title: Autophagy, lipophagy and lysosomal lipid storage disorders.
abstract: Autophagy is a catabolic process with an essential function in the maintenance of cellular and tissue homeostasis. It is primarily recognised for its role in the degradation of dysfunctional proteins and unwanted organelles, however in recent years the range of autophagy substrates has also been extended to lipids. Degradation of lipids via autophagy is termed lipophagy. The ability of autophagy to contribute to the maintenance of lipo-homeostasis becomes particularly relevant in the context of genetic lysosomal storage disorders where perturbations of autophagic flux have been suggested to contribute to the disease aetiology. Here we review recent discoveries of the molecular mechanisms mediating lipid turnover by the autophagy pathways. We further focus on the relevance of autophagy, and specifically lipophagy, to the disease mechanisms. Moreover, autophagy is also discussed as a potential therapeutic target in several key lysosomal storage disorders.
authors.affiliation: Institute of Biomedical Research, Institute of Cancer and Genomic Sciences, College of Medical and Dental Sciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom.
authors.forename: Carl
authors.initials: C
authors.lastname: Ward
authors.affiliation: Department of Medicine, Department of Molecular Pharmacology, Institute for Aging Studies, Diabetes Research Center, Albert Einstein College of Medicine, Bronx, NY 10461, USA; Institute for Cell and Molecular Biosciences, Newcastle University Institute for Ageing, Campus for Ageing and Vitality, Newcastle University, Newcastle upon Tyne NE4 5PL, United Kingdom.
authors.forename: Nuria
authors.initials: N
authors.lastname: Martinez-Lopez
authors.affiliation: Institute for Cell and Molecular Biosciences, Newcastle University Institute for Ageing, Campus for Ageing and Vitality, Newcastle University, Newcastle upon Tyne NE4 5PL, United Kingdom.
authors.forename: Elsje G
authors.initials: EG
authors.lastname: Otten
authors.affiliation: Institute for Cell and Molecular Biosciences, Newcastle University Institute for Ageing, Campus for Ageing and Vitality, Newcastle University, Newcastle upon Tyne NE4 5PL, United Kingdom.
authors.forename: Bernadette
authors.initials: B
authors.lastname: Carroll
authors.affiliation: Whitehead Institute for Biomedical Research, Massachusetts Institute of Technology, Cambridge, MA 02142, USA.
authors.forename: Dorothea
authors.initials: D
authors.lastname: Maetzel
authors.affiliation: Department of Medicine, Department of Molecular Pharmacology, Institute for Aging Studies, Diabetes Research Center, Albert Einstein College of Medicine, Bronx, NY 10461, USA; Institute for Cell and Molecular Biosciences, Newcastle University Institute for Ageing, Campus for Ageing and Vitality, Newcastle University, Newcastle upon Tyne NE4 5PL, United Kingdom.
authors.forename: Rajat
authors.initials: R
authors.lastname: Singh
authors.affiliation: Institute of Biomedical Research, Institute of Cancer and Genomic Sciences, College of Medical and Dental Sciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom.
authors.forename: Sovan
authors.initials: S
authors.lastname: Sarkar
authors.affiliation: Institute for Cell and Molecular Biosciences, Newcastle University Institute for Ageing, Campus for Ageing and Vitality, Newcastle University, Newcastle upon Tyne NE4 5PL, United Kingdom.
authors.forename: Viktor I
authors.initials: VI
authors.lastname: Korolchuk
mesh_terms: D000818:Animals; D001343:Autophagy / Q000235:genetics; D005234:Fatty Liver / Q000235:genetics / Q000378:metabolism / Q000473:pathology; D006801:Humans; D050356:Lipid Metabolism / Q000235:genetics; D008052:Lipid Metabolism, Inborn Errors / Q000235:genetics / Q000378:metabolism* / Q000473:pathology; D016464:Lysosomal Storage Diseases / Q000235:genetics / Q000378:metabolism* / Q000473:pathology; D008247:Lysosomes / Q000378:metabolism* / Q000473:pathology; D000076222:Mechanistic Target of Rapamycin Complex 1; D046912:Multiprotein Complexes / Q000378:metabolism; D015398:Signal Transduction; D058570:TOR Serine-Threonine Kinases / Q000378:metabolism
chemical_list: D046912:Multiprotein Complexes; C546842:MTOR protein, human; D000076222:Mechanistic Target of Rapamycin Complex 1; D058570:TOR Serine-Threonine Kinases
keywords: Autophagy; Lipid metabolism; Lipid storage disorders