Biological Functions of Autophagy Genes: A Disease Perspective

Cell, Journal Year: 2019, Volume and Issue: 176(1-2), P. 11 - 42

Published: Jan. 1, 2019

Language: Английский

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Autophagy in major human diseases

The EMBO Journal, Journal Year: 2021, Volume and Issue: 40(19)

Published: Aug. 30, 2021

Review30 August 2021Open Access Autophagy in major human diseases Daniel J Klionsky orcid.org/0000-0002-7828-8118 Life Sciences Institute, University of Michigan, Ann Arbor, MI, USA Search for more papers by this author Giulia Petroni Department Radiation Oncology, Weill Cornell Medical College, New York, NY, Ravi K Amaravadi Medicine, Pennsylvania, Philadelphia, PA, Abramson Cancer Center, Eric H Baehrecke Molecular, Cell and Biology, Massachusetts School, Worcester, MA, Andrea Ballabio orcid.org/0000-0003-1381-4604 Telethon Institute Genetics Pozzuoli, Italy Translational Sciences, Section Pediatrics, Federico II University, Naples, Molecular Human Genetics, Baylor College Jan Dan Duncan Neurological Research Texas Children Hospital, Houston, TX, Patricia Boya orcid.org/0000-0003-3045-951X Margarita Salas Center Biological Research, Spanish National Council, Madrid, Spain José Manuel Bravo-San Pedro Faculty Physiology, Complutense Networked Biomedical Neurodegenerative Diseases (CIBERNED), Ken Cadwell Kimmel Biology Medicine at the Skirball York Grossman School Microbiology, Division Gastroenterology Hepatology, Langone Health, Francesco Cecconi orcid.org/0000-0002-5614-4359 Stress Survival Unit, Autophagy, Recycling Disease (CARD), Danish Society Copenhagen, Denmark Pediatric Onco-Hematology Gene Therapy, IRCCS Bambino Gesù Children's Rome, Rome 'Tor Vergata', Augustine M Choi Pulmonary Critical Care Joan Sanford I. York-Presbyterian Mary E Nephrology Hypertension, Charleen T Chu orcid.org/0000-0002-5052-8271 Pathology, Pittsburgh Pittsburgh, Patrice Codogno orcid.org/0000-0002-5492-3180 Institut Necker-Enfants Malades, INSERM U1151-CNRS UMR 8253, Paris, France Université de Maria Isabel Colombo Laboratorio Mecanismos Moleculares Implicados en el Tráfico Vesicular y la Autofagia-Instituto Histología Embriología (IHEM)-Universidad Nacional Cuyo, CONICET- Facultad Ciencias Médicas, Mendoza, Argentina Ana Cuervo orcid.org/0000-0002-0771-700X Developmental Albert Einstein Bronx, Aging Studies, Vojo Deretic Inflammation Metabolism (AIM, Excellence, Mexico Health Albuquerque, NM, Ivan Dikic orcid.org/0000-0001-8156-9511 Biochemistry II, Goethe Frankfurt, Frankfurt am Main, Germany Buchmann Zvulun Elazar Biomolecular The Weizmann Science, Rehovot, Israel Eeva-Liisa Eskelinen Biomedicine, Turku, Finland Gian Fimia orcid.org/0000-0003-4438-3325 Sapienza Epidemiology, Preclinical Advanced Diagnostics, Infectious 'L. Spallanzani' IRCCS, David A Gewirtz orcid.org/0000-0003-0437-4934 Pharmacology Toxicology, Virginia Commonwealth Richmond, VA, Douglas R Green Immunology, St. Jude Memphis, TN, Malene Hansen Burnham Prebys Discovery Program Development, Aging, Regeneration, La Jolla, CA, Marja Jäättelä orcid.org/0000-0001-5950-7111 Death Metabolism, & Disease, Cellular Terje Johansen orcid.org/0000-0003-1451-9578 Group, Tromsø—The Arctic Norway, Tromsø, Norway Gábor Juhász Szeged, Hungary Anatomy, Eötvös Loránd Budapest, Vassiliki Karantza Merck Co., Inc., Kenilworth, NJ, Claudine Kraft orcid.org/0000-0002-3324-4701 ZBMZ, Freiburg, CIBSS - Centre Integrative Signalling Guido Kroemer orcid.org/0000-0002-9334-4405 Recherche des Cordeliers, Equipe Labellisée par Ligue Contre le Cancer, Sorbonne Université, Inserm U1138, Universitaire France, Metabolomics Platforms, Gustave Roussy, Villejuif, Pôle Biologie, Hôpital Européen Georges Pompidou, AP-HP, Suzhou Systems Chinese Academy Suzhou, China Karolinska Women's Stockholm, Sweden Nicholas Ktistakis Programme, Babraham Cambridge, UK Sharad Kumar orcid.org/0000-0001-7126-9814 South Australia, Adelaide, SA, Australia Carlos Lopez-Otin orcid.org/0000-0001-6964-1904 Departamento Bioquímica Biología Medicina, Instituto Universitario Oncología del Principado Asturias (IUOPA), Universidad Oviedo, Centro Investigación Biomédica Red Cáncer (CIBERONC), Kay F Macleod Ben May Gordon W-338, Chicago, IL, Frank Madeo Biosciences, NAWI Graz, Austria BioTechMed-Graz, Field Excellence BioHealth – Jennifer Martinez Immunity, Laboratory, Environmental NIH, Triangle Park, NC, Alicia Meléndez Department, Queens City Flushing, Graduate PhD Programs Noboru Mizushima orcid.org/0000-0002-6258-6444 Tokyo, Japan Christian Münz orcid.org/0000-0001-6419-1940 Viral Immunobiology, Experimental Zurich, Switzerland Josef Penninger Biotechnology Austrian (IMBA), Vienna BioCenter (VBC), Vienna, British Columbia, Vancouver, BC, Canada Rushika Perera orcid.org/0000-0003-2435-2273 California, San Francisco, Helen Diller Family Comprehensive Mauro Piacentini orcid.org/0000-0003-2919-1296 "Tor Vergata", Laboratory Cytology Russian Saint Petersburg, Russia Fulvio Reggiori orcid.org/0000-0003-2652-2686 Cells Systems, Section, Groningen, Netherlands C Rubinsztein Cambridge Dementia Kevin Ryan Beatson Glasgow, Junichi Sadoshima Cardiovascular Rutgers Jersey Newark, Laura Santambrogio Sandra Edward Meyer Caryl Englander Precision Luca Scorrano orcid.org/0000-0002-8515-8928 Istituto Veneto di Medicina Molecolare, Padova, Hans-Uwe Simon Pharmacology, Bern, Clinical Immunology Allergology, Sechenov Moscow, Fundamental Kazan Federal Kazan, Anna Katharina Kennedy Rheumatology, NDORMS, Oxford, Anne Simonsen orcid.org/0000-0003-4711-7057 Basic Oslo, Reprogramming, Oslo Hospital Montebello, Alexandra Stolz orcid.org/0000-0002-3340-439X Nektarios Tavernarakis orcid.org/0000-0002-5253-1466 Biotechnology, Foundation Technology-Hellas, Heraklion, Crete, Greece Sharon Tooze orcid.org/0000-0002-2182-3116 Francis Crick London, Tamotsu Yoshimori orcid.org/0000-0001-9787-3788 Osaka Suita, Intracellular Membrane Dynamics, Frontier Integrated Science Division, Open Transdisciplinary Initiatives (OTRI), Junying Yuan Interdisciplinary on Chemistry, Shanghai Organic Shanghai, Harvard Boston, Zhenyu Yue Neurology, Friedman Brain Icahn Mount Sinai, Qing Zhong orcid.org/0000-0001-6979-955X Key Differentiation Apoptosis Ministry Education, Pathophysiology, Jiao Tong (SJTU-SM), Lorenzo Galluzzi Corresponding Author [email protected] orcid.org/0000-0003-2257-8500 Dermatology, Yale Haven, CT, Pietrocola orcid.org/0000-0002-2930-234X Biosciences Nutrition, Huddinge, mor

Language: Английский

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New insights into the interplay between autophagy, gut microbiota and inflammatory responses in IBD

Autophagy, Journal Year: 2019, Volume and Issue: 16(1), P. 38 - 51

Published: July 9, 2019

One of the most significant challenges inflammatory bowel disease (IBD) research is to understand how alterations in symbiotic relationship between genetic composition host and intestinal microbiota, under impact specific environmental factors, lead chronic inflammation. Genome-wide association studies, followed by functional have identified a role for numerous autophagy genes IBD, especially Crohn disease. Studies using vitro vivo models, addition human clinical studies revealed that pivotal homeostasis maintenance, gut ecology regulation, appropriate immune responses anti-microbial protection. This review describes latest researches on mechanisms which dysfunctional leads disrupted epithelial function, dysbiosis, defect peptide secretion Paneth cells, endoplasmic reticulum stress response aberrant pathogenic bacteria. A better understanding IBD pathogenesis may provide sub-classification phenotypes novel approaches management.Abbreviations: AIEC: adherent-invasive Escherichia coli; AMPK: AMP-activated protein kinase; ATF6: activating transcription factor 6; ATG: related; Atg16l1[ΔIEC] mice: mice with Atg16l1 depletion specifically cells; Atg16l1[HM] hypomorphic expression; BCL2: B cell leukemia/lymphoma 2; BECN1: beclin 1, CALCOCO2: calcium binding coiled-coil domain CASP: caspase; CD: disease; CGAS: cyclic GMP-AMP synthase; CHUK/IKKA: conserved helix-loop-helix ubiquitous CLDN2: claudin DAPK1: death associated kinase 1; DCs: dendritic DSS: dextran sulfate sodium; EIF2A: eukaryotic translation initiation 2A; EIF2AK: 2 alpha ER: reticulum; ERBIN: Erbb2 interacting protein; ERN1/IRE1A: ER nucleus signaling FNBP1L: formin 1-like; FOXP3: forkhead box P3; GPR65: G-protein coupled receptor 65; GSK3B: glycogen synthase 3 beta; IBD: IECs: IFN: interferon; IL: interleukin; IL10R: interleukin 10 receptor; IRGM: immunity related GTPase M; ISC: stem cell; LAMP1: lysosomal-associated membrane LAP: LC3-associated phagocytosis; MAP1LC3B: microtubule-associated 1 light chain LPS: lipopolysaccharide; LRRK2: leucine-rich repeat MAPK: mitogen-activated MHC: major histocompatibility complex; MIF: macrophage migration inhibitory factor; MIR/miRNA: microRNA; MTMR3: myotubularin 3; MTOR: mechanistic target rapamycin MYD88: myeloid differentiation primary gene 88; NLRP3: NLR family, pyrin containing NOD2: nucleotide-binding oligomerization NPC: Niemann-Pick type C; NPC1: NPC intracellular cholesterol transporter OMVs: outer vesicles; OPTN: optineurin; PI3K: phosphoinositide 3-kinase; PRR: pattern-recognition PTPN2: tyrosine phosphatase, non-receptor PTPN22: 22 (lymphoid); PYCARD/ASC: PYD CARD containing; RAB2A: RAB2A, member RAS oncogene family; RELA: v-rel reticuloendotheliosis viral homolog (avian); RIPK2: (TNFRSF)-interacting serine-threonine ROS: reactive oxygen species; SNPs: single nucleotide polymorphisms; SQSTM1: sequestosome TAX1BP1: Tax1 Th: T helper TIRAP/TRIF: toll-interleukin (TIR) domain-containing adaptor TLR: toll-like TMEM173/STING: transmembrane 173; TMEM59: 59; TNF/TNFA: tumor necrosis Treg: regulatory T; TREM1: triggering expressed cells UC: ulcerative colitis; ULK1: unc-51 like WT: wild-type; XBP1: X-box XIAP: X-linked inhibitor apoptosis.

Language: Английский

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Targeting the Endocytic Pathway and Autophagy Process as a Novel Therapeutic Strategy in COVID-19

International Journal of Biological Sciences, Journal Year: 2020, Volume and Issue: 16(10), P. 1724 - 1731

Published: Jan. 1, 2020

Coronaviruses (CoVs) are a group of enveloped, single-stranded positive genomic RNA viruses and some them known to cause severe respiratory diseases in human, including Severe Acute Respiratory Syndrome (SARS), Middle East (MERS) the ongoing coronavirus disease-19 (COVID-19).One key element viral infection is process entry into host cells.In last two decades, there increasing understanding on importance endocytic pathway autophagy replication.As result, endosome lysosome has become important targets for development therapeutic strategies combating caused by CoVs.In this mini-review, we will focus as well several pathogenic CoVs inclusive SARS-CoV, MERS-CoV new CoV named acute syndrome 2 (SARS-CoV-2), discuss agents targeting these processes.Such knowledge provide clues control epidemic SARS-CoV-2 treatment COVID-19.

Language: Английский

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TMTpro reagents: a set of isobaric labeling mass tags enables simultaneous proteome-wide measurements across 16 samples

Nature Methods, Journal Year: 2020, Volume and Issue: 17(4), P. 399 - 404

Published: March 16, 2020

Language: Английский

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Machinery, regulation and pathophysiological implications of autophagosome maturation

Nature Reviews Molecular Cell Biology, Journal Year: 2021, Volume and Issue: 22(11), P. 733 - 750

Published: July 23, 2021

Language: Английский

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Crosstalk Between Mammalian Autophagy and the Ubiquitin-Proteasome System

Frontiers in Cell and Developmental Biology, Journal Year: 2018, Volume and Issue: 6

Published: Oct. 2, 2018

Crosstalk Between Mammalian Autophagy and the Ubiquitin-Proteasome System Nur Mehpare Kocaturk1 Devrim Gozuacik1,2,3* 1Sabanci University, Faculty of Engineering Natural Sciences, Molecular Biology, Genetics Bioengineering Program, Istanbul, 34956, Turkey. 2Sabanci Center Excellence for Functional Surfaces Interfaces Nano Diagnostics (EFSUN), 3Sabanci University Nanotechnology Application (SUNUM), * Correspondence: Gozuacik [email protected] ubiquitin–proteasome system (UPS) are two major intracellular quality control recycling mechanisms that responsible cellular homeostasis in eukaryotes. Ubiquitylation is utilized as a degradation signal by both systems, yet, different play. The UPS short-lived proteins soluble misfolded whereas autophagy eliminates long-lived proteins, insoluble protein aggregates even whole organelles (e.g., mitochondria, peroxisomes) parasites bacteria). Both selective recognize their targets through ubiquitin tags. In addition to an indirect connection between systems ubiquitylated recent data indicate presence connections reciprocal regulation these pathways. this review, we summarize direct interactions crosstalks UPS, implications stress responses homeostasis.

Language: Английский

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Diverse Cellular Roles of Autophagy

Annual Review of Cell and Developmental Biology, Journal Year: 2019, Volume and Issue: 35(1), P. 453 - 475

Published: July 8, 2019

Macroautophagy is an intracellular degradation system that delivers diverse cytoplasmic materials to lysosomes via autophagosomes. Recent advances have enabled identification of several selective autophagy substrates and receptors, greatly expanding our understanding the cellular functions autophagy. In this review, we describe macroautophagy, including its essential contribution metabolic adaptation homeostasis. We also discuss emerging findings on mechanisms various types

Language: Английский

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Complex interplay between autophagy and oxidative stress in the development of pulmonary disease

Redox Biology, Journal Year: 2020, Volume and Issue: 36, P. 101679 - 101679

Published: Aug. 11, 2020

The autophagic pathway involves the encapsulation of substrates in double-membraned vesicles, which are subsequently delivered to lysosome for enzymatic degradation and recycling metabolic precursors. Autophagy is a major cellular defense against oxidative stress, or related conditions that cause accumulation damaged proteins organelles. Selective forms autophagy can maintain organelle populations remove aggregated proteins. Dysregulation redox homeostasis under pathological results excessive generation reactive oxygen species (ROS), leading stress associated damage components. Accumulating evidence indicates necessary homeostasis. ROS activates autophagy, facilitates adaptation diminishes by degrading intracellular macromolecules dysfunctional responses triggered include altered regulation signaling pathways culminate autophagy. Current research suggests central role as mammalian response its interrelationship other systems. Altered phenotypes have been observed lung diseases such chronic obstructive disease, acute injury, cystic fibrosis, idiopathic pulmonary arterial hypertension, asthma. Understanding mechanisms regulate will provide novel therapeutic targets diseases. This review highlights our current understanding on interplay between development disease.

Language: Английский

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The autophagic membrane tether ATG2A transfers lipids between membranes

eLife, Journal Year: 2019, Volume and Issue: 8

Published: July 4, 2019

An enigmatic step in de novo formation of the autophagosome membrane compartment is expansion precursor phagophore, which requires acquisition lipids to serve as building blocks. Autophagy-related 2 (ATG2), rod-shaped protein that tethers phosphatidylinositol 3-phosphate (PI3P)-enriched phagophores endoplasmic reticulum (ER), suggested be essential for phagophore expansion, but underlying mechanism remains unclear. Here, we demonstrate human ATG2A a lipid transfer protein. can extract from vesicles and unload them other vesicles. Lipid by more efficient between tethered than untethered The PI3P effectors WIPI4 WIPI1 associate stably PI3P-containing vesicles, thereby facilitating ATG2A-mediated tethering PI3P-free Based on these results, propose ATG2-mediated ER enables expansion.

Language: Английский

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