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Cited by 44Autophagy in Disease and TherapyCellular transport and secretionCalcium signaling and nucleotide metabolism

Neuronal Autophagy: Regulations and Implications in Health and Disease

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Liénard, Caroline, Pintart, Alexandre, Bomont, Pascale·2024·Cells
DOI 10.3390/cells13010103PMC PMC10778363
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Abstract

Autophagy is a major degradative pathway that plays a key role in sustaining cell homeostasis, integrity, and physiological functions. Macroautophagy, which ensures the clearance of cytoplasmic components engulfed in a double-membrane autophagosome that fuses with lysosomes, is orchestrated by a complex cascade of events. Autophagy has a particularly strong impact on the nervous system, and mutations in core components cause numerous neurological diseases. We first review the regulation of autophagy, from autophagosome biogenesis to lysosomal degradation and associated neurodevelopmental/neurodegenerative disorders. We then describe how this process is specifically regulated in the axon and in the somatodendritic compartment and how it is altered in diseases. In particular, we present the neuronal specificities of autophagy, with the spatial control of autophagosome biogenesis, the close relationship of maturation with axonal transport, and the regulation by synaptic activity. Finally, we discuss the physiological functions of autophagy in the nervous system, during development and in adulthood.

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  • Genetic, biochemical, and imaging studies suggest that the autophagic defect in AD lies not in autophagosome formation but in their maturation and fusion with lysosomes, impairing cargo degradation.

    “Genetic, biochemical, and imaging studies suggest that the defect lies not in autophagosome formation but in their maturation and fusion with lysosomes, impairing cargo degradation [136].”

    From Toward a Unified Framework in Molecular Neurobiology of Alzheimer’s Disease: Revisiting the Pathophysiological Hypotheses (2026) · cites this paper as [136]

    Section 3.1 reports immature autophagic vesicles in AD brain samples and says this suggests a defect in their maturation and/or transport. Section 2.3 explains that fusion with lysosomes enables cargo degradation, but the AD passage does not establish fusion failure specifically. Section 4.4 also mentions failed autophagosome formation in dementia symptoms present in AD, so the claim’s exclusion of formation defects is not supported. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

  • A hallmark observation in AD brains is accumulation of autophagic vacuoles in swollen dystrophic neurites, reflecting impaired clearance rather than upregulated initiation.

    “A hallmark observation in AD brains is the accumulation of autophagic vacuoles in swollen dystrophic neurites, reflecting impaired clearance rather than upregulated initiation [136].”

    From Toward a Unified Framework in Molecular Neurobiology of Alzheimer’s Disease: Revisiting the Pathophysiological Hypotheses (2026) · cites this paper as [136]

    Section 3.1 reports that AD brain samples have an abnormal accumulation of immature autophagic vacuoles in dystrophic neurites and says this suggests defective maturation and/or transport. It does not establish impaired clearance as the definitive cause or explicitly rule out upregulated initiation. The reference to swollen axons concerns AD mice, not the described human brain samples; page numbers are unavailable in our copy. (LLM, conf=0.84)

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  1. [1]Parzych K.R. Klionsky D.J. An Overview of Autophagy: Morphology, Mechanism, and Regulation Antioxid. Redox Signal. 2014 20 460 473 10.1089/ars.2013.5371 23725295 PMC3894687 · DOI · Paper page
  2. [2]Klionsky D.J. Petroni G. Amaravadi R.K. Baehrecke E.H. Ballabio A. Boya P. Bravo-San Pedro J.M. Cadwell K. Cecconi F. Choi A.M.K. Autophagy in Major Human Diseases EMBO J. 2021 40 e108863 10.15252/embj.2021108863 34459017 PMC8488577 · DOI · Paper page
  3. [3]Ichimiya T. Yamakawa T. Hirano T. Yokoyama Y. Hayashi Y. Hirayama D. Wagatsuma K. Itoi T. Nakase H. Autophagy and Autophagy-Related Diseases: A Review Int. J. Mol. Sci. 2020 21 8974 10.3390/ijms21238974 33255983 PMC7729615 · DOI
  4. [5]Mizushima N. Yamamoto A. Matsui M. Yoshimori T. Ohsumi Y. In Vivo Analysis of Autophagy in Response to Nutrient Starvation Using Transgenic Mice Expressing a Fluorescent Autophagosome Marker Mol. Biol. Cell 2004 15 1101 1111 10.1091/mbc.e03-09-0704 14699058 PMC363084 · DOI
  5. [6]Deng Z. Zhou X. Lu J.-H. Yue Z. Autophagy Deficiency in Neurodevelopmental Disorders Cell Biosci. 2021 11 214 10.1186/s13578-021-00726-x 34920755 PMC8684077 · DOI
  6. [7]Fleming A. Bourdenx M. Fujimaki M. Karabiyik C. Krause G.J. Lopez A. Martín-Segura A. Puri C. Scrivo A. Skidmore J. The Different Autophagy Degradation Pathways and Neurodegeneration Neuron 2022 110 935 966 10.1016/j.neuron.2022.01.017 35134347 PMC8930707 · DOI
  7. [8]Zatyka M. Sarkar S. Barrett T. Autophagy in Rare (NonLysosomal) Neurodegenerative Diseases J. Mol. Biol. 2020 432 2735 2753 10.1016/j.jmb.2020.02.012 32087199 PMC7232014 · DOI
  8. [9]Ashford T.P. Porter K.R. Cytoplasmic components in hepatic cell lysosomes J. Cell Biol. 1962 12 198 202 10.1083/jcb.12.1.198 13862833 PMC2106008 · DOI
  9. [10]Deter R.L. De Duve C. Influence of glucagon, an inducer of cellular autophagy, on some physical properties of rat liver lysosomes J. Cell Biol. 1967 33 437 449 10.1083/jcb.33.2.437 4292315 PMC2108350 · DOI · Paper page
  10. [12]Mortimore G.E. Schworer C.M. Induction of Autophagy by Amino-Acid Deprivation in Perfused Rat Liver Nature 1977 270 174 176 10.1038/270174a0 927529 · DOI
  11. [13]Li W. He P. Huang Y. Li Y.-F. Lu J. Li M. Kurihara H. Luo Z. Meng T. Onishi M. Selective Autophagy of Intracellular Organelles: Recent Research Advances Theranostics 2021 11 222 256 10.7150/thno.49860 33391472 PMC7681076 · DOI
  12. [15]Kim J. Kundu M. Viollet B. Guan K.-L. AMPK and mTOR Regulate Autophagy through Direct Phosphorylation of Ulk1 Nat. Cell Biol. 2011 13 132 141 10.1038/ncb2152 21258367 PMC3987946 · DOI · Paper page
  13. [16]Noda N.N. Fujioka Y. Atg1 Family Kinases in Autophagy Initiation Cell. Mol. Life Sci. 2015 72 3083 3096 10.1007/s00018-015-1917-z 25948417 PMC4506457 · DOI
  14. [17]Kim B.-W. Jin Y. Kim J. Kim J.H. Jung J. Kang S. Kim I.Y. Kim J. Cheong H. Song H.K. The C-Terminal Region of ATG101 Bridges ULK1 and PtdIns3K Complex in Autophagy Initiation Autophagy 2018 14 2104 2116 10.1080/15548627.2018.1504716 30081750 PMC6984762 · DOI
  15. [18]Petiot A. Ogier-Denis E. Blommaart E.F. Meijer A.J. Codogno P. Distinct Classes of Phosphatidylinositol 3′-Kinases Are Involved in Signaling Pathways That Control Macroautophagy in HT-29 Cells J. Biol. Chem. 2000 275 992 998 10.1074/jbc.275.2.992 10625637 · DOI
  16. [19]Polson H.E.J. de Lartigue J. Rigden D.J. Reedijk M. Urbé S. Clague M.J. Tooze S.A. Mammalian Atg18 (WIPI2) Localizes to Omegasome-Anchored Phagophores and Positively Regulates LC3 Lipidation Autophagy 2010 6 506 522 10.4161/auto.6.4.11863 20505359 · DOI · Paper page
  17. [20]Kishi-Itakura C. Koyama-Honda I. Itakura E. Mizushima N. Ultrastructural Analysis of Autophagosome Organization Using Mammalian Autophagy-Deficient Cells J. Cell Sci. 2014 127 4984 10.1242/jcs.164293 25052093 · DOI
  18. [21]Dooley H.C. Razi M. Polson H.E.J. Girardin S.E. Wilson M.I. Tooze S.A. WIPI2 Links LC3 Conjugation with PI3P, Autophagosome Formation, and Pathogen Clearance by Recruiting Atg12–5-16L1 Mol. Cell 2014 55 238 252 10.1016/j.molcel.2014.05.021 24954904 PMC4104028 · DOI
  19. [22]Bakula D. Müller A.J. Zuleger T. Takacs Z. Franz-Wachtel M. Thost A.-K. Brigger D. Tschan M.P. Frickey T. Robenek H. WIPI3 and WIPI4 β-Propellers Are Scaffolds for LKB1-AMPK-TSC Signalling Circuits in the Control of Autophagy Nat. Commun. 2017 8 15637 10.1038/ncomms15637 28561066 PMC5460038 · DOI
  20. [23]Maeda S. Otomo C. Otomo T. The Autophagic Membrane Tether ATG2A Transfers Lipids between Membranes eLife 2019 8 e45777 10.7554/eLife.45777 31271352 PMC6625793 · DOI
  21. [24]Valverde D.P. Yu S. Boggavarapu V. Kumar N. Lees J.A. Walz T. Reinisch K.M. Melia T.J. ATG2 Transports Lipids to Promote Autophagosome Biogenesis J. Cell Biol. 2019 218 1787 1798 10.1083/jcb.201811139 30952800 PMC6548141 · DOI
  22. [25]Young A.R.J. Chan E.Y.W. Hu X.W. Köchl R. Crawshaw S.G. High S. Hailey D.W. Lippincott-Schwartz J. Tooze S.A. Starvation and ULK1-Dependent Cycling of Mammalian Atg9 between the TGN and Endosomes J. Cell Sci. 2006 119 3888 3900 10.1242/jcs.03172 16940348 · DOI · Paper page
  23. [26]Cooper G.M. Coe B.P. Girirajan S. Rosenfeld J.A. Vu T.H. Baker C. Williams C. Stalker H. Hamid R. Hannig V. A Copy Number Variation Morbidity Map of Developmental Delay Nat. Genet. 2011 43 838 846 10.1038/ng.909 21841781 PMC3171215 · DOI · Paper page
  24. [27]Degenhardt F. Priebe L. Meier S. Lennertz L. Streit F. Witt S.H. Hofmann A. Becker T. Mössner R. Maier W. Duplications in RB1CC1 Are Associated with Schizophrenia; Identification in Large European Sample Sets Transl. Psychiatry 2013 3 e326 10.1038/tp.2013.101 26151896 PMC3849960 · DOI
  25. [29]Xu B. Roos J.L. Dexheimer P. Boone B. Plummer B. Levy S. Gogos J.A. Karayiorgou M. Exome Sequencing Supports a de Novo Mutational Paradigm for Schizophrenia Nat. Genet. 2011 43 864 868 10.1038/ng.902 21822266 PMC3196550 · DOI
  26. [30]Ye J. Tong Y. Lv J. Peng R. Chen S. Kuang L. Su K. Zheng Y. Zhang T. Zhang F. Rare Mutations in the Autophagy-Regulating Gene AMBRA1 Contribute to Human Neural Tube Defects Hum. Mutat. 2020 41 1383 1393 10.1002/humu.24028 32333458 · DOI
  27. [31]Gstrein T. Edwards A. Přistoupilová A. Leca I. Breuss M. Pilat-Carotta S. Hansen A.H. Tripathy R. Traunbauer A.K. Hochstoeger T. Mutations in Vps15 Perturb Neuronal Migration in Mice and Are Associated with Neurodevelopmental Disease in Humans Nat. Neurosci. 2018 21 207 217 10.1038/s41593-017-0053-5 29311744 PMC5897053 · DOI
  28. [32]Vilariño-Güell C. Wider C. Ross O.A. Dachsel J.C. Kachergus J.M. Lincoln S.J. Soto-Ortolaza A.I. Cobb S.A. Wilhoite G.J. Bacon J.A. VPS35 Mutations in Parkinson Disease Am. J. Hum. Genet. 2011 89 162 167 10.1016/j.ajhg.2011.06.001 21763482 PMC3135796 · DOI
  29. [33]Zimprich A. Benet-Pagès A. Struhal W. Graf E. Eck S.H. Offman M.N. Haubenberger D. Spielberger S. Schulte E.C. Lichtner P. A Mutation in VPS35, Encoding a Subunit of the Retromer Complex, Causes Late-Onset Parkinson Disease Am. J. Hum. Genet. 2011 89 168 175 10.1016/j.ajhg.2011.06.008 21763483 PMC3135812 · DOI
  30. [34]Zavodszky E. Seaman M.N.J. Moreau K. Jimenez-Sanchez M. Breusegem S.Y. Harbour M.E. Rubinsztein D.C. Mutation in VPS35 Associated with Parkinson’s Disease Impairs WASH Complex Association and Inhibits Autophagy Nat. Commun. 2014 5 3828 10.1038/ncomms4828 24819384 PMC4024763 · DOI · Paper page
  31. [35]Collier J.J. Guissart C. Oláhová M. Sasorith S. Piron-Prunier F. Suomi F. Zhang D. Martinez-Lopez N. Leboucq N. Bahr A. Developmental Consequences of Defective ATG7-Mediated Autophagy in Humans N. Engl. J. Med. 2021 384 2406 2417 10.1056/NEJMoa1915722 34161705 PMC7611730 · DOI
  32. [36]Chen D. Pang S. Feng X. Huang W. Hawley R.G. Yan B. Genetic Analysis of the ATG7 Gene Promoter in Sporadic Parkinson’s Disease Neurosci. Lett. 2013 534 193 198 10.1016/j.neulet.2012.12.039 23295909 · DOI
  33. [37]Chen D. Zhu C. Wang X. Feng X. Pang S. Huang W. Hawley R.G. Yan B. A Novel and Functional Variant within the ATG5 Gene Promoter in Sporadic Parkinson’s Disease Neurosci. Lett. 2013 538 49 53 10.1016/j.neulet.2013.01.044 23384565 · DOI
  34. [38]Kim M. Sandford E. Gatica D. Qiu Y. Liu X. Zheng Y. Schulman B.A. Xu J. Semple I. Ro S.-H. Mutation in ATG5 Reduces Autophagy and Leads to Ataxia with Developmental Delay eLife 2016 5 e12245 10.7554/eLife.12245 26812546 PMC4786408 · DOI · Paper page
  35. [39]Xu J. Xia L. Shang Q. Du J. Zhu D. Wang Y. Bi D. Song J. Ma C. Gao C. A Variant of the Autophagy-Related 5 Gene Is Associated with Child Cerebral Palsy Front. Cell. Neurosci. 2017 11 407 10.3389/fncel.2017.00407 29326554 PMC5741640 · DOI
  36. [40]Li Y. Huang J. Pang S. Wang H. Zhang A. Hawley R.G. Yan B. Novel and Functional ATG12 Gene Variants in Sporadic Parkinson’s Disease Neurosci. Lett. 2017 643 22 26 10.1016/j.neulet.2017.02.028 28229934 · DOI
  37. [41]Saitsu H. Nishimura T. Muramatsu K. Kodera H. Kumada S. Sugai K. Kasai-Yoshida E. Sawaura N. Nishida H. Hoshino A. De Novo Mutations in the Autophagy Gene WDR45 Cause Static Encephalopathy of Childhood with Neurodegeneration in Adulthood Nat. Genet. 2013 45 445 449 10.1038/ng.2562 23435086 · DOI · Paper page
  38. [42]Jelani M. Dooley H.C. Gubas A. Mohamoud H.S.A. Khan M.T.M. Ali Z. Kang C. Rahim F. Jan A. Vadgama N. A Mutation in the Major Autophagy Gene, WIPI2, Associated with Global Developmental Abnormalities Brain 2019 142 1242 1254 10.1093/brain/awz075 30968111 PMC6487338 · DOI · Paper page
  39. [43]Maroofian R. Gubas A. Kaiyrzhanov R. Scala M. Hundallah K. Severino M. Abdel-Hamid M.S. Rosenfeld J.A. Ebrahimi-Fakhari D. Ali Z. Homozygous Missense WIPI2 Variants Cause a Congenital Disorder of Autophagy with Neurodevelopmental Impairments of Variable Clinical Severity and Disease Course Brain Commun. 2021 3 fcab183 10.1093/braincomms/fcab183 34557665 PMC8453401 · DOI
  40. [44]Xu J. Yang Y. Pang S. Huang W. Qin X. Hawley R.G. Yan B. Identification of a Novel 21bp-Insertion Variant within the LC3B Gene Promoter in Sporadic Parkinson’s Disease Transl. Res. 2013 161 441 443 10.1016/j.trsl.2012.12.006 23318414 · DOI
  41. [45]Poultney C.S. Goldberg A.P. Drapeau E. Kou Y. Harony-Nicolas H. Kajiwara Y. De Rubeis S. Durand S. Stevens C. Rehnström K. Identification of Small Exonic CNV from Whole-Exome Sequence Data and Application to Autism Spectrum Disorder Am. J. Hum. Genet. 2013 93 607 619 10.1016/j.ajhg.2013.09.001 24094742 PMC3791269 · DOI · Paper page
  42. [46]Kadir R. Harel T. Markus B. Perez Y. Bakhrat A. Cohen I. Volodarsky M. Feintsein-Linial M. Chervinski E. Zlotogora J. ALFY-Controlled DVL3 Autophagy Regulates Wnt Signaling, Determining Human Brain Size PLoS Genet. 2016 12 e1005919 10.1371/journal.pgen.1005919 27008544 PMC4805177 · DOI
  43. [47]Haack T.B. Ignatius E. Calvo-Garrido J. Iuso A. Isohanni P. Maffezzini C. Lönnqvist T. Suomalainen A. Gorza M. Kremer L.S. Absence of the Autophagy Adaptor SQSTM1/P62 Causes Childhood-Onset Neurodegeneration with Ataxia, Dystonia, and Gaze Palsy Am. J. Hum. Genet. 2016 99 735 743 10.1016/j.ajhg.2016.06.026 27545679 PMC5010644 · DOI
  44. [48]Fecto F. SQSTM1 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis Arch. Neurol. 2011 68 1440 10.1001/archneurol.2011.250 22084127 · DOI · Paper page
  45. [49]Rubino E. Rainero I. Chio A. Rogaeva E. Galimberti D. Fenoglio P. Grinberg Y. Isaia G. Calvo A. Gentile S. SQSTM1 Mutations in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis Neurology 2012 79 1556 1562 10.1212/WNL.0b013e31826e25df 22972638 PMC3655323 · DOI · Paper page
  46. [50]Le Ber I. SQSTM1 Mutations in French Patients with Frontotemporal Dementia or Frontotemporal Dementia with Amyotrophic Lateral Sclerosis JAMA Neurol. 2013 70 1403 1410 10.1001/jamaneurol.2013.3849 24042580 PMC4199096 · DOI
  47. [51]Boutoleau-Bretonnière C. Camuzat A. Le Ber I. Bouya-Ahmed K. Guerreiro R. Deruet A.-L. Evrard C. Bras J. Lamy E. Auffray-Calvier E. A Phenotype of Atypical Apraxia of Speech in a Family Carrying SQSTM1 Mutation J. Alzheimers Dis. 2014 43 625 630 10.3233/JAD-141512 25114083 PMC4337967 · DOI
  48. [52]Goode A. Butler K. Long J. Cavey J. Scott D. Shaw B. Sollenberger J. Gell C. Johansen T. Oldham N.J. Defective Recognition of LC3B by Mutant SQSTM1/P62 Implicates Impairment of Autophagy as a Pathogenic Mechanism in ALS-FTLD Autophagy 2016 12 1094 1104 10.1080/15548627.2016.1170257 27158844 PMC4990988 · DOI · Paper page
  49. [53]Deng Z. Lim J. Wang Q. Purtell K. Wu S. Palomo G.M. Tan H. Manfredi G. Zhao Y. Peng J. ALS-FTLD-Linked Mutations of SQSTM1/P62 Disrupt Selective Autophagy and NFE2L2/NRF2 Anti-Oxidative Stress Pathway Autophagy 2020 16 917 931 10.1080/15548627.2019.1644076 31362587 PMC7144840 · DOI
  50. [54]Cuyvers E. van der Zee J. Bettens K. Engelborghs S. Vandenbulcke M. Robberecht C. Dillen L. Merlin C. Geerts N. Graff C. Genetic Variability in SQSTM1 and Risk of Early-Onset Alzheimer Dementia: A European Early-Onset Dementia Consortium Study Neurobiol. Aging 2015 36 2005.e15 2005.e22 10.1016/j.neurobiolaging.2015.02.014 25796131 · DOI
  51. [55]Odagiri S. Tanji K. Mori F. Kakita A. Takahashi H. Wakabayashi K. Autophagic Adapter Protein NBR1 Is Localized in Lewy Bodies and Glial Cytoplasmic Inclusions and Is Involved in Aggregate Formation in α-Synucleinopathy Acta Neuropathol. 2012 124 173 186 10.1007/s00401-012-0975-7 22484440 · DOI
  52. [57]Maruyama H. Morino H. Ito H. Izumi Y. Kato H. Watanabe Y. Kinoshita Y. Kamada M. Nodera H. Suzuki H. Mutations of Optineurin in Amyotrophic Lateral Sclerosis Nature 2010 465 223 226 10.1038/nature08971 20428114 · DOI · Paper page
  53. [58]Shen W.-C. Li H.-Y. Chen G.-C. Chern Y. Tu P. Mutations in the Ubiquitin-Binding Domain of OPTN/Optineurin Interfere with Autophagy-Mediated Degradation of Misfolded Proteins by a Dominant-Negative Mechanism Autophagy 2015 11 685 700 10.4161/auto.36098 25484089 PMC4502753 · DOI
  54. [59]Synofzik M. Maetzler W. Grehl T. Prudlo J. vom Hagen J.M. Haack T. Rebassoo P. Munz M. Schöls L. Biskup S. Screening in ALS and FTD Patients Reveals 3 Novel UBQLN2 Mutations Outside the PXX Domain and a Pure FTD Phenotype Neurobiol. Aging 2012 33 2949.e13 2949.e17 10.1016/j.neurobiolaging.2012.07.002 22892309 · DOI
  55. [60]Deng H.-X. Chen W. Hong S.-T. Boycott K.M. Gorrie G.H. Siddique N. Yang Y. Fecto F. Shi Y. Zhai H. Mutations in UBQLN2 Cause Dominant X-Linked Juvenile and Adult-Onset ALS and ALS/Dementia Nature 2011 477 211 215 10.1038/nature10353 21857683 PMC3169705 · DOI · Paper page
  56. [61]Zivony-Elboum Y. Westbroek W. Kfir N. Savitzki D. Shoval Y. Bloom A. Rod R. Khayat M. Gross B. Samri W. A Founder Mutation in Vps37A Causes Autosomal Recessive Complex Hereditary Spastic Paraparesis J. Med. Genet. 2012 49 462 472 10.1136/jmedgenet-2012-100742 22717650 · DOI
  57. [62]Rodger C. Flex E. Allison R.J. Sanchis-Juan A. Hasenahuer M.A. Cecchetti S. French C.E. Edgar J.R. Carpentieri G. Ciolfi A. De Novo VPS4A Mutations Cause Multisystem Disease with Abnormal Neurodevelopment Am. J. Hum. Genet. 2020 107 1129 1148 10.1016/j.ajhg.2020.10.012 33186545 PMC7820634 · DOI
  58. [63]Mochida G.H. Ganesh V.S. de Michelena M.I. Dias H. Atabay K.D. Kathrein K.L. Huang H.-T. Hill R.S. Felie J.M. Rakiec D. CHMP1A Encodes an Essential Regulator of BMI1-INK4A in Cerebellar Development Nat. Genet. 2012 44 1260 1264 10.1038/ng.2425 23023333 PMC3567443 · DOI
  59. [67]Lee J.-A. Beigneux A. Ahmad S.T. Young S.G. Gao F.-B. ESCRT-III Dysfunction Causes Autophagosome Accumulation and Neurodegeneration Curr. Biol. 2007 17 1561 1567 10.1016/j.cub.2007.07.029 17683935 · DOI
  60. [68]Lee J.-A. Gao F.-B. Inhibition of Autophagy Induction Delays Neuronal Cell Loss Caused by Dysfunctional ESCRT-III in Frontotemporal Dementia J. Neurosci. 2009 29 8506 8511 10.1523/JNEUROSCI.0924-09.2009 19571141 PMC2726650 · DOI
  61. [69]Verhoeven K. De Jonghe P. Coen K. Verpoorten N. Auer-Grumbach M. Kwon J.M. FitzPatrick D. Schmedding E. De Vriendt E. Jacobs A. Mutations in the Small GTP-Ase Late Endosomal Protein RAB7 Cause Charcot-Marie-Tooth Type 2B Neuropathy Am. J. Hum. Genet. 2003 72 722 727 10.1086/367847 12545426 PMC1180247 · DOI
  62. [70]Romano R. Del Fiore V.S. Saveri P. Palamà I.E. Pisciotta C. Pareyson D. Bucci C. Guerra F. Autophagy and Lysosomal Functionality in CMT2B Fibroblasts Carrying the RAB7K126R Mutation Cells 2022 11 496 10.3390/cells11030496 35159308 PMC8834514 · DOI
  63. [71]Cullup T. Kho A.L. Dionisi-Vici C. Brandmeier B. Smith F. Urry Z. Simpson M.A. Yau S. Bertini E. McClelland V. Recessive Mutations in EPG5 Cause Vici Syndrome, a Multisystem Disorder with Defective Autophagy Nat. Genet. 2013 45 83 87 10.1038/ng.2497 23222957 PMC4012842 · DOI
  64. [72]Ji C. Zhao H. Chen D. Zhang H. Zhao Y.G. β-Propeller Proteins WDR45 and WDR45B Regulate Autophagosome Maturation into Autolysosomes in Neural Cells Curr. Biol. 2021 31 1666 1677.e6 10.1016/j.cub.2021.01.081 33636118 · DOI
  65. [73]Akizu N. Cantagrel V. Zaki M.S. Al-Gazali L. Wang X. Rosti R.O. Dikoglu E. Gelot A.B. Rosti B. Vaux K.K. Biallelic Mutations in SNX14 Cause a Syndromic Form of Cerebellar Atrophy and Lysosome-Autophagosome Dysfunction Nat. Genet. 2015 47 528 534 10.1038/ng.3256 25848753 PMC4414867 · DOI
  66. [74]Bryant D. Liu Y. Datta S. Hariri H. Seda M. Anderson G. Peskett E. Demetriou C. Sousa S. Jenkins D. SNX14 Mutations Affect Endoplasmic Reticulum-Associated Neutral Lipid Metabolism in Autosomal Recessive Spinocerebellar Ataxia 20 Hum. Mol. Genet. 2018 27 1927 1940 10.1093/hmg/ddy101 29635513 PMC5961352 · DOI
  67. [75]Thomas A.C. Williams H. Setó-Salvia N. Bacchelli C. Jenkins D. O’Sullivan M. Mengrelis K. Ishida M. Ocaka L. Chanudet E. Mutations in SNX14 Cause a Distinctive Autosomal-Recessive Cerebellar Ataxia and Intellectual Disability Syndrome Am. J. Hum. Genet. 2014 95 611 621 10.1016/j.ajhg.2014.10.007 25439728 PMC4225633 · DOI
  68. [76]Liang C.-C. Wang C. Peng X. Gan B. Guan J.-L. Neural-Specific Deletion of FIP200 Leads to Cerebellar Degeneration Caused by Increased Neuronal Death and Axon Degeneration J. Biol. Chem. 2010 285 3499 3509 10.1074/jbc.M109.072389 19940130 PMC2823459 · DOI
  69. [77]Wen J. Zellner A. Braun N.C. Bajaj T. Gassen N.C. Peitz M. Brüstle O. Loss of Function of FIP200 in Human Pluripotent Stem Cell-Derived Neurons Leads to Axonal Pathology and Hyperactivity Transl. Psychiatry 2023 13 143 10.1038/s41398-023-02432-3 37137886 PMC10156752 · DOI
  70. [78]Maria Fimia G. Stoykova A. Romagnoli A. Giunta L. Di Bartolomeo S. Nardacci R. Corazzari M. Fuoco C. Ucar A. Schwartz P. Ambra1 Regulates Autophagy and Development of the Nervous System Nature 2007 447 1121 1125 10.1038/nature05925 17589504 · DOI
  71. [79]Mattera R. Park S.Y. De Pace R. Guardia C.M. Bonifacino J.S. AP-4 Mediates Export of ATG9A from the Trans -Golgi Network to Promote Autophagosome Formation Proc. Natl. Acad. Sci. USA 2017 114 E10697 E10706 10.1073/pnas.1717327114 29180427 PMC5740629 · DOI
  72. [80]De Pace R. Skirzewski M. Damme M. Mattera R. Mercurio J. Foster A.M. Cuitino L. Jarnik M. Hoffmann V. Morris H.D. Altered Distribution of ATG9A and Accumulation of Axonal Aggregates in Neurons from a Mouse Model of AP-4 Deficiency Syndrome PLoS Genet. 2018 14 e1007363 10.1371/journal.pgen.1007363 29698489 PMC5940238 · DOI
  73. [81]Behne R. Teinert J. Wimmer M. D’Amore A. Davies A.K. Scarrott J.M. Eberhardt K. Brechmann B. Chen I.P.-F. Buttermore E.D. Adaptor Protein Complex 4 Deficiency: A Paradigm of Childhood-Onset Hereditary Spastic Paraplegia Caused by Defective Protein Trafficking Hum. Mol. Genet. 2020 29 320 334 10.1093/hmg/ddz310 31915823 PMC7001721 · DOI
  74. [82]Mizushima N. Noda T. Yoshimori T. Tanaka Y. Ishii T. George M.D. Klionsky D.J. Ohsumi M. Ohsumi Y. A Protein Conjugation System Essential for Autophagy Nature 1998 395 395 398 10.1038/26506 9759731 · DOI
  75. [83]Kim J. Dalton V.M. Eggerton K.P. Scott S.V. Klionsky D.J. Apg7p/Cvt2p Is Required for the Cytoplasm-to-Vacuole Targeting, Macroautophagy, and Peroxisome Degradation Pathways Mol. Biol. Cell 1999 10 1337 1351 10.1091/mbc.10.5.1337 10233148 PMC25275 · DOI
  76. [84]Shintani T. Mizushima N. Ogawa Y. Matsuura A. Noda T. Ohsumi Y. Apg10p, a Novel Protein-Conjugating Enzyme Essential for Autophagy in Yeast EMBO J. 1999 18 5234 5241 10.1093/emboj/18.19.5234 10508157 PMC1171594 · DOI
  77. [85]Nishimura T. Kaizuka T. Cadwell K. Sahani M.H. Saitoh T. Akira S. Virgin H.W. Mizushima N. FIP200 Regulates Targeting of Atg16L1 to the Isolation Membrane EMBO Rep. 2013 14 284 291 10.1038/embor.2013.6 23392225 PMC3589088 · DOI
  78. [86]Kuma A. Mizushima N. Ishihara N. Ohsumi Y. Formation of the Approximately 350-kDa Apg12-Apg5.Apg16 Multimeric Complex, Mediated by Apg16 Oligomerization, Is Essential for Autophagy in Yeast J. Biol. Chem. 2002 277 18619 18625 10.1074/jbc.M111889200 11897782 · DOI
  79. [88]Kirisako T. Ichimura Y. Okada H. Kabeya Y. Mizushima N. Yoshimori T. Ohsumi M. Takao T. Noda T. Ohsumi Y. The Reversible Modification Regulates the Membrane-Binding State of Apg8/Aut7 Essential for Autophagy and the Cytoplasm to Vacuole Targeting Pathway J. Cell Biol. 2000 151 263 276 10.1083/jcb.151.2.263 11038174 PMC2192639 · DOI
  80. [89]Ichimura Y. Kirisako T. Takao T. Satomi Y. Shimonishi Y. Ishihara N. Mizushima N. Tanida I. Kominami E. Ohsumi M. A Ubiquitin-like System Mediates Protein Lipidation Nature 2000 408 488 492 10.1038/35044114 11100732 · DOI
  81. [91]Hanada T. Satomi Y. Takao T. Ohsumi Y. The Amino-Terminal Region of Atg3 Is Essential for Association with Phosphatidylethanolamine in Atg8 Lipidation FEBS Lett. 2009 583 1078 1083 10.1016/j.febslet.2009.03.009 19285500 · DOI
  82. [92]Fujita N. Itoh T. Omori H. Fukuda M. Noda T. Yoshimori T. The Atg16L Complex Specifies the Site of LC3 Lipidation for Membrane Biogenesis in Autophagy Mol. Biol. Cell 2008 19 2092 2100 10.1091/mbc.e07-12-1257 18321988 PMC2366860 · DOI
  83. [94]Hara T. Nakamura K. Matsui M. Yamamoto A. Nakahara Y. Suzuki-Migishima R. Yokoyama M. Mishima K. Saito I. Okano H. Suppression of Basal Autophagy in Neural Cells Causes Neurodegenerative Disease in Mice Nature 2006 441 885 889 10.1038/nature04724 16625204 · DOI · Paper page
  84. [96]Wu G. Wang X. Feng X. Zhang A. Li J. Gu K. Huang J. Pang S. Dong H. Gao H. Altered Expression of Autophagic Genes in the Peripheral Leukocytes of Patients with Sporadic Parkinson’s Disease Brain Res. 2011 1394 105 111 10.1016/j.brainres.2011.04.013 21514572 · DOI
  85. [97]N’Diaye E.-N. Debnath J. Brown E.J. Ubiquilins Accelerate Autophagosome Maturation and Promote Cell Survival during Nutrient Starvation Autophagy 2009 5 573 575 10.4161/auto.5.4.8312 19398896 · DOI
  86. [99]Wang H. Monteiro M.J. Ubiquilin Interacts and Enhances the Degradation of Expanded-Polyglutamine Proteins Biochem. Biophys. Res. Commun. 2007 360 423 427 10.1016/j.bbrc.2007.06.097 17603015 PMC2062524 · DOI
  87. [100]Rutherford N.J. Lewis J. Clippinger A.K. Thomas M.A. Adamson J. Cruz P.E. Cannon A. Xu G. Golde T.E. Shaw G. Unbiased Screen Reveals Ubiquilin-1 and -2 Highly Associated with Huntingtin Inclusions Brain Res. 2013 1524 62 73 10.1016/j.brainres.2013.06.006 23774650 PMC3914001 · DOI
  88. [101]Khaminets A. Behl C. Dikic I. Ubiquitin-Dependent And Independent Signals In Selective Autophagy Trends Cell Biol. 2016 26 6 16 10.1016/j.tcb.2015.08.010 26437584 · DOI
  89. [102]Adriaenssens E. Ferrari L. Martens S. Orchestration of Selective Autophagy by Cargo Receptors Curr. Biol. 2022 32 R1357 R1371 10.1016/j.cub.2022.11.002 36538890 · DOI
  90. [103]Bjørkøy G. Lamark T. Brech A. Outzen H. Perander M. Øvervatn A. Stenmark H. Johansen T. P62/SQSTM1 Forms Protein Aggregates Degraded by Autophagy and Has a Protective Effect on Huntingtin-Induced Cell Death J. Cell Biol. 2005 171 603 614 10.1083/jcb.200507002 16286508 PMC2171557 · DOI · Paper page
  91. [104]Pankiv S. Clausen T.H. Lamark T. Brech A. Bruun J.-A. Outzen H. Øvervatn A. Bjørkøy G. Johansen T. P62/SQSTM1 Binds Directly to Atg8/LC3 to Facilitate Degradation of Ubiquitinated Protein Aggregates by Autophagy J. Biol. Chem. 2007 282 24131 24145 10.1074/jbc.M702824200 17580304 · DOI · Paper page
  92. [105]Lamark T. Svenning S. Johansen T. Regulation of Selective Autophagy: The P62/SQSTM1 Paradigm Essays Biochem. 2017 61 609 624 10.1042/EBC20170035 29233872 · DOI
  93. [106]Simonsen A. Birkeland H.C.G. Gillooly D.J. Mizushima N. Kuma A. Yoshimori T. Slagsvold T. Brech A. Stenmark H. Alfy, a Novel FYVE-Domain-Containing Protein Associated with Protein Granules and Autophagic Membranes J. Cell Sci. 2004 117 4239 4251 10.1242/jcs.01287 15292400 · DOI
  94. [107]Clausen T.H. Lamark T. Isakson P. Finley K.D. Larsen K.B. Brech A. Øvervatn A. Stenmark H. Bjørkøy G. Simonsen A. P62/SQSTM1 and ALFY Interact to Facilitate the Formation of P62 Bodies/ALIS and Their Degradation by Autophagy Autophagy 2010 6 330 344 10.4161/auto.6.3.11226 20168092 · DOI
  95. [108]Filimonenko M. Isakson P. Finley K.D. Anderson M. Jeong H. Melia T.J. Bartlett B.J. Myers K.M. Birkeland H.C.G. Lamark T. The Selective Macroautophagic Degradation of Aggregated Proteins Requires the PI3P-Binding Protein Alfy Mol. Cell 2010 38 265 279 10.1016/j.molcel.2010.04.007 20417604 PMC2867245 · DOI
  96. [109]Deng Z. Purtell K. Lachance V. Wold M.S. Chen S. Yue Z. Autophagy Receptors and Neurodegenerative Diseases Trends Cell Biol. 2017 27 491 504 10.1016/j.tcb.2017.01.001 28169082 · DOI
  97. [110]Rué L. López-Soop G. Gelpi E. Martínez-Vicente M. Alberch J. Pérez-Navarro E. Brain Region- and Age-Dependent Dysregulation of P62 and NBR1 in a Mouse Model of Huntington’s Disease Neurobiol. Dis. 2013 52 219 228 10.1016/j.nbd.2012.12.008 23295856 · DOI
  98. [111]Wu J.J. Cai A. Greenslade J.E. Higgins N.R. Fan C. Le N.T.T. Tatman M. Whiteley A.M. Prado M.A. Dieriks B.V. ALS/FTD Mutations in UBQLN2 Impede Autophagy by Reducing Autophagosome Acidification through Loss of Function Proc. Natl. Acad. Sci. USA 2020 117 15230 15241 10.1073/pnas.1917371117 32513711 PMC7334651 · DOI · Paper page
  99. [112]Le N.T.T. Chang L. Kovlyagina I. Georgiou P. Safren N. Braunstein K.E. Kvarta M.D. Van Dyke A.M. LeGates T.A. Philips T. Motor Neuron Disease, TDP-43 Pathology, and Memory Deficits in Mice Expressing ALS–FTD-Linked UBQLN2 Mutations Proc. Natl. Acad. Sci. USA 2016 113 E7580 E7589 10.1073/pnas.1608432113 27834214 PMC5127348 · DOI
  100. [113]Jiang W. Chen X. Ji C. Zhang W. Song J. Li J. Wang J. Key Regulators of Autophagosome Closure Cells 2021 10 2814 10.3390/cells10112814 34831036 PMC8616111 · DOI
  101. [114]Sou Y. Waguri S. Iwata J. Ueno T. Fujimura T. Hara T. Sawada N. Yamada A. Mizushima N. Uchiyama Y. The Atg8 Conjugation System Is Indispensable for Proper Development of Autophagic Isolation Membranes in Mice Mol. Biol. Cell 2008 19 4762 4775 10.1091/mbc.e08-03-0309 18768753 PMC2575156 · DOI
  102. [115]Velikkakath A.K.G. Nishimura T. Oita E. Ishihara N. Mizushima N. Mammalian Atg2 Proteins Are Essential for Autophagosome Formation and Important for Regulation of Size and Distribution of Lipid Droplets Mol. Biol. Cell 2012 23 896 909 10.1091/mbc.e11-09-0785 22219374 PMC3290647 · DOI
  103. [116]Bozic M. van den Bekerom L. Milne B.A. Goodman N. Roberston L. Prescott A.R. Macartney T.J. Dawe N. McEwan D.G. A Conserved ATG2-GABARAP Family Interaction Is Critical for Phagophore Formation EMBO Rep. 2020 21 e48412 10.15252/embr.201948412 32009292 PMC7054675 · DOI
  104. [117]Takahashi Y. Liang X. Hattori T. Tang Z. He H. Chen H. Liu X. Abraham T. Imamura-Kawasawa Y. Buchkovich N.J. VPS37A Directs ESCRT Recruitment for Phagophore Closure J. Cell Biol. 2019 218 3336 3354 10.1083/jcb.201902170 31519728 PMC6781443 · DOI
  105. [118]Takahashi Y. He H. Tang Z. Hattori T. Liu Y. Young M.M. Serfass J.M. Chen L. Gebru M. Chen C. An Autophagy Assay Reveals the ESCRT-III Component CHMP2A as a Regulator of Phagophore Closure Nat. Commun. 2018 9 2855 10.1038/s41467-018-05254-w 30030437 PMC6054611 · DOI
  106. [119]Zhou F. Wu Z. Zhao M. Murtazina R. Cai J. Zhang A. Li R. Sun D. Li W. Zhao L. Rab5-Dependent Autophagosome Closure by ESCRT J. Cell Biol. 2019 218 1908 1927 10.1083/jcb.201811173 31010855 PMC6548130 · DOI
  107. [120]Itakura E. Kishi-Itakura C. Mizushima N. The Hairpin-Type Tail-Anchored SNARE Syntaxin 17 Targets to Autophagosomes for Fusion with Endosomes/Lysosomes Cell 2012 151 1256 1269 10.1016/j.cell.2012.11.001 23217709 · DOI
  108. [121]Furuta N. Fujita N. Noda T. Yoshimori T. Amano A. Combinational Soluble N-Ethylmaleimide-Sensitive Factor Attachment Protein Receptor Proteins VAMP8 and Vti1b Mediate Fusion of Antimicrobial and Canonical Autophagosomes with Lysosomes Mol. Biol. Cell 2010 21 1001 1010 10.1091/mbc.e09-08-0693 20089838 PMC2836953 · DOI
  109. [122]Diao J. Liu R. Rong Y. Zhao M. Zhang J. Lai Y. Zhou Q. Wilz L.M. Li J. Vivona S. ATG14 Promotes Membrane Tethering and Fusion of Autophagosomes to Endolysosomes Nature 2015 520 563 566 10.1038/nature14147 25686604 PMC4442024 · DOI
  110. [123]Liu R. Zhi X. Zhong Q. ATG14 Controls SNARE-Mediated Autophagosome Fusion with a Lysosome Autophagy 2015 11 847 849 10.1080/15548627.2015.1037549 25945523 PMC4509447 · DOI
  111. [124]Wang Z. Miao G. Xue X. Guo X. Yuan C. Wang Z. Zhang G. Chen Y. Feng D. Hu J. The Vici Syndrome Protein EPG5 Is a Rab7 Effector That Determines the Fusion Specificity of Autophagosomes with Late Endosomes/Lysosomes Mol. Cell 2016 63 781 795 10.1016/j.molcel.2016.08.021 27588602 · DOI · Paper page
  112. [125]Tian Y. Li Z. Hu W. Ren H. Tian E. Zhao Y. Lu Q. Huang X. Yang P. Li X. C. elegans Screen Identifies Autophagy Genes Specific to Multicellular Organisms Cell 2010 141 1042 1055 10.1016/j.cell.2010.04.034 20550938 · DOI · Paper page
  113. [126]Zhao H. Zhao Y.G. Wang X. Xu L. Miao L. Feng D. Chen Q. Kovács A.L. Fan D. Zhang H. Mice Deficient in Epg5 Exhibit Selective Neuronal Vulnerability to Degeneration J. Cell Biol. 2013 200 731 741 10.1083/jcb.201211014 23479740 PMC3601354 · DOI
  114. [127]Metcalf D. Isaacs A.M. The Role of ESCRT Proteins in Fusion Events Involving Lysosomes, Endosomes and Autophagosomes Biochem. Soc. Trans. 2010 38 1469 1473 10.1042/BST0381469 21118109 · DOI
  115. [128]Colecchia D. Stasi M. Leonardi M. Manganelli F. Nolano M. Veneziani B.M. Santoro L. Eskelinen E.-L. Chiariello M. Bucci C. Alterations of Autophagy in the Peripheral Neuropathy Charcot-Marie-Tooth Type 2B Autophagy 2018 14 930 941 10.1080/15548627.2017.1388475 29130394 PMC6103410 · DOI
  116. [129]Dionisi Vici C. Sabetta G. Gambarara M. Vigevano F. Bertini E. Boldrini R. Parisi S.G. Quinti I. Aiuti F. Fiorilli M. Agenesis of the Corpus Callosum, Combined Immunodeficiency, Bilateral Cataract, and Hypopigmentation in Two Brothers Am. J. Med. Genet. 1988 29 1 8 10.1002/ajmg.1320290102 3344762 · DOI
  117. [130]Maday S. Holzbaur E.L.F. Compartment-Specific Regulation of Autophagy in Primary Neurons J. Neurosci. 2016 36 5933 5945 10.1523/JNEUROSCI.4401-15.2016 27251616 PMC4887563 · DOI · Paper page
  118. [131]Bunge M.B. Fine structure of nerve fibers and growth cones of isolated sympathetic neurons in culture J. Cell Biol. 1973 56 713 735 10.1083/jcb.56.3.713 4347207 PMC2108939 · DOI
  119. [132]Hollenbeck P.J. Products of Endocytosis and Autophagy Are Retrieved from Axons by Regulated Retrograde Organelle Transport J. Cell Biol. 1993 121 305 315 10.1083/jcb.121.2.305 7682217 PMC2200099 · DOI
  120. [133]Maday S. Holzbaur E.L.F. Autophagosome Assembly and Cargo Capture in the Distal Axon Autophagy 2012 8 858 860 10.4161/auto.20055 22617438 PMC3378425 · DOI · Paper page
  121. [134]Matoba K. Kotani T. Tsutsumi A. Tsuji T. Mori T. Noshiro D. Sugita Y. Nomura N. Iwata S. Ohsumi Y. Atg9 Is a Lipid Scramblase That Mediates Autophagosomal Membrane Expansion Nat. Struct. Mol. Biol. 2020 27 1185 1193 10.1038/s41594-020-00518-w 33106658 · DOI · Paper page
  122. [135]Ivankovic D. Drew J. Lesept F. White I.J. López Doménech G. Tooze S.A. Kittler J.T. Axonal Autophagosome Maturation Defect through Failure of ATG9A Sorting Underpins Pathology in AP-4 Deficiency Syndrome Autophagy 2020 16 391 407 10.1080/15548627.2019.1615302 31142229 PMC6999640 · DOI
  123. [136]Yang S. Park D. Manning L. Hill S.E. Cao M. Xuan Z. Gonzalez I. Dong Y. Clark B. Shao L. Presynaptic Autophagy Is Coupled to the Synaptic Vesicle Cycle via ATG-9 Neuron 2022 110 824 840.e10 10.1016/j.neuron.2021.12.031 35065714 PMC9017068 · DOI
  124. [138]Xuan Z. Yang S. Clark B. Hill S.E. Manning L. Colón-Ramos D.A. The Active Zone Protein Clarinet Regulates Synaptic Sorting of ATG-9 and Presynaptic Autophagy PLoS Biol. 2023 21 e3002030 10.1371/journal.pbio.3002030 37053235 PMC10101500 · DOI
  125. [139]Maday S. Holzbaur E.L.F. Autophagosome Biogenesis in Primary Neurons Follows an Ordered and Spatially Regulated Pathway Dev. Cell 2014 30 71 85 10.1016/j.devcel.2014.06.001 25026034 PMC4109719 · DOI · Paper page
  126. [140]Okerlund N.D. Schneider K. Leal-Ortiz S. Montenegro-Venegas C. Kim S.A. Garner L.C. Waites C.L. Gundelfinger E.D. Reimer R.J. Garner C.C. Bassoon Controls Presynaptic Autophagy through Atg5 Neuron 2017 93 897 913.e7 10.1016/j.neuron.2017.01.026 28231469 · DOI
  127. [142]Soukup S.-F. Kuenen S. Vanhauwaert R. Manetsberger J. Hernández-Díaz S. Swerts J. Schoovaerts N. Vilain S. Gounko N.V. Vints K. A LRRK2-Dependent EndophilinA Phosphoswitch Is Critical for Macroautophagy at Presynaptic Terminals Neuron 2016 92 829 844 10.1016/j.neuron.2016.09.037 27720484 · DOI
  128. [143]Murdoch J.D. Rostosky C.M. Gowrisankaran S. Arora A.S. Soukup S.-F. Vidal R. Capece V. Freytag S. Fischer A. Verstreken P. Endophilin-A Deficiency Induces the Foxo3a-Fbxo32 Network in the Brain and Causes Dysregulation of Autophagy and the Ubiquitin-Proteasome System Cell Rep. 2016 17 1071 1086 10.1016/j.celrep.2016.09.058 27720640 PMC5080600 · DOI
  129. [144]Vanhauwaert R. Kuenen S. Masius R. Bademosi A. Manetsberger J. Schoovaerts N. Bounti L. Gontcharenko S. Swerts J. Vilain S. The SAC1 Domain in Synaptojanin Is Required for Autophagosome Maturation at Presynaptic Terminals EMBO J. 2017 36 1392 1411 10.15252/embj.201695773 28331029 PMC5430236 · DOI
  130. [145]Zimprich A. Biskup S. Leitner P. Lichtner P. Farrer M. Lincoln S. Kachergus J. Hulihan M. Uitti R.J. Calne D.B. Mutations in LRRK2 Cause Autosomal-Dominant Parkinsonism with Pleomorphic Pathology Neuron 2004 44 601 607 10.1016/j.neuron.2004.11.005 15541309 · DOI
  131. [146]Matta S. Van Kolen K. da Cunha R. van den Bogaart G. Mandemakers W. Miskiewicz K. De Bock P.-J. Morais V.A. Vilain S. Haddad D. LRRK2 Controls an EndoA Phosphorylation Cycle in Synaptic Endocytosis Neuron 2012 75 1008 1021 10.1016/j.neuron.2012.08.022 22998870 · DOI
  132. [147]Bademosi A.T. Decet M. Kuenen S. Calatayud C. Swerts J. Gallego S.F. Schoovaerts N. Karamanou S. Louros N. Martin E. EndophilinA-Dependent Coupling between Activity-Induced Calcium Influx and Synaptic Autophagy Is Disrupted by a Parkinson-Risk Mutation Neuron 2023 111 1402 1422.e13 10.1016/j.neuron.2023.02.001 36827984 PMC10166451 · DOI
  133. [148]Decet M. Soukup S.-F. Endophilin-A/SH3GL2 Calcium Switch for Synaptic Autophagy Induction Is Impaired by a Parkinson’s Risk Variant Autophagy 2023 1 3 online ahead of print 10.1080/15548627.2023.2200627 PMC11062392 37067454 · DOI
  134. [150]Lee S. Sato Y. Nixon R.A. Lysosomal Proteolysis Inhibition Selectively Disrupts Axonal Transport of Degradative Organelles and Causes an Alzheimer’s-Like Axonal Dystrophy J. Neurosci. 2011 31 7817 7830 10.1523/JNEUROSCI.6412-10.2011 21613495 PMC3351137 · DOI
  135. [151]Cheng X.-T. Zhou B. Lin M.-Y. Cai Q. Sheng Z.-H. Axonal Autophagosomes Recruit Dynein for Retrograde Transport through Fusion with Late Endosomes J. Cell Biol. 2015 209 377 386 10.1083/jcb.201412046 25940348 PMC4427784 · DOI
  136. [152]Calderilla-Barbosa L. Seibenhener M.L. Du Y. Diaz-Meco M.-T. Moscat J. Yan J. Wooten M.W. Wooten M.C. Interaction of SQSTM1 with the Motor Protein Dynein: SQSTM1 Is Required for Normal Dynein Function and Trafficking J. Cell Sci. 2014 127 4052 4063 10.1242/jcs.152363 25015291 PMC4163647 · DOI
  137. [153]Zhang L. Fang Y. Cheng X. Lian Y. Xu H. Interaction between TRPML1 and P62 in Regulating Autophagosome-Lysosome Fusion and Impeding Neuroaxonal Dystrophy in Alzheimer’s Disease Oxid. Med. Cell. Longev. 2022 2022 8096009 10.1155/2022/8096009 35116093 PMC8807035 · DOI
  138. [154]Overly C.C. Lee K.D. Berthiaume E. Hollenbeck P.J. Quantitative Measurement of Intraorganelle pH in the Endosomal-Lysosomal Pathway in Neurons by Using Ratiometric Imaging with Pyranine Proc. Natl. Acad. Sci. USA 1995 92 3156 3160 10.1073/pnas.92.8.3156 7724533 PMC42124 · DOI
  139. [155]Aplin A. Jasionowski T. Tuttle D.L. Lenk S.E. Dunn W.A. Cytoskeletal Elements Are Required for the Formation and Maturation of Autophagic Vacuoles J. Cell. Physiol. 1992 152 458 466 10.1002/jcp.1041520304 1506410 · DOI
  140. [156]Köchl R. Hu X.W. Chan E.Y.W. Tooze S.A. Microtubules Facilitate Autophagosome Formation and Fusion of Autophagosomes with Endosomes Traffic 2006 7 129 145 10.1111/j.1600-0854.2005.00368.x 16420522 · DOI
  141. [157]Fu M. Nirschl J.J. Holzbaur E.L.F. LC3 Binding to the Scaffolding Protein JIP1 Regulates Processive Dynein-Driven Transport of Autophagosomes Dev. Cell 2014 29 577 590 10.1016/j.devcel.2014.04.015 24914561 PMC4109720 · DOI
  142. [158]Wong Y.C. Holzbaur E.L.F. The Regulation of Autophagosome Dynamics by Huntingtin and HAP1 Is Disrupted by Expression of Mutant Huntingtin, Leading to Defective Cargo Degradation J. Neurosci. 2014 34 1293 1305 10.1523/JNEUROSCI.1870-13.2014 24453320 PMC3898289 · DOI
  143. [159]Cason S.E. Carman P.J. Van Duyne C. Goldsmith J. Dominguez R. Holzbaur E.L.F. Sequential Dynein Effectors Regulate Axonal Autophagosome Motility in a Maturation-Dependent Pathway J. Cell Biol. 2021 220 e202010179 10.1083/jcb.202010179 34014261 PMC8142281 · DOI
  144. [160]Nieto-Torres J.L. Shanahan S.-L. Chassefeyre R. Chaiamarit T. Zaretski S. Landeras-Bueno S. Verhelle A. Encalada S.E. Hansen M. LC3B Phosphorylation Regulates FYCO1 Binding and Directional Transport of Autophagosomes Curr. Biol. CB 2021 31 3440 3449.e7 10.1016/j.cub.2021.05.052 34146484 PMC8439105 · DOI
  145. [161]Pankiv S. Alemu E.A. Brech A. Bruun J.-A. Lamark T. Øvervatn A. Bjørkøy G. Johansen T. FYCO1 Is a Rab7 Effector That Binds to LC3 and PI3P to Mediate Microtubule plus End–Directed Vesicle Transport J. Cell Biol. 2010 188 253 269 10.1083/jcb.200907015 20100911 PMC2812517 · DOI
  146. [162]Jordens I. Fernandez-Borja M. Marsman M. Dusseljee S. Janssen L. Calafat J. Janssen H. Wubbolts R. Neefjes J. The Rab7 Effector Protein RILP Controls Lysosomal Transport by Inducing the Recruitment of Dynein-Dynactin Motors Curr. Biol. 2001 11 1680 1685 10.1016/S0960-9822(01)00531-0 11696325 · DOI · Paper page
  147. [163]Wijdeven R.H. Janssen H. Nahidiazar L. Janssen L. Jalink K. Berlin I. Neefjes J. Cholesterol and ORP1L-Mediated ER Contact Sites Control Autophagosome Transport and Fusion with the Endocytic Pathway Nat. Commun. 2016 7 11808 10.1038/ncomms11808 27283760 PMC4906411 · DOI
  148. [164]Fu M. Holzbaur E.L.F. JIP1 Regulates the Directionality of APP Axonal Transport by Coordinating Kinesin and Dynein Motors J. Cell Biol. 2013 202 495 508 10.1083/jcb.201302078 23897889 PMC3734084 · DOI
  149. [165]Fu M. Holzbaur E.L.F. MAPK8IP1/JIP1 Regulates the Trafficking of Autophagosomes in Neurons Autophagy 2014 10 2079 2081 10.4161/auto.34451 25483967 PMC4502678 · DOI
  150. [166]Brown H.M. Van Epps H.A. Goncharov A. Grant B.D. Jin Y. The JIP3 Scaffold Protein UNC-16 Regulates RAB-5 Dependent Membrane Trafficking at C. elegans Synapses Dev. Neurobiol. 2009 69 174 190 10.1002/dneu.20690 19105215 PMC2707823 · DOI
  151. [167]Drerup C.M. Nechiporuk A.V. JNK-Interacting Protein 3 Mediates the Retrograde Transport of Activated c-Jun N-Terminal Kinase and Lysosomes PLoS Genet. 2013 9 e1003303 10.1371/journal.pgen.1003303 23468645 PMC3585007 · DOI
  152. [168]Gowrishankar S. Wu Y. Ferguson S.M. Impaired JIP3-Dependent Axonal Lysosome Transport Promotes Amyloid Plaque Pathology J. Cell Biol. 2017 216 3291 3305 10.1083/jcb.201612148 28784610 PMC5626538 · DOI
  153. [169]Hill S.E. Kauffman K.J. Krout M. Richmond J.E. Melia T.J. Colón-Ramos D.A. Maturation and Clearance of Autophagosomes in Neurons Depends on a Specific Cysteine Protease Isoform, ATG-4.2 Dev. Cell 2019 49 251 266.e8 10.1016/j.devcel.2019.02.013 30880001 PMC6482087 · DOI
  154. [170]Li T. Lu D. Yao C. Li T. Dong H. Li Z. Xu G. Chen J. Zhang H. Yi X. Kansl1 Haploinsufficiency Impairs Autophagosome-Lysosome Fusion and Links Autophagic Dysfunction with Koolen-de Vries Syndrome in Mice Nat. Commun. 2022 13 931 10.1038/s41467-022-28613-0 35177641 PMC8854428 · DOI
  155. [171]Linda K. Lewerissa E.I. Verboven A.H.A. Gabriele M. Frega M. Klein Gunnewiek T.M. Devilee L. Ulferts E. Hommersom M. Oudakker A. Imbalanced Autophagy Causes Synaptic Deficits in a Human Model for Neurodevelopmental Disorders Autophagy 2022 18 423 442 10.1080/15548627.2021.1936777 34286667 PMC8942553 · DOI
  156. [172]Nixon R.A. Wegiel J. Kumar A. Yu W.H. Peterhoff C. Cataldo A. Cuervo A.M. Extensive Involvement of Autophagy in Alzheimer Disease: An Immuno-Electron Microscopy Study J. Neuropathol. Exp. Neurol. 2005 64 10 10.1093/jnen/64.2.113 15751225 · DOI · Paper page
  157. [173]Tammineni P. Ye X. Feng T. Aikal D. Cai Q. Impaired Retrograde Transport of Axonal Autophagosomes Contributes to Autophagic Stress in Alzheimer’s Disease Neurons eLife 2017 6 e21776 10.7554/eLife.21776 28085665 PMC5235353 · DOI
  158. [174]Hafezparast M. Klocke R. Ruhrberg C. Marquardt A. Ahmad-Annuar A. Bowen S. Lalli G. Witherden A.S. Hummerich H. Nicholson S. Mutations in Dynein Link Motor Neuron Degeneration to Defects in Retrograde Transport Science 2003 300 808 812 10.1126/science.1083129 12730604 · DOI
  159. [175]Ravikumar B. Acevedo-Arozena A. Imarisio S. Berger Z. Vacher C. O’Kane C.J. Brown S.D.M. Rubinsztein D.C. Dynein Mutations Impair Autophagic Clearance of Aggregate-Prone Proteins Nat. Genet. 2005 37 771 776 10.1038/ng1591 15980862 · DOI
  160. [176]Li D. Shi J.-J. Mao C.-J. Liu S. Wang J.-D. Chen J. Wang F. Yang Y.-P. Hu W.-D. Hu L.-F. Alteration of Dynein Function Affects α-Synuclein Degradation via the Autophagosome-Lysosome Pathway Int. J. Mol. Sci. 2013 14 24242 24254 10.3390/ijms141224242 24351814 PMC3876108 · DOI
  161. [177]Poirier K. Lebrun N. Broix L. Tian G. Saillour Y. Boscheron C. Parrini E. Valence S. SaintPierre B. Oger M. Mutations in TUBG1, DYNC1H1, KIF5C and KIF2A Cause Malformations of Cortical Development and Microcephaly Nat. Genet. 2013 45 639 647 10.1038/ng.2613 23603762 PMC3826256 · DOI
  162. [178]Harms M.B. Ori-McKenney K.M. Scoto M. Tuck E.P. Bell S. Ma D. Masi S. Allred P. Al-Lozi M. Reilly M.M. Mutations in the Tail Domain of DYNC1H1 Cause Dominant Spinal Muscular Atrophy Neurology 2012 78 1714 1720 10.1212/WNL.0b013e3182556c05 22459677 PMC3359582 · DOI
  163. [179]Weedon M.N. Hastings R. Caswell R. Xie W. Paszkiewicz K. Antoniadi T. Williams M. King C. Greenhalgh L. Newbury-Ecob R. Exome Sequencing Identifies a DYNC1H1 Mutation in a Large Pedigree with Dominant Axonal Charcot-Marie-Tooth Disease Am. J. Hum. Genet. 2011 89 308 312 10.1016/j.ajhg.2011.07.002 21820100 PMC3155164 · DOI
  164. [180]Boecker C.A. Goldsmith J. Dou D. Cajka G.G. Holzbaur E.L.F. Increased LRRK2 Kinase Activity Alters Neuronal Autophagy by Disrupting the Axonal Transport of Autophagosomes Curr. Biol. 2021 31 2140 2154.e6 10.1016/j.cub.2021.02.061 33765413 PMC8154747 · DOI
  165. [181]Dou D. Smith E.M. Evans C.S. Boecker C.A. Holzbaur E.L.F. Regulatory Imbalance between LRRK2 Kinase, PPM1H Phosphatase, and ARF6 GTPase Disrupts the Axonal Transport of Autophagosomes Cell Rep. 2023 42 112448 10.1016/j.celrep.2023.112448 37133994 PMC10304398 · DOI
  166. [182]Sleigh J.N. Rossor A.M. Fellows A.D. Tosolini A.P. Schiavo G. Axonal Transport and Neurological Disease Nat. Rev. Neurol. 2019 15 691 703 10.1038/s41582-019-0257-2 31558780 · DOI
  167. [183]Perlson E. Maday S. Fu M. Moughamian A.J. Holzbaur E.L.F. Retrograde Axonal Transport: Pathways To Cell Death? Trends Neurosci. 2010 33 335 344 10.1016/j.tins.2010.03.006 20434225 PMC2902719 · DOI
  168. [184]Almeida-Souza L. Asselbergh B. d’Ydewalle C. Moonens K. Goethals S. de Winter V. Azmi A. Irobi J. Timmermans J.-P. Gevaert K. Small Heat-Shock Protein HSPB1 Mutants Stabilize Microtubules in Charcot-Marie-Tooth Neuropathy J. Neurosci. Off. J. Soc. Neurosci. 2011 31 15320 15328 10.1523/JNEUROSCI.3266-11.2011 PMC6703512 22031878 · DOI
  169. [185]Zhang X. Qiao Y. Han R. Gao Y. Yang X. Zhang Y. Wan Y. Yu W. Pan X. Xing J. A Charcot-Marie-Tooth-Causing Mutation in HSPB1 Decreases Cell Adaptation to Repeated Stress by Disrupting Autophagic Clearance of Misfolded Proteins Cells 2022 11 2886 10.3390/cells11182886 36139461 PMC9496658 · DOI
  170. [186]Haidar M. Asselbergh B. Adriaenssens E. De Winter V. Timmermans J.-P. Auer-Grumbach M. Juneja M. Timmerman V. Neuropathy-Causing Mutations in HSPB1 Impair Autophagy by Disturbing the Formation of SQSTM1/P62 Bodies Autophagy 2019 15 1051 1068 10.1080/15548627.2019.1569930 30669930 PMC6526868 · DOI
  171. [187]Gowrishankar S. Yuan P. Wu Y. Schrag M. Paradise S. Grutzendler J. De Camilli P. Ferguson S.M. Massive Accumulation of Luminal Protease-Deficient Axonal Lysosomes at Alzheimer’s Disease Amyloid Plaques Proc. Natl. Acad. Sci. USA 2015 112 E3699 E3708 10.1073/pnas.1510329112 26124111 PMC4507205 · DOI · Paper page
  172. [188]Farfel-Becker T. Roney J.C. Cheng X.-T. Li S. Cuddy S.R. Sheng Z.-H. Neuronal Soma-Derived Degradative Lysosomes Are Continuously Delivered to Distal Axons to Maintain Local Degradation Capacity Cell Rep. 2019 28 51 64.e4 10.1016/j.celrep.2019.06.013 31269450 PMC6696943 · DOI · Paper page
  173. [189]Özkan N. Koppers M. van Soest I. van Harten A. Jurriens D. Liv N. Klumperman J. Kapitein L.C. Hoogenraad C.C. Farías G.G. ER—Lysosome Contacts at a Pre-Axonal Region Regulate Axonal Lysosome Availability Nat. Commun. 2021 12 4493 10.1038/s41467-021-24713-5 34301956 PMC8302662 · DOI
  174. [190]Cheng X.-T. Xie Y.-X. Zhou B. Huang N. Farfel-Becker T. Sheng Z.-H. Characterization of LAMP1-Labeled Nondegradative Lysosomal and Endocytic Compartments in Neurons J. Cell Biol. 2018 217 3127 3139 10.1083/jcb.201711083 29695488 PMC6123004 · DOI
  175. [191]Bomont P. Cavalier L. Blondeau F. Hamida C.B. Belal S. Tazir M. Demir E. Topaloglu H. Korinthenberg R. Tüysüz B. The Gene Encoding Gigaxonin, a New Member of the Cytoskeletal BTB/Kelch Repeat Family, Is Mutated in Giant Axonal Neuropathy Nat. Genet. 2000 26 370 374 10.1038/81701 11062483 · DOI
  176. [192]Scrivo A. Codogno P. Bomont P. Gigaxonin E3 Ligase Governs ATG16L1 Turnover to Control Autophagosome Production Nat. Commun. 2019 10 780 10.1038/s41467-019-08331-w 30770803 PMC6377711 · DOI
  177. [193]Cai Q. Zakaria H.M. Simone A. Sheng Z.-H. Spatial Parkin Translocation and Degradation of Damaged Mitochondria via Mitophagy in Live Cortical Neurons Curr. Biol. 2012 22 545 552 10.1016/j.cub.2012.02.005 22342752 PMC3313683 · DOI
  178. [194]Zheng Y. Zhang X. Wu X. Jiang L. Ahsan A. Ma S. Xiao Z. Han F. Qin Z.-H. Hu W. Somatic Autophagy of Axonal Mitochondria in Ischemic Neurons J. Cell Biol. 2019 218 1891 1907 10.1083/jcb.201804101 30979799 PMC6548140 · DOI
  179. [195]Shehata M. Matsumura H. Okubo-Suzuki R. Ohkawa N. Inokuchi K. Neuronal Stimulation Induces Autophagy in Hippocampal Neurons That Is Involved in AMPA Receptor Degradation after Chemical Long-Term Depression J. Neurosci. 2012 32 10413 10422 10.1523/JNEUROSCI.4533-11.2012 22836274 PMC6703735 · DOI · Paper page
  180. [196]Kallergi E. Daskalaki A.-D. Kolaxi A. Camus C. Ioannou E. Mercaldo V. Haberkant P. Stein F. Sidiropoulou K. Dalezios Y. Dendritic Autophagy Degrades Postsynaptic Proteins and Is Required for Long-Term Synaptic Depression in Mice Nat. Commun. 2022 13 680 10.1038/s41467-022-28301-z 35115539 PMC8814153 · DOI
  181. [197]Baas P.W. Black M.M. Banker G.A. Changes in Microtubule Polarity Orientation during the Development of Hippocampal Neurons in Culture J. Cell Biol. 1989 109 3085 3094 10.1083/jcb.109.6.3085 2592416 PMC2115969 · DOI
  182. [198]Kulkarni V.V. Anand A. Herr J.B. Miranda C. Vogel M.C. Maday S. Synaptic Activity Controls Autophagic Vacuole Motility and Function in Dendrites J. Cell Biol. 2021 220 e202002084 10.1083/jcb.202002084 33783472 PMC8020715 · DOI
  183. [199]Goo M.S. Sancho L. Slepak N. Boassa D. Deerinck T.J. Ellisman M.H. Bloodgood B.L. Patrick G.N. Activity-Dependent Trafficking of Lysosomes in Dendrites and Dendritic Spines J. Cell Biol. 2017 216 2499 2513 10.1083/jcb.201704068 28630145 PMC5551717 · DOI · Paper page
  184. [200]Yap C.C. Digilio L. McMahon L.P. Garcia A.D.R. Winckler B. Degradation of Dendritic Cargos Requires Rab7-Dependent Transport to Somatic Lysosomes J. Cell Biol. 2018 217 3141 3159 10.1083/jcb.201711039 29907658 PMC6122995 · DOI
  185. [201]Giehl K.M. Neuronal Development Prog. Exp. Tumor Res. 2007 39 1 29 10.1159/000100041 17314498 · DOI
  186. [202]Molnár Z. Clowry G.J. Šestan N. Alzu’bi A. Bakken T. Hevner R.F. Hüppi P.S. Kostović I. Rakic P. Anton E.S. New Insights into the Development of the Human Cerebral Cortex J. Anat. 2019 235 432 451 10.1111/joa.13055 31373394 PMC6704245 · DOI
  187. [204]Wu X. Fleming A. Ricketts T. Pavel M. Virgin H. Menzies F.M. Rubinsztein D.C. Autophagy Regulates Notch Degradation and Modulates Stem Cell Development and Neurogenesis Nat. Commun. 2016 7 10533 10.1038/ncomms10533 26837467 PMC4742842 · DOI
  188. [205]Li M. Lu G. Hu J. Shen X. Ju J. Gao Y. Qu L. Xia Y. Chen Y. Bai Y. EVA1A/TMEM166 Regulates Embryonic Neurogenesis by Autophagy Stem Cell Rep. 2016 6 396 410 10.1016/j.stemcr.2016.01.011 26905199 PMC4788774 · DOI
  189. [206]Le Duc D. Giulivi C. Hiatt S.M. Napoli E. Panoutsopoulos A. Harlan De Crescenzo A. Kotzaeridou U. Syrbe S. Anagnostou E. Azage M. Pathogenic WDFY3 Variants Cause Neurodevelopmental Disorders and Opposing Effects on Brain Size Brain 2019 142 2617 2630 10.1093/brain/awz198 31327001 PMC6736092 · DOI
  190. [208]Jacquemont M. Sanlaville D. Redon R. Raoul O. Cormier-Daire V. Lyonnet S. Amiel J. Merrer M.L. Heron D. de Blois M. Array-based Comparative Genomic Hybridisation Identifies High Frequency of Cryptic Chromosomal Rearrangements in Patients with Syndromic Autism Spectrum Disorders J. Med. Genet. 2006 43 843 849 10.1136/jmg.2006.043166 16840569 PMC2563185 · DOI · Paper page
  191. [209]Iossifov I. Ronemus M. Levy D. Wang Z. Hakker I. Rosenbaum J. Yamrom B. Lee Y. Narzisi G. Leotta A. De Novo Gene Disruptions in Children on the Autistic Spectrum Neuron 2012 74 285 299 10.1016/j.neuron.2012.04.009 22542183 PMC3619976 · DOI · Paper page
  192. [211]Yazdankhah M. Farioli-Vecchioli S. Tonchev A.B. Stoykova A. Cecconi F. The Autophagy Regulators Ambra1 and Beclin 1 Are Required for Adult Neurogenesis in the Brain Subventricular Zone Cell Death Dis. 2014 5 e1403 10.1038/cddis.2014.358 25188513 PMC4540193 · DOI
  193. [213]Wang C. Yeo S. Haas M.A. Guan J.-L. Autophagy Gene FIP200 in Neural Progenitors Non-Cell Autonomously Controls Differentiation by Regulating Microglia J. Cell Biol. 2017 216 2581 2596 10.1083/jcb.201609093 28634261 PMC5551701 · DOI
  194. [214]Lv X. Jiang H. Li B. Liang Q. Wang S. Zhao Q. Jiao J. The Crucial Role of Atg5 in Cortical Neurogenesis During Early Brain Development Sci. Rep. 2014 4 6010 10.1038/srep06010 25109817 PMC4127499 · DOI
  195. [215]Kenific C.M. Stehbens S.J. Goldsmith J. Leidal A.M. Faure N. Ye J. Wittmann T. Debnath J. NBR1 Enables Autophagy-Dependent Focal Adhesion Turnover J. Cell Biol. 2016 212 577 590 10.1083/jcb.201503075 26903539 PMC4772495 · DOI
  196. [216]Sharifi M.N. Mowers E.E. Drake L.E. Collier C. Chen H. Zamora M. Mui S. Macleod K.F. Autophagy Promotes Focal Adhesion Disassembly and Cell Motility of Metastatic Tumor Cells through the Direct Interaction of Paxillin with LC3 Cell Rep. 2016 15 1660 1672 10.1016/j.celrep.2016.04.065 27184837 PMC4880529 · DOI
  197. [217]Bressan C. Pecora A. Gagnon D. Snapyan M. Labrecque S. De Koninck P. Parent M. Saghatelyan A. The Dynamic Interplay between ATP/ADP Levels and Autophagy Sustain Neuronal Migration in Vivo eLife 2020 9 e56006 10.7554/eLife.56006 32985978 PMC7556871 · DOI
  198. [218]Molnár M. Sőth Á. Simon-Vecsei Z. Pathways of Integrins in the Endo-Lysosomal System Biol. Futura 2022 73 171 185 10.1007/s42977-022-00120-9 35501574 · DOI
  199. [219]Peng C. Ye J. Yan S. Kong S. Shen Y. Li C. Li Q. Zheng Y. Deng K. Xu T. Ablation of Vacuole Protein Sorting 18 (Vps18) Gene Leads to Neurodegeneration and Impaired Neuronal Migration by Disrupting Multiple Vesicle Transport Pathways to Lysosomes J. Biol. Chem. 2012 287 32861 32873 10.1074/jbc.M112.384305 22854957 PMC3463306 · DOI
  200. [220]Petri R. Pircs K. Jönsson M.E. Åkerblom M. Brattås P.L. Klussendorf T. Jakobsson J. Let-7 Regulates Radial Migration of New-born Neurons through Positive Regulation of Autophagy EMBO J. 2017 36 1379 1391 10.15252/embj.201695235 28336683 PMC5430214 · DOI

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Authors
Liénard, C., Pintart, A., & Bomont, P.
Affiliations
Lyon 1 Université (FR)
Corresponding author
Bomont, Pascale
ORCID
Venue
Cells
Publisher
MDPI AG
Published
2024-01-04
Volume
13
Issue
1
Pages
103
ISSN
2073-4409 (ISSN-L)
DOI
10.3390/cells13010103
PMC
PMC10778363
OpenAlex
W4390587267
Cited by
44
References
22
Citations by year
2026: 10 · 2025: 25 · 2024: 9
FWCI
2.68
Type
journal article
Language
en
Open access
Licence
Locations
  • Cells (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • HAL (submittedVersion, cc-by)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • Institut National de la Santé et de la Recherche Médicale (INSERM)
  • Centre Hospitalo-Universitaire de Montpellier
Topics
  • Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
Keywords
neuronal autophagy, macroautophagy, autophagosome formation, lysosomal degradation, neurodevelopmental disorders, neurodegenerative diseases, axonal transport, synaptic activity, axons, brain development, autophagy regulation
MeSH terms
Autophagosomes, Macroautophagy, Autophagy, Axonal Transport, Lysosomes

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