title: Autophagy and cancer metabolism.
abstract: The metabolism of malignant cells is profoundly altered in order to maintain their survival and proliferation in adverse microenvironmental conditions. Autophagy is an intracellular recycling process that maintains basal levels of metabolites and biosynthetic intermediates under starvation or other forms of stress, hence serving as an important mechanism for metabolic adaptation in cancer cells. Although it is widely acknowledged that autophagy sustains metabolism in neoplastic cells under duress, many questions remain with regard to the mutual relationship between autophagy and metabolism in cancer. Importantly, autophagy has often been described as a "double-edged sword" that can either impede or promote cancer initiation and progression. Here, we overview such a dual function of autophagy in tumorigenesis and our current understanding of the coordinated regulation of autophagy and cancer cell metabolism in the control of tumor growth, progression, and resistance to therapy.
authors.affiliation: Department of Pathology, Helen Diller Family Comprehensive Cancer Center and Biomedical Science Graduate Program, University of California, San Francisco, California, USA.
authors.forename: Juliet
authors.initials: J
authors.lastname: Goldsmith
authors.affiliation: Departments of Internal Medicine and Microbiology, Center for Autophagy Research, and Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, Texas, USA.
authors.forename: Beth
authors.initials: B
authors.lastname: Levine
authors.affiliation: Department of Pathology, Helen Diller Family Comprehensive Cancer Center and Biomedical Science Graduate Program, University of California, San Francisco, California, USA. Electronic address: jayanta.debnath@ucsf.edu.
authors.forename: Jayanta
authors.initials: J
authors.lastname: Debnath
mesh_terms: D048868:Adaptor Proteins, Signal Transducing / Q000378:metabolism; D033942:Adaptor Proteins, Vesicular Transport / Q000378:metabolism; D000596:Amino Acids / Q000378:metabolism; D000818:Animals; D051017:Apoptosis Regulatory Proteins / Q000378:metabolism; D001343:Autophagy / Q000502:physiology*; D000071183:Autophagy-Related Proteins; D000071186:Beclin-1; D015687:Cell Hypoxia; D002470:Cell Survival; D058546:Class III Phosphatidylinositol 3-Kinases / Q000378:metabolism; D005947:Glucose / Q000378:metabolism; D005973:Glutamine / Q000378:metabolism; D006019:Glycolysis; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism; D009369:Neoplasms / Q000378:metabolism* / Q000473:pathology*; D017382:Reactive Oxygen Species / Q000378:metabolism; D000071456:Sequestosome-1 Protein; D017154:Stromal Cells / Q000378:metabolism / Q000473:pathology
chemical_list: C539000:ATG14 protein, human; D048868:Adaptor Proteins, Signal Transducing; D033942:Adaptor Proteins, Vesicular Transport; D000596:Amino Acids; D051017:Apoptosis Regulatory Proteins; D000071183:Autophagy-Related Proteins; C491997:BECN1 protein, human; D000071186:Beclin-1; D008565:Membrane Proteins; D017382:Reactive Oxygen Species; C099718:SQSTM1 protein, human; D000071456:Sequestosome-1 Protein; D005973:Glutamine; D058546:Class III Phosphatidylinositol 3-Kinases; D005947:Glucose
keywords: Autophagy; Cancer metabolism; Cancer therapy; Glutaminolysis; Glycolysis; Hypoxia