{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,8]],"date-time":"2026-04-08T02:19:49Z","timestamp":1775614789853,"version":"3.50.1"},"update-to":[{"DOI":"10.1371\/journal.pbio.3002290","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2023,12,4]],"date-time":"2023-12-04T00:00:00Z","timestamp":1701648000000}}],"reference-count":69,"publisher":"Public Library of Science (PLoS)","issue":"11","license":[{"start":{"date-parts":[[2023,11,20]],"date-time":"2023-11-20T00:00:00Z","timestamp":1700438400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100010663","name":"H2020 European Research Council","doi-asserted-by":"publisher","award":["101001521 - LOFlu"],"award-info":[{"award-number":["101001521 - LOFlu"]}],"id":[{"id":"10.13039\/100010663","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001871","name":"Funda\u00e7\u00e3o para a Ci\u00eancia e a Tecnologia","doi-asserted-by":"publisher","award":["2022.02716.PTDC"],"award-info":[{"award-number":["2022.02716.PTDC"]}],"id":[{"id":"10.13039\/501100001871","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Lisboa 2020\/FEDER\/FCT","award":["PPBI-POCI-01-0145-FEDER-022122"],"award-info":[{"award-number":["PPBI-POCI-01-0145-FEDER-022122"]}]},{"name":"Electron Microscopy Facility and Flow Cytometry Facility"},{"DOI":"10.13039\/501100001871","name":"Funda\u00e7\u00e3o para a Ci\u00eancia e a Tecnologia","doi-asserted-by":"publisher","award":["PD\/BD\/128436\/2017"],"award-info":[{"award-number":["PD\/BD\/128436\/2017"]}],"id":[{"id":"10.13039\/501100001871","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001871","name":"Funda\u00e7\u00e3o para a Ci\u00eancia e a Tecnologia","doi-asserted-by":"publisher","award":["PD\/BD\/148391\/2019"],"award-info":[{"award-number":["PD\/BD\/148391\/2019"]}],"id":[{"id":"10.13039\/501100001871","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001871","name":"Funda\u00e7\u00e3o para a Ci\u00eancia e a Tecnologia","doi-asserted-by":"publisher","award":["UI\/BD\/152254\/2021"],"award-info":[{"award-number":["UI\/BD\/152254\/2021"]}],"id":[{"id":"10.13039\/501100001871","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001871","name":"Funda\u00e7\u00e3o para a Ci\u00eancia e a Tecnologia","doi-asserted-by":"publisher","award":["D.L. 57"],"award-info":[{"award-number":["D.L. 57"]}],"id":[{"id":"10.13039\/501100001871","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.plosbiology.org"],"crossmark-restriction":false},"short-container-title":["PLoS Biol"],"abstract":"<jats:p>It is now established that many viruses that threaten public health establish condensates via phase transitions to complete their lifecycles, and knowledge on such processes may offer new strategies for antiviral therapy. In the case of influenza A virus (IAV), liquid condensates known as viral inclusions, concentrate the 8 distinct viral ribonucleoproteins (vRNPs) that form IAV genome and are viewed as sites dedicated to the assembly of the 8-partite genomic complex. Despite not being delimited by host membranes, IAV liquid inclusions accumulate host membranes inside as a result of vRNP binding to the recycling endocytic marker Rab11a, a driver of the biogenesis of these structures. We lack molecular understanding on how Rab11a-recycling endosomes condensate specifically near the endoplasmic reticulum (ER) exit sites upon IAV infection. We show here that liquid viral inclusions interact with the ER to fuse, divide, and slide. We uncover that, contrary to previous indications, the reported reduction in recycling endocytic activity is a regulated process rather than a competition for cellular resources involving a novel role for the host factor ATG9A. In infection, ATG9A mediates the removal of Rab11a-recycling endosomes carrying vRNPs from microtubules. We observe that the recycling endocytic usage of microtubules is rescued when ATG9A is depleted, which prevents condensation of Rab11a endosomes near the ER. The failure to produce viral inclusions accumulates vRNPs in the cytosol and reduces genome assembly and the release of infectious virions. We propose that the ER supports the dynamics of liquid IAV inclusions, with ATG9A facilitating their formation. This work advances our understanding on how epidemic and pandemic influenza genomes are formed. It also reveals the plasticity of recycling endosomes to undergo condensation in response to infection, disclosing new roles for ATG9A beyond its classical involvement in autophagy.<\/jats:p>","DOI":"10.1371\/journal.pbio.3002290","type":"journal-article","created":{"date-parts":[[2023,11,20]],"date-time":"2023-11-20T18:42:41Z","timestamp":1700505761000},"page":"e3002290","update-policy":"https:\/\/doi.org\/10.1371\/journal.pbio.corrections_policy","source":"Crossref","is-referenced-by-count":19,"title":["ATG9A regulates the dissociation of recycling endosomes from microtubules to form liquid influenza A virus inclusions"],"prefix":"10.1371","volume":"21","author":[{"given":"S\u00edlvia","family":"Vale-Costa","sequence":"first","affiliation":[]},{"given":"Temitope Akhigbe","family":"Etibor","sequence":"additional","affiliation":[]},{"given":"Daniela","family":"Br\u00e1s","sequence":"additional","affiliation":[]},{"given":"Ana Laura","family":"Sousa","sequence":"additional","affiliation":[]},{"given":"Mariana","family":"Ferreira","sequence":"additional","affiliation":[]},{"given":"Gabriel G.","family":"Martins","sequence":"additional","affiliation":[]},{"given":"Victor Hugo","family":"Mello","sequence":"additional","affiliation":[]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4129-6659","authenticated-orcid":true,"given":"Maria Jo\u00e3o","family":"Amorim","sequence":"additional","affiliation":[]}],"member":"340","published-online":{"date-parts":[[2023,11,20]]},"reference":[{"key":"pbio.3002290.ref001","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1016\/S0140-6736(22)00982-5","article-title":"Influenza","volume":"400","author":"TM Uyeki","year":"2022","journal-title":"Lancet"},{"key":"pbio.3002290.ref002","article-title":"Influenza A Virus Cell Entry, Replication, Virion Assembly and Movement","volume":"9","author":"D Dou","year":"2018","journal-title":"Front Immunol"},{"key":"pbio.3002290.ref003","doi-asserted-by":"crossref","first-page":"2424","DOI":"10.3390\/v5102424","article-title":"Transport of the Influenza Virus Genome from Nucleus to Nucleus","volume":"5","author":"EC Hutchinson","year":"2013","journal-title":"Viruses"},{"key":"pbio.3002290.ref004","doi-asserted-by":"crossref","first-page":"1629","DOI":"10.1038\/s41467-019-09549-4","article-title":"Influenza A virus ribonucleoproteins form liquid organelles at endoplasmic reticulum exit sites","volume":"10","author":"M Alenquer","year":"2019","journal-title":"Nat Commun"},{"key":"pbio.3002290.ref005","doi-asserted-by":"crossref","first-page":"e85182","DOI":"10.7554\/eLife.85182","article-title":"Defining basic rules for hardening influenza A virus liquid condensates","volume":"12","author":"TA Etibor","year":"2023","journal-title":"Elife"},{"key":"pbio.3002290.ref006","doi-asserted-by":"crossref","first-page":"1697","DOI":"10.1242\/jcs.188409","article-title":"Influenza A virus ribonucleoproteins modulate host recycling by competing with Rab11 effectors","volume":"129","author":"S Vale-Costa","year":"2016","journal-title":"J Cell Sci"},{"key":"pbio.3002290.ref007","doi-asserted-by":"crossref","first-page":"4143","DOI":"10.1128\/JVI.02606-10","article-title":"A Rab11- and Microtubule-Dependent Mechanism for Cytoplasmic Transport of Influenza A Virus Viral RNA","volume":"85","author":"MJ Amorim","year":"2011","journal-title":"J Virol"},{"key":"pbio.3002290.ref008","doi-asserted-by":"crossref","first-page":"6117","DOI":"10.1128\/JVI.00378-11","article-title":"RAB11A Is Essential for Transport of the Influenza Virus Genome to the Plasma Membrane","author":"AJ Eisfeld","year":"2011","journal-title":"J Virol"},{"key":"pbio.3002290.ref009","doi-asserted-by":"crossref","first-page":"e21123","DOI":"10.1371\/journal.pone.0021123","article-title":"Apical transport of influenza A virus ribonucleoprotein requires Rab11-positive recycling endosome","volume":"6","author":"F Momose","year":"2011","journal-title":"PLoS ONE"},{"key":"pbio.3002290.ref010","doi-asserted-by":"crossref","first-page":"5848","DOI":"10.1128\/JVI.00307-10","article-title":"The Rab11 pathway is required for influenza A virus budding and filament formation","volume":"84","author":"EA Bruce","year":"2010","journal-title":"J Virol"},{"key":"pbio.3002290.ref011","doi-asserted-by":"crossref","first-page":"e1009517","DOI":"10.1371\/journal.ppat.1009517","article-title":"Host factor Rab11a is critical for efficient assembly of influenza A virus genomic segments","volume":"17","author":"J Han","year":"2021","journal-title":"PLoS Pathog"},{"key":"pbio.3002290.ref012","doi-asserted-by":"crossref","first-page":"6074","DOI":"10.3390\/ijms21176074","article-title":"The Endosomal Recycling Pathway\u2014At the Crossroads of the Cell","volume":"21","author":"MJ O\u2019Sullivan","year":"2020","journal-title":"Int J Mol Sci"},{"key":"pbio.3002290.ref013","doi-asserted-by":"crossref","first-page":"1433","DOI":"10.1128\/JVI.05820-11","article-title":"Replication-Competent Influenza A Virus That Encodes a Split-Green Fluorescent Protein-Tagged PB2 Polymerase Subunit Allows Live-Cell Imaging of the Virus Life Cycle","author":"SV Avilov","year":"2012","journal-title":"J Virol"},{"key":"pbio.3002290.ref014","doi-asserted-by":"crossref","first-page":"e1003358","DOI":"10.1371\/journal.ppat.1003358","article-title":"Colocalization of Different Influenza Viral RNA Segments in the Cytoplasm before Viral Budding as Shown by Single-molecule Sensitivity FISH Analysis","author":"Y-Y Chou","year":"2013","journal-title":"PLoS Pathog"},{"key":"pbio.3002290.ref015","doi-asserted-by":"crossref","first-page":"e1003971","DOI":"10.1371\/journal.ppat.1003971","article-title":"Influenza a virus assembly intermediates fuse in the cytoplasm","volume":"10","author":"SS Lakdawala","year":"2014","journal-title":"PLoS Pathog"},{"key":"pbio.3002290.ref016","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1038\/s41467-019-13838-3","article-title":"Quantitative live cell imaging reveals influenza virus manipulation of Rab11A transport through reduced dynein association","volume":"11","author":"AR Bhagwat","year":"2020","journal-title":"Nat Commun"},{"key":"pbio.3002290.ref017","doi-asserted-by":"crossref","first-page":"e1009321","DOI":"10.1371\/journal.ppat.1009321","article-title":"Rab11a mediates cell-cell spread and reassortment of influenza A virus genomes via tunneling nanotubes","volume":"17","author":"K Ganti","year":"2021","journal-title":"PLoS Pathog"},{"key":"pbio.3002290.ref018","doi-asserted-by":"crossref","first-page":"e0197921","DOI":"10.1128\/jvi.01979-21","article-title":"The C-Terminal Domains of the PB2 Subunit of the Influenza A Virus RNA Polymerase Directly Interact with Cellular GTPase Rab11a","volume":"96","author":"H Veler","year":"2022","journal-title":"J Virol"},{"key":"pbio.3002290.ref019","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1016\/j.devcel.2020.06.033","article-title":"Phase Separation in Membrane Biology: The Interplay between Membrane-Bound Organelles and Membraneless Condensates","volume":"55","author":"YG Zhao","year":"2020","journal-title":"Dev Cell"},{"key":"pbio.3002290.ref020","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1016\/j.molcel.2019.09.016","article-title":"The Control Centers of Biomolecular Phase Separation: How Membrane Surfaces, PTMs, and Active Processes Regulate Condensation","volume":"76","author":"WT Snead","year":"2019","journal-title":"Mol Cell"},{"key":"pbio.3002290.ref021","doi-asserted-by":"crossref","first-page":"eaay7108","DOI":"10.1126\/science.aay7108","article-title":"Endoplasmic reticulum contact sites regulate the dynamics of membraneless organelles","volume":"367","author":"JE Lee","year":"2020","journal-title":"Science"},{"key":"pbio.3002290.ref022","article-title":"Calcium transients on the ER surface trigger liquid-liquid phase separation of FIP200 to specify autophagosome initiation sites","author":"Q Zheng","year":"2022","journal-title":"Cell"},{"key":"pbio.3002290.ref023","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1038\/s41556-022-00882-3","article-title":"Membrane surfaces regulate assembly of ribonucleoprotein condensates","volume":"24","author":"WT Snead","year":"2022","journal-title":"Nat Cell Biol"},{"key":"pbio.3002290.ref024","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1038\/nrmicro.2016.60","article-title":"Opportunistic intruders: how viruses orchestrate ER functions to infect cells","volume":"14","author":"MS Ravindran","year":"2016","journal-title":"Nat Rev Microbiol"},{"key":"pbio.3002290.ref025","doi-asserted-by":"crossref","first-page":"604","DOI":"10.1126\/science.aat5671","article-title":"A liquid phase of synapsin and lipid vesicles","volume":"361","author":"D Milovanovic","year":"2018","journal-title":"Science"},{"key":"pbio.3002290.ref026","doi-asserted-by":"crossref","first-page":"1185","DOI":"10.1038\/s41594-020-00518-w","article-title":"Atg9 is a lipid scramblase that mediates autophagosomal membrane expansion","volume":"27","author":"K Matoba","year":"2020","journal-title":"Nat Struct Mol Biol"},{"key":"pbio.3002290.ref027","doi-asserted-by":"crossref","first-page":"846","DOI":"10.1038\/s41556-021-00706-w","article-title":"ATG9A protects the plasma membrane from programmed and incidental permeabilization","volume":"23","author":"A Claude-Taupin","year":"2021","journal-title":"Nat Cell Biol"},{"key":"pbio.3002290.ref028","doi-asserted-by":"crossref","first-page":"6750","DOI":"10.1038\/s41467-021-26999-x","article-title":"The autophagy protein ATG9A enables lipid mobilization from lipid droplets","volume":"12","author":"E Mailler","year":"2021","journal-title":"Nat Commun"},{"key":"pbio.3002290.ref029","doi-asserted-by":"crossref","first-page":"20842","DOI":"10.1073\/pnas.0911267106","article-title":"Atg9a controls dsDNA-driven dynamic translocation of STING and the innate immune response","volume":"106","author":"T Saitoh","year":"2009","journal-title":"Proc Natl Acad Sci U S A"},{"key":"pbio.3002290.ref030","doi-asserted-by":"crossref","first-page":"1396","DOI":"10.1038\/s41467-017-01557-6","article-title":"Influenza virus genome reaches the plasma membrane via a modified endoplasmic reticulum and Rab11-dependent vesicles","volume":"8","author":"IF de Castro Martin","year":"2017","journal-title":"Nat Commun"},{"key":"pbio.3002290.ref031","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1006\/excr.2000.4947","article-title":"Rab11b Is Essential for Recycling of Transferrin to the Plasma Membrane","volume":"259","author":"B Schlierf","year":"2000","journal-title":"Exp Cell Res"},{"key":"pbio.3002290.ref032","doi-asserted-by":"crossref","first-page":"612","DOI":"10.1006\/bbrc.1997.7520","article-title":"Rab11 Is Associated with Transferrin-Containing Recycling Compartments in K562 Cells","volume":"239","author":"EG Green","year":"1997","journal-title":"Biochem Biophys Res Commun"},{"key":"pbio.3002290.ref033","doi-asserted-by":"crossref","first-page":"913","DOI":"10.1083\/jcb.135.4.913","article-title":"Rab11 regulates recycling through the pericentriolar recycling endosome","volume":"135","author":"O Ullrich","year":"1996","journal-title":"J Cell Biol"},{"key":"pbio.3002290.ref034","doi-asserted-by":"crossref","first-page":"1022","DOI":"10.1016\/j.tim.2020.05.009","article-title":"Double-Membrane Vesicles as Platforms for Viral Replication","volume":"28","author":"G Wolff","year":"2020","journal-title":"Trends Microbiol"},{"key":"pbio.3002290.ref035","doi-asserted-by":"crossref","first-page":"146","DOI":"10.3389\/fcell.2018.00146","article-title":"Initial Steps in Mammalian Autophagosome Biogenesis","volume":"6","author":"D Grasso","year":"2018","journal-title":"Front Cell Dev Biol"},{"key":"pbio.3002290.ref036","doi-asserted-by":"crossref","first-page":"12420","DOI":"10.1038\/ncomms12420","article-title":"Autophagy initiation by ULK complex assembly on ER tubulovesicular regions marked by ATG9 vesicles","volume":"7","author":"E Karanasios","year":"2016","journal-title":"Nat Commun"},{"key":"pbio.3002290.ref037","doi-asserted-by":"crossref","first-page":"3120","DOI":"10.1002\/1873-3468.13637","article-title":"Hijacking intracellular membranes to feed autophagosomal growth","volume":"593","author":"L Staiano","year":"2019","journal-title":"FEBS Lett"},{"key":"pbio.3002290.ref038","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1038\/s41422-020-00416-2","article-title":"COPII mitigates ER stress by promoting formation of ER whorls","volume":"31","author":"F Xu","year":"2021","journal-title":"Cell Res"},{"key":"pbio.3002290.ref039","doi-asserted-by":"crossref","first-page":"28","DOI":"10.4161\/15548627.2014.984267","article-title":"Posttranslational modification of autophagy-related proteins in macroautophagy","volume":"11","author":"Y. Xie","year":"2015","journal-title":"Autophagy"},{"key":"pbio.3002290.ref040","first-page":"1713","article-title":"Evaluation of white silica sands in North Eastern Desert, Egypt","volume":"8","author":"HAH Ismaiel","year":"2017","journal-title":"Int J Sci Eng Res"},{"key":"pbio.3002290.ref041","doi-asserted-by":"crossref","first-page":"1586","DOI":"10.15252\/embr.201744559","article-title":"Remodeling of ER-exit sites initiates a membrane supply pathway for autophagosome biogenesis","volume":"18","author":"L Ge","year":"2017","journal-title":"EMBO Rep"},{"key":"pbio.3002290.ref042","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1016\/j.devcel.2018.03.008","article-title":"The RAB11A-Positive Compartment Is a Primary Platform for Autophagosome Assembly Mediated by WIPI2 Recognition of PI3P-RAB11","volume":"45","author":"C Puri","year":"2018","journal-title":"A. Dev Cell"},{"key":"pbio.3002290.ref043","doi-asserted-by":"crossref","first-page":"1682","DOI":"10.4161\/auto.21486","article-title":"Recycling endosomes contribute to autophagosome formation","volume":"8","author":"A Longatti","year":"2012","journal-title":"Autophagy"},{"key":"pbio.3002290.ref044","doi-asserted-by":"crossref","first-page":"3888","DOI":"10.1242\/jcs.03172","article-title":"Starvation and ULK1-dependent cycling of mammalian Atg9 between the TGN and endosomes","volume":"119","author":"ARJ Young","year":"2006","journal-title":"J Cell Sci"},{"key":"pbio.3002290.ref045","doi-asserted-by":"crossref","first-page":"1860","DOI":"10.1091\/mbc.e11-09-0746","article-title":"Dynamic and transient interactions of Atg9 with autophagosomes, but not membrane integration, are required for autophagy","volume":"23","author":"A Orsi","year":"2012","journal-title":"Mol Biol Cell"},{"key":"pbio.3002290.ref046","doi-asserted-by":"crossref","first-page":"1634","DOI":"10.1083\/jcb.201901115","article-title":"ATG9A shapes the forming autophagosome through Arfaptin 2 and phosphatidylinositol 4-kinase III\u03b2","author":"D Judith","year":"2019","journal-title":"J Cell Biol"},{"key":"pbio.3002290.ref047","doi-asserted-by":"crossref","first-page":"11869","DOI":"10.1128\/JVI.01634-08","article-title":"Mutational analysis of cis-acting RNA signals in segment 7 of influenza A virus","volume":"82","author":"EC Hutchinson","year":"2008","journal-title":"J Virol"},{"key":"pbio.3002290.ref048","doi-asserted-by":"crossref","first-page":"366","DOI":"10.3390\/v13030366","article-title":"Liquid Biomolecular Condensates and Viral Lifecycles: Review and Perspectives","volume":"13","author":"T Etibor","year":"2021","journal-title":"Viruses"},{"key":"pbio.3002290.ref049","doi-asserted-by":"crossref","first-page":"176","DOI":"10.3389\/fcell.2018.00176","article-title":"A Comprehensive Review on the Interaction Between the Host GTPase Rab11 and Influenza A Virus","volume":"6","author":"MJ Amorim","year":"2019","journal-title":"Front Cell Dev Biol"},{"key":"pbio.3002290.ref050","doi-asserted-by":"crossref","first-page":"eaan5835","DOI":"10.1126\/science.aan5835","article-title":"Here, there, and everywhere: The importance of ER membrane contact sites","volume":"361","author":"H Wu","year":"2018","journal-title":"Science"},{"key":"pbio.3002290.ref051","doi-asserted-by":"crossref","first-page":"e2024681118","DOI":"10.1073\/pnas.2024681118","article-title":"Influenza A viruses balance ER stress with host protein synthesis shutoff","volume":"118","author":"B Mazel-Sanchez","year":"2021","journal-title":"Proc Natl Acad Sci U S A"},{"key":"pbio.3002290.ref052","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/j.chom.2014.01.006","article-title":"A LC3-interacting motif in the influenza A virus M2 protein is required to subvert autophagy and maintain virion stability","volume":"15","author":"R Beale","year":"2014","journal-title":"Cell Host Microbe"},{"key":"pbio.3002290.ref053","doi-asserted-by":"crossref","DOI":"10.1126\/science.aaz7714","article-title":"Reconstitution of autophagosome nucleation defines Atg9 vesicles as seeds for membrane formation","volume":"369","author":"J Sawa-Makarska","year":"2020","journal-title":"Science"},{"key":"pbio.3002290.ref054","article-title":"ATG9A and ATG2A form a heteromeric complex essential for autophagosome formation","author":"AR van Vliet","year":"2022","journal-title":"Mol Cell"},{"key":"pbio.3002290.ref055","doi-asserted-by":"crossref","first-page":"4027","DOI":"10.1002\/1873-3468.12916","article-title":"Mammalian Atg9 contributes to the post-Golgi transport of lysosomal hydrolases by interacting with adaptor protein-1","volume":"591","author":"S Jia","year":"2017","journal-title":"FEBS Lett"},{"key":"pbio.3002290.ref056","doi-asserted-by":"crossref","first-page":"764","DOI":"10.1080\/15548627.2017.1314897","article-title":"Atg9a deficiency causes axon-specific lesions including neuronal circuit dysgenesis","volume":"14","author":"J Yamaguchi","year":"2018","journal-title":"Autophagy"},{"key":"pbio.3002290.ref057","doi-asserted-by":"crossref","first-page":"824","DOI":"10.1016\/j.neuron.2021.12.031","article-title":"Presynaptic autophagy is coupled to the synaptic vesicle cycle via ATG-9","volume":"110","author":"S Yang","year":"2022","journal-title":"Neuron"},{"key":"pbio.3002290.ref058","doi-asserted-by":"crossref","first-page":"e202106014","DOI":"10.1083\/jcb.202106014","article-title":"The core autophagy protein ATG9A controls dynamics of cell protrusions and directed migration","volume":"221","author":"D Campisi","year":"2022","journal-title":"J Cell Biol"},{"key":"pbio.3002290.ref059","doi-asserted-by":"crossref","first-page":"e1005284","DOI":"10.1371\/journal.ppat.1005284","article-title":"Influenza Virus Induces Cholesterol-Enriched Endocytic Recycling Compartments for Budozone Formation via Cell Cycle-Independent Centrosome Maturation","volume":"11","author":"A Kawaguchi","year":"2015","journal-title":"PLoS Pathog"},{"key":"pbio.3002290.ref060","doi-asserted-by":"crossref","first-page":"1660","DOI":"10.1080\/15548627.2019.1632124","article-title":"ATG9A supplies PtdIns4P to the autophagosome initiation site","author":"D Judith","year":"2019","journal-title":"Autophagy"},{"key":"pbio.3002290.ref061","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.sbi.2020.09.004","article-title":"How do intrinsically disordered protein regions encode a driving force for liquid\u2013liquid phase separation?","volume":"67","author":"W Borcherds","year":"2021","journal-title":"Curr Opin Struct Biol"},{"key":"pbio.3002290.ref062","doi-asserted-by":"crossref","first-page":"538","DOI":"10.1016\/j.tcb.2006.08.009","article-title":"Biophysical properties of lipids and dynamic membranes","volume":"16","author":"PA Janmey","year":"2006","journal-title":"Trends Cell Biol"},{"key":"pbio.3002290.ref063","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1006\/jsbi.1996.0013","article-title":"Computer Visualization of Three-Dimensional Image Data Using IMOD","volume":"116","author":"JR Kremer","year":"1996","journal-title":"J Struct Biol"},{"key":"pbio.3002290.ref064","doi-asserted-by":"crossref","first-page":"676","DOI":"10.1038\/nmeth.2019","article-title":"Fiji: an open-source platform for biological-image analysis","volume":"9","author":"J Schindelin","year":"2012","journal-title":"Nat Methods"},{"key":"pbio.3002290.ref065","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1016\/j.ymeth.2016.09.016","article-title":"TrackMate: An open and extensible platform for single-particle tracking","volume":"115","author":"J-Y Tinevez","year":"2017","journal-title":"Methods"},{"key":"pbio.3002290.ref066","article-title":"Probabilistic Noise2Void: Unsupervised Content-Aware Denoising","volume":"2","author":"A Krull","year":"2020","journal-title":"Front Comp Sci"},{"key":"pbio.3002290.ref067","doi-asserted-by":"crossref","first-page":"2276","DOI":"10.1038\/s41467-021-22518-0","article-title":"Democratising deep learning for microscopy with ZeroCostDL4Mic","volume":"12","author":"L von Chamier","year":"2021","journal-title":"Nat Commun"},{"key":"pbio.3002290.ref068","doi-asserted-by":"crossref","first-page":"3993","DOI":"10.1529\/biophysj.103.038422","article-title":"Automatic and Quantitative Measurement of Protein-Protein Colocalization in Live Cells","volume":"86","author":"SV Costes","year":"2004","journal-title":"Biophys J"},{"key":"pbio.3002290.ref069","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.jviromet.2010.12.014","article-title":"Strand-specific real-time RT-PCR for distinguishing influenza vRNA, cRNA, and mRNA","volume":"173","author":"E. Kawakami","year":"2011","journal-title":"J Virol Methods"}],"updated-by":[{"DOI":"10.1371\/journal.pbio.3002290","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2023,12,4]],"date-time":"2023-12-04T00:00:00Z","timestamp":1701648000000}}],"container-title":["PLOS Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pbio.3002290","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,11,2]],"date-time":"2024-11-02T08:04:25Z","timestamp":1730534665000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pbio.3002290"}},"subtitle":[],"editor":[{"given":"Andrew","family":"Mehle","sequence":"first","affiliation":[]}],"short-title":[],"issued":{"date-parts":[[2023,11,20]]},"references-count":69,"journal-issue":{"issue":"11","published-online":{"date-parts":[[2023,11,20]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pbio.3002290","relation":{"new_version":[{"id-type":"doi","id":"10.1371\/journal.pbio.3002290","asserted-by":"object"}]},"ISSN":["1545-7885"],"issn-type":[{"value":"1545-7885","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,11,20]]}}}