. We find that mAtg9 is located in the trans-Golgi network and late endosomes and colocalizes with TGN46, the cation-independent mannose-6-phosphate receptor, Rab7 and Rab9. Amino acid starvation or rapamycin treatment, which upregulates autophagy, causes a redistribution of mAtg9 from the TGN to peripheral, endosomal membranes, which are positive for the autophagosomal marker GFP-LC3. siRNA-mediated depletion of the putative mammalian homologue of Atg1p, ULK1, inhibits this starvation-induced redistribution. The redistribution of mAtg9 also requires PI 3-kinase activity, and is reversed after restoration of amino acids. We speculate that starvation-induced autophagy, which requires mAtg9, may rely on an alteration of the steady-state trafficking of mAtg9, in a Atg1-dependent manner."xsd:string
http://purl.uniprot.org/citations/16940348http://purl.org/dc/terms/identifier"doi:10.1242/jcs.03172"xsd:string
http://purl.uniprot.org/citations/16940348http://purl.org/dc/terms/identifier"doi:10.1242/jcs.03172"xsd:string
http://purl.uniprot.org/citations/16940348http://purl.uniprot.org/core/author"Tooze S.A."xsd:string
http://purl.uniprot.org/citations/16940348http://purl.uniprot.org/core/author"Tooze S.A."xsd:string
http://purl.uniprot.org/citations/16940348http://purl.uniprot.org/core/author"Lippincott-Schwartz J."xsd:string
http://purl.uniprot.org/citations/16940348http://purl.uniprot.org/core/author"Lippincott-Schwartz J."xsd:string
http://purl.uniprot.org/citations/16940348http://purl.uniprot.org/core/author"Hailey D.W."xsd:string
http://purl.uniprot.org/citations/16940348http://purl.uniprot.org/core/author"Hailey D.W."xsd:string
http://purl.uniprot.org/citations/16940348http://purl.uniprot.org/core/author"Crawshaw S.G."xsd:string
http://purl.uniprot.org/citations/16940348http://purl.uniprot.org/core/author"Crawshaw S.G."xsd:string
http://purl.uniprot.org/citations/16940348http://purl.uniprot.org/core/author"High S."xsd:string
http://purl.uniprot.org/citations/16940348http://purl.uniprot.org/core/author"High S."xsd:string
http://purl.uniprot.org/citations/16940348http://purl.uniprot.org/core/author"Chan E.Y."xsd:string
http://purl.uniprot.org/citations/16940348http://purl.uniprot.org/core/author"Chan E.Y."xsd:string
http://purl.uniprot.org/citations/16940348http://purl.uniprot.org/core/author"Hu X.W."xsd:string
http://purl.uniprot.org/citations/16940348http://purl.uniprot.org/core/author"Hu X.W."xsd:string
http://purl.uniprot.org/citations/16940348http://purl.uniprot.org/core/author"Kochl R."xsd:string
http://purl.uniprot.org/citations/16940348http://purl.uniprot.org/core/author"Kochl R."xsd:string
http://purl.uniprot.org/citations/16940348http://purl.uniprot.org/core/author"Young A.R."xsd:string
http://purl.uniprot.org/citations/16940348http://purl.uniprot.org/core/author"Young A.R."xsd:string
http://purl.uniprot.org/citations/16940348http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16940348http://purl.uniprot.org/core/date"2006"xsd:gYear