title: Trafficking and signaling in mammalian autophagy.
abstract: Macroautophagy, here called autophagy, is literally a "self-eating" catabolic process, which is evolutionarily conserved. Autophagy is initiated by cellular stress pathways, resulting in the sequestration or engulfment of cytosolic proteins, membranes, and organelles in a double membrane structure that fuses with endosomes and lysosomes, thus delivering the sequestered material for degradation. Autophagy is implicated in a number of human diseases, many of which can either be characterized by an imbalance in protein, organelle, or cellular homeostasis, ultimately resulting in an alteration of the autophagic response. Here, we will review the recent progress made in understanding the induction of autophagy, with emphasis on the contributions from our laboratory.
authors.affiliation: Secretory Pathways Laboratory, London Research Institute, Cancer Research UK, London, UK. Sharon.tooze@cancer.org.uk
authors.forename: Sharon A
authors.initials: SA
authors.lastname: Tooze
authors.forename: Harold B J
authors.initials: HB
authors.lastname: Jefferies
authors.forename: Eyal
authors.initials: E
authors.lastname: Kalie
authors.forename: Andrea
authors.initials: A
authors.lastname: Longatti
authors.forename: Fiona E
authors.initials: FE
authors.lastname: McAlpine
authors.forename: Nicole C
authors.initials: NC
authors.lastname: McKnight
authors.forename: Andrea
authors.initials: A
authors.lastname: Orsi
authors.forename: Hannah E J
authors.initials: HE
authors.lastname: Polson
authors.forename: Minoo
authors.initials: M
authors.lastname: Razi
authors.forename: Deborah J
authors.initials: DJ
authors.lastname: Robinson
authors.forename: Jemma L
authors.initials: JL
authors.lastname: Webber
mesh_terms: D048868:Adaptor Proteins, Signal Transducing / Q000502:physiology; D001343:Autophagy / Q000502:physiology*; D000071189:Autophagy-Related Protein-1 Homolog; D000071183:Autophagy-Related Proteins; D002352:Carrier Proteins / Q000378:metabolism; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins / Q000502:physiology; D000076222:Mechanistic Target of Rapamycin Complex 1; D008565:Membrane Proteins / Q000502:physiology; D008954:Models, Biological; D046912:Multiprotein Complexes; D010588:Phagosomes / Q000502:physiology; D019869:Phosphatidylinositol 3-Kinases / Q000502:physiology; D018129:Phosphatidylinositol Phosphates / Q000378:metabolism; D017346:Protein Serine-Threonine Kinases / Q000502:physiology; D011506:Proteins; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000502:physiology; D058570:TOR Serine-Threonine Kinases; D014157:Transcription Factors / Q000502:physiology
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D000071189:Autophagy-Related Protein-1 Homolog; D000071183:Autophagy-Related Proteins; D002352:Carrier Proteins; D047908:Intracellular Signaling Peptides and Proteins; D000076222:Mechanistic Target of Rapamycin Complex 1; D008565:Membrane Proteins; D046912:Multiprotein Complexes; D019869:Phosphatidylinositol 3-Kinases; D018129:Phosphatidylinositol Phosphates; D017346:Protein Serine-Threonine Kinases; D011506:Proteins; D029701:Saccharomyces cerevisiae Proteins; D058570:TOR Serine-Threonine Kinases; D014157:Transcription Factors; C413216:ATG13 protein, S cerevisiae; C441008:ATG18 protein, S cerevisiae; C484754:ULK1 protein, human