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<article xsi:noNamespaceSchemaLocation="http://jats.nlm.nih.gov/publishing/1.1/xsd/JATS-journalpublishing1-mathml3.xsd" dtd-version="1.1" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance"><front><journal-meta><journal-id journal-id-type="publisher-id">JCNR</journal-id><journal-title-group><journal-title>Journal of Clinical and Nursing Research</journal-title></journal-title-group><issn>2208-3685</issn><eissn>2208-3693</eissn><publisher><publisher-name>Bio-Byword Scientific Publishing Pty. Ltd.</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="doi">10.26689/jcnr.v9i7.11445</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title>Research Advances in Mitophagy in Hepatic Ischemia-Reperfusion Injury</title><url>https://artdesignp.com/journal/JCNR/9/7/10.26689/jcnr.v9i7.11445</url><author>YangErhua,YangZhimeng,ZhaoDejiang,WangXuefeng</author><pub-date pub-type="publication-year"><year>2025</year></pub-date><volume>9</volume><issue>7</issue><history><date date-type="pub"><published-time>2025-08-04</published-time></date></history><abstract>Hepatic ischemia-reperfusion injury (IRI) is a prevalent pathophysiological phenomenon encountered during liver surgeries and transplantation, leading to hepatocyte damage and liver dysfunction, which significantly affects patient prognosis. In recent years, the role of mitophagy in hepatic IRI has garnered considerable attention. Mitochondria, known as the "powerhouses" of the cell, are crucial for maintaining normal cellular physiological functions. During the ischemia-reperfusion process, mitochondria are susceptible to damage, generating excessive harmful substances, such as reactive oxygen species (ROS), which further exacerbate cellular injury. Mitophagy is a selective cellular self-protection mechanism that maintains the quality and quantity balance of mitochondria within cells by clearing damaged or dysfunctional mitochondria. In the context of liver IRI, the activation of mitophagy is of significant importance. On one hand, mitophagy can rapidly remove damaged mitochondria, thereby reducing the release of harmful products and alleviating oxidative stress and cellular damage. Research has indicated that under ischemia-reperfusion conditions, mitophagy-related pathways are activated, promoting the clearance of damaged mitochondria. On the other hand, mitophagy also regulates cellular energy metabolism, providing essential energy support for cells under stress. With the continuous advancement of research, the understanding of the role of mitophagy in hepatic IRI has become increasingly clear. Numerous studies are dedicated to exploring the specific molecular mechanisms of mitophagy and its regulation, aiming to develop new therapeutic strategies to alleviate hepatic IRI. Although studies have demonstrated that mitophagy has a protective effect in hepatic ischemia-reperfusion injury, many issues still require further investigation. First, it is essential to further elucidate the mechanisms underlying the role of mitophagy in ischemia-reperfusion. Additionally, understanding how to mitigate liver ischemia-reperfusion injury through the modulation of mitophagy represents a key focus for future research. Future studies may encompass drug development, gene therapy, and cell therapy approaches aimed at improving the prognosis of patients affected by liver ischemia-reperfusion.</abstract><keywords/></article-meta></front><body/><back><ref-list><ref id="B1" content-type="article"><label>1</label><element-citation publication-type="journal"><p>Battaglioni S, Benjamin D, Wälchli M, et al., 2022, mTOR Substrate Phosphorylation in Growth Control. Cell, 185(11): 1814–1836.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B2" content-type="article"><label>2</label><element-citation publication-type="journal"><p>Wullschleger S, Loewith R, Hall MN, 2006, TOR Signaling in Growth and Metabolism. Cell, 124(3): 471–484.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B3" content-type="article"><label>3</label><element-citation publication-type="journal"><p>Szwed A, Kim E, Jacinto E, 2021, Regulation and Metabolic Functions of mTORC1 and mTORC2. Physiol Rev, 101(1): 137–192.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B4" content-type="article"><label>4</label><element-citation publication-type="journal"><p>Mossmann D, Park S, Hall MN, 2018, mTOR Signalling and Cellular Metabolism Are Mutual Determinants in Cancer. Nat Rev Cancer, 18(12): 744–757.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B5" content-type="article"><label>5</label><element-citation publication-type="journal"><p>Paquette M, El-Houjeiri L, Pause A, 2018, mTOR Pathways in Cancer and Autophagy. Cancers, 10(1): 18.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B6" content-type="article"><label>6</label><element-citation publication-type="journal"><p>Murugan AK, 2019, mTOR: Role in Cancer, Metastasis and Drug Resistance. Semin Cancer Biol, 59: 92–111.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B7" content-type="article"><label>7</label><element-citation publication-type="journal"><p>Ben-Sahra I, Manning BD, 2017, mTORC1 Signaling and the Metabolic Control of Cell Growth. Curr Opin Cell Biol, 45: 72–82.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B8" content-type="article"><label>8</label><element-citation publication-type="journal"><p>Saxton RA, Sabatini DM, 2017, mTOR Signaling in Growth, Metabolism, and Disease. Cell, 168(6): 960–976.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B9" content-type="article"><label>9</label><element-citation publication-type="journal"><p>Shimobayashi M, Hall MN, 2014, Making New Contacts: The mTOR Network in Metabolism and Signalling Crosstalk. Nat Rev Mol Cell Biol, 15(3): 155–162.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B10" content-type="article"><label>10</label><element-citation publication-type="journal"><p>Jiang X, Overholtzer M, Thompson CB, 2015, Autophagy in Cellular Metabolism and Cancer. J Clin Invest, 125(1): 47–54.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B11" content-type="article"><label>11</label><element-citation publication-type="journal"><p>Li X, He S, Ma B, 2022, Autophagy and Autophagy-Related Proteins in Cancer. Mol Cancer, 21(1): 1–29.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B12" content-type="article"><label>12</label><element-citation publication-type="journal"><p>White E, Mehnert JM, Chan CS, 2015, Autophagy, Metabolism, and Cancer. Clin Cancer Res, 21(22): 5037–5046.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B13" content-type="article"><label>13</label><element-citation publication-type="journal"><p>Yang A, Herter-Sprie GS, Zhang H, et al., 2018, Autophagy Sustains Pancreatic Cancer Growth Through Both Cell-Autonomous and Non-Autonomous Mechanisms. Cancer Discov, 8(3): 276–287.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B14" content-type="article"><label>14</label><element-citation publication-type="journal"><p>Pópulo H, Lopes JM, Soares P, 2012, The mTOR Signalling Pathway in Human Cancer. Int J Mol Sci, 13(2): 1886–1918.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B15" content-type="article"><label>15</label><element-citation publication-type="journal"><p>Ravikumar B, Sarkar S, Davies JE, et al., 2010, Regulation of Mammalian Autophagy in Physiology and Pathophysiology. Physiol Rev, 90(4): 1383–1435.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B16" content-type="article"><label>16</label><element-citation publication-type="journal"><p>Jiang GM, Tan YZ, Wang H, et al., 2019, The Relationship Between Autophagy and the Immune System and Its Applications for Tumor Immunotherapy. Mol Cancer, 18(1): 1–17.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B17" content-type="article"><label>17</label><element-citation publication-type="journal"><p>Palm W, Thompson CB, 2017, Nutrient Acquisition Strategies of Mammalian Cells. Nature, 546(7657): 234–242.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B18" content-type="article"><label>18</label><element-citation publication-type="journal"><p>Saxton RA, Sabatini DM, 2017, mTOR Signaling in Growth, Metabolism, and Disease. Cell, 168(6): 960–976.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B19" content-type="article"><label>19</label><element-citation publication-type="journal"><p>Xie Y, Zhou L, Xie Y, et al., 2020, mTOR Signaling Pathway in Cancer and Autophagy. Int J Mol Sci, 21(21): 7594.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B20" content-type="article"><label>20</label><element-citation publication-type="journal"><p>Wei Y, Liu M, Li X, et al., 2020, Origin of the Autophagosome Membrane in Mammals. Biomed Pharmacother, 128: 110245.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B21" content-type="article"><label>21</label><element-citation publication-type="journal"><p>Mercer TJ, Gubas A, Tooze SA, 2018, A Molecular Perspective of Mammalian Autophagosome Biogenesis. J Biol Chem, 293(15): 5386–5395.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B22" content-type="article"><label>22</label><element-citation publication-type="journal"><p>Feng Y, He D, Yao Z, et al., 2014, The Machinery of Macroautophagy. Cell Res, 24(1): 24–41.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B23" content-type="article"><label>23</label><element-citation publication-type="journal"><p>Parzych KR, Klionsky DJ, 2014, An Overview of Autophagy: Morphology, Mechanism, and Regulation. Antioxid Redox Signal, 20(3): 460–473.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B24" content-type="article"><label>24</label><element-citation publication-type="journal"><p>Dikic I, Elazar Z, 2018, Mechanism and Medical Implications of Mammalian Autophagy. Nat Rev Mol Cell Biol, 19(6): 349–364.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B25" content-type="article"><label>25</label><element-citation publication-type="journal"><p>Kim J, Kundu M, Viollet B, et al., 2011, AMPK and mTOR Regulate Autophagy Through Direct Phosphorylation of Ulk1. Nat Cell Biol, 13(2): 132–141.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B26" content-type="article"><label>26</label><element-citation publication-type="journal"><p>Alers S, Löffler AS, Wesselborg S, et al., 2012, Role of AMPK–mTOR–Ulk1/2 in the Regulation of Autophagy: Cross Talk, Shortcuts, and Feedbacks. Mol Cell Biol, 32(1): 2–11.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B27" content-type="article"><label>27</label><element-citation publication-type="journal"><p>Hurley JH, Young LN, 2017, Mechanisms of Autophagy Initiation. Annu Rev Biochem, 86: 225–244.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B28" content-type="article"><label>28</label><element-citation publication-type="journal"><p>Mizushima N, 2010, The Role of the Atg1/ULK1 Complex in Autophagy Regulation. Curr Opin Cell Biol, 22(2): 132–139.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B29" content-type="article"><label>29</label><element-citation publication-type="journal"><p>Hosokawa N, Hara T, Kaizuka T, et al., 2009, Nutrient-Dependent mTORC1 Association with the ULK1–Atg13–FIP200 Complex Required for Autophagy. Mol Biol Cell, 20(7): 1981–1991.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B30" content-type="article"><label>30</label><element-citation publication-type="journal"><p>Jung CH, Jun CB, Ro SH, et al., 2009, ULK–Atg13–FIP200 Complex: A New Regulator of mTOR Signaling and Autophagy. Cell, 137(7): 132–133.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B31" content-type="article"><label>31</label><element-citation publication-type="journal"><p>Wong PM, Puente C, Ganley IG, et al., 2013, The ULK1 Complex: Sensing Nutritional Stress for Autophagy Activation. Autophagy, 9(2): 124–137.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B32" content-type="article"><label>32</label><element-citation publication-type="journal"><p>Chan EY, Longatti A, McKnight NC, et al., 2009, Kinase-Inactivated ULK Proteins Inhibit Autophagy via Their Conserved C-Terminal Domains Using an Atg13-Independent Mechanism. Mol Cell Biol, 29(1): 157–171.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B33" content-type="article"><label>33</label><element-citation publication-type="journal"><p>Egan DF, Shackelford DB, Mihaylova MM, et al., 2011, Phosphorylation of ULK1 (hATG1) by AMP-Activated Protein Kinase Connects Energy Sensing to Mitophagy. Science, 331(6016): 456–461.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B34" content-type="article"><label>34</label><element-citation publication-type="journal"><p>Russell RC, Tian Y, Yuan H, et al. 2013, ULK1 Induces Autophagy by Phosphorylating Beclin-1 and Activating VPS34 Lipid Kinase. Nat Cell Biol, 15(7): 741–750.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B35" content-type="article"><label>35</label><element-citation publication-type="journal"><p>He C, Levine B, 2010, The Beclin 1 Interactome. Curr Opin Cell Biol, 22(2): 140–149.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B36" content-type="article"><label>36</label><element-citation publication-type="journal"><p>Kihara A, Noda T, Ishihara N, et al., 2001, Two Distinct Vps34 Phosphatidylinositol 3-Kinase Complexes Function in Autophagy and Carboxypeptidase Y Sorting in Saccharomyces cerevisiae. J Cell Biol, 152(3): 519–530.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B37" content-type="article"><label>37</label><element-citation publication-type="journal"><p>Itakura E, Kishi C, Inoue K, et al., 2008, Beclin 1 Forms Two Distinct Phosphatidylinositol 3-Kinase Complexes with Mammalian Atg14 and UVRAG. Mol Biol Cell, 19(12): 5360–5372.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B38" content-type="article"><label>38</label><element-citation publication-type="journal"><p>Obara K, Sekito T, Ohsumi Y, 2006, Assortment of Phosphatidylinositol 3-Kinase Complexes—Atg14p-Containing Complex Localizes to the Pre-Autophagosomal Structure. Autophagy, 2(6): 400–402.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B39" content-type="article"><label>39</label><element-citation publication-type="journal"><p>Matsunaga K, Saitoh T, Tabata K, et al., 2009, Two Beclin 1-Binding Proteins, Atg14L and Rubicon, Reciprocally Regulate Autophagy at Different Stages. Nat Cell Biol, 11(4): 385–396.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B40" content-type="article"><label>40</label><element-citation publication-type="journal"><p>Sun Q, Fan W, Chen K, et al., 2008, Identification of Barkor as a Mammalian Autophagy-Specific Factor for Beclin 1 and Class III Phosphatidylinositol 3-Kinase. Proc Natl Acad Sci USA, 105(49): 19211–19216.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B41" content-type="article"><label>41</label><element-citation publication-type="journal"><p>Liang C, Lee JS, Inn KS, et al., 2008, Beclin1-Binding UVRAG Targets the Class C Vps Complex to Coordinate Autophagosome Maturation and Endocytic Trafficking. Nat Cell Biol, 10(7): 776–787.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B42" content-type="article"><label>42</label><element-citation publication-type="journal"><p>Zhong Y, Wang QJ, Li X, et al. 2009, Distinct Regulation of Autophagic Activity by Atg14L and Rubicon Associated with Beclin 1–Phosphatidylinositol-3-Kinase Complex. Nat Cell Biol, 11(4): 468–476.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B43" content-type="article"><label>43</label><element-citation publication-type="journal"><p>He C, Baba M, Klionsky DJ, 2009, Double Duty of Atg9 Self-Interaction in Autophagosome Biogenesis. Autophagy, 5(3): 385–387.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B44" content-type="article"><label>44</label><element-citation publication-type="journal"><p>Young ARJ, Chan EYW, Hu XW, et al., 2006, Starvation and ULK1-Dependent Cycling of Mammalian Atg9 between the TGN and Endosomes. J Cell Sci, 119(18): 3888–3900.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B45" content-type="article"><label>45</label><element-citation publication-type="journal"><p>Orsi A, Razi M, Dooley HC, et al., 2012, Dynamic and Transient Interactions of Atg9 with Autophagosomes, but Not Membranes Involved in Secretion or Endocytosis. Mol Biol Cell, 23(10): 1860–1873.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B46" content-type="article"><label>46</label><element-citation publication-type="journal"><p>Yamada T, Carson AR, Caniggia I, et al., 2005, Endothelial Nitric-Oxide Synthase (eNOS) Is Regulated by a Histone H3K27 Demethylase, JMJD3, in Response to Hypoxia. J Biol Chem, 280(43): 43189–43195.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B47" content-type="article"><label>47</label><element-citation publication-type="journal"><p>Ge L, Zhang M, Schekman R, 2014, Phosphatidylinositol 3-Kinase and COPII Generate LC3 Lipidation Vesicles from the ER-Golgi Intermediate Compartment. eLife, 3: e04135.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B48" content-type="article"><label>48</label><element-citation publication-type="journal"><p>Ge L, Zhang M, Kenny SJ, Liu D, et al., 2017, Remodeling of ER–Exit Sites Initiates a Membrane Supply Pathway for Autophagosome Biogenesis. EMBO Rep, 18(9): 1586–1603.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B49" content-type="article"><label>49</label><element-citation publication-type="journal"><p>Suzuki K, Kubota Y, Sekito T, et al., 2007, Hierarchy of Atg Proteins in Pre-Autophagosomal Structure Organization. Genes Cells, 12(2): 209–218.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B50" content-type="article"><label>50</label><element-citation publication-type="journal"><p>Weidberg H, Shvets E, Elazar Z, 2011, Biogenesis and Cargo Selectivity of Autophagosomes. Annu Rev Biochem, 80: 125–156.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B51" content-type="article"><label>51</label><element-citation publication-type="journal"><p>Axe EL, Walker SA, Manifava M, et al., 2008, Autophagosome Formation from Membrane Compartments Enriched in Phosphatidylinositol 3-Phosphate and Dynamin 2. Nat Cell Biol, 10(12): 1243–1250.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B52" content-type="article"><label>52</label><element-citation publication-type="journal"><p>Nascimbeni AC, Codogno P, Morel E, 2017, Phosphatidylinositol-3-Phosphate in the Regulation of Autophagy Membranes. Front Cell Dev Biol, 5: 71.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B53" content-type="article"><label>53</label><element-citation publication-type="journal"><p>Razi M, Chan EYW, Tooze SA, 2009, Early Endosomes and Endosome-Associated ER Subdomains Are Required for Autophagosome Formation. J Cell Biol, 185(2): 305–321.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B54" content-type="article"><label>54</label><element-citation publication-type="journal"><p>Matsunaga K, Morita E, Saitoh T, et al., 2010, Autophagy Requires Endoplasmic Reticulum-Localized PI3K Complex for Pre-Autophagosomal Structure Formation. EMBO Rep, 11(11): 916–922.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B55" content-type="article"><label>55</label><element-citation publication-type="journal"><p>Funderburk SF, Wang QJ, Yue Z, 2010, The Beclin 1–VPS34 Complex—At the Crossroads of Autophagy and Endocytic Trafficking. Autophagy, 6(5): 680–689.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B56" content-type="article"><label>56</label><element-citation publication-type="journal"><p>Karanasios E, Walker SA, Okkenhaug H, et al., 2016, Autophagy Initiation by ULK Complex Assembly on ER Tubulovesicular Regions Marked by ATG9 Vesicles. Nat Commun, 7: 12420.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B57" content-type="article"><label>57</label><element-citation publication-type="journal"><p>Yamamoto H, Kakuta S, Watanabe TM, et al., 2012, Atg9 Vesicles Are an Important Membrane Source during Early Steps of Autophagosome Formation. J Cell Biol, 198(2): 219–233.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B58" content-type="article"><label>58</label><element-citation publication-type="journal"><p>Koyama-Honda I, Itakura E, Fujiwara TK, et al., 2013, Temporal Analysis of Recruitment of Mammalian ATG Proteins to the Autophagosome Formation Site. Autophagy, 9(10): 1491–1499.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B59" content-type="article"><label>59</label><element-citation publication-type="journal"><p>Orsi A, Razi M, Dooley HC, et al., 2012, Dynamic and Transient Interactions of Atg9 with Autophagosomes, but Not Membranes Involved in Secretion or Endocytosis. Mol Biol Cell, 23(10): 1860–1873.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B60" content-type="article"><label>60</label><element-citation publication-type="journal"><p>Takahashi Y, Takabatake Y, Kimura T, et al., 2011, Loss of Autophagy in Dopaminergic Neurons Causes Lewy Body Formation and Motor Dysfunction in Mice. J Clin Invest, 121(7): 2395–2407.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B61" content-type="article"><label>61</label><element-citation publication-type="journal"><p>Young ARJ, Chan EYW, Hu XW, et al., 2006, Starvation and ULK1-Dependent Cycling of Mammalian Atg9 between the TGN and Endosomes. J Cell Sci, 119(18): 3888–3900.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B62" content-type="article"><label>62</label><element-citation publication-type="journal"><p>Orsi A, Razi M, Dooley HC, et al., 2012, Dynamic and Transient Interactions of Atg9 with Autophagosomes, but Not Membranes Involved in Secretion or Endocytosis. Mol Biol Cell, 23(10): 1860–1873.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B63" content-type="article"><label>63</label><element-citation publication-type="journal"><p>Takahashi Y, Takabatake Y, Kimura T, et al., 2011, Loss of Autophagy in Dopaminergic Neurons Causes Lewy Body Formation and Motor Dysfunction in Mice. J Clin Invest, 121(7): 2395–2407.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B64" content-type="article"><label>64</label><element-citation publication-type="journal"><p>Karanasios E, Walker SA, Okkenhaug H, et al., 2016, Autophagy Initiation by ULK Complex Assembly on ER Tubulovesicular Regions Marked by ATG9 Vesicles. Nat Commun, 7: 12420.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B65" content-type="article"><label>65</label><element-citation publication-type="journal"><p>Yamamoto H, Kakuta S, Watanabe TM, et al., 2012, Atg9 Vesicles Are an Important Membrane Source during Early Steps of Autophagosome Formation. J Cell Biol, 198(2): 219–233.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B66" content-type="article"><label>66</label><element-citation publication-type="journal"><p>Koyama-Honda I, Itakura E, Fujiwara TK, et al., 2013, Temporal Analysis of Recruitment of Mammalian ATG Proteins to the Autophagosome Formation Site. Autophagy, 9(10): 1491–1499.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B67" content-type="article"><label>67</label><element-citation publication-type="journal"><p>Axe EL, Walker SA, Manifava M, et al., 2008, Autophagosome Formation from Membrane Compartments Enriched in Phosphatidylinositol 3-Phosphate and Dynamin 2. Nat Cell Biol, 10(12): 1243–1250.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B68" content-type="article"><label>68</label><element-citation publication-type="journal"><p>Nascimbeni AC, Codogno P, Morel E, 2017, Phosphatidylinositol-3-Phosphate in the Regulation of Autophagy Membranes. Front Cell Dev Biol, 5: 71.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B69" content-type="article"><label>69</label><element-citation publication-type="journal"><p>Razi M, Chan EYW, Tooze SA, 2009, Early Endosomes and Endosome-Associated ER Subdomains Are Required for Autophagosome Formation. J Cell Biol, 185(2): 305–321.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B70" content-type="article"><label>70</label><element-citation publication-type="journal"><p>Matsunaga K, Morita E, Saitoh T, et al., 2010, Autophagy Requires Endoplasmic Reticulum-Localized PI3K Complex for Pre-Autophagosomal Structure Formation. EMBO Rep, 11(11): 916–922.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B71" content-type="article"><label>71</label><element-citation publication-type="journal"><p>Funderburk SF, Wang QJ, Yue Z, 2010, The Beclin 1–VPS34 Complex—At the Crossroads of Autophagy and Endocytic Trafficking. Autophagy, 6(5): 680–689.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B72" content-type="article"><label>72</label><element-citation publication-type="journal"><p>Young ARJ, Chan EYW, Hu XW, et al., 2006, Starvation and ULK1-Dependent Cycling of Mammalian Atg9 between the TGN and Endosomes. J Cell Sci, 119(18): 3888–3900.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B73" content-type="article"><label>73</label><element-citation publication-type="journal"><p>Karanasios E, Walker SA, Okkenhaug H, et al., 2016, Autophagy Initiation by ULK Complex Assembly on ER Tubulovesicular Regions Marked by ATG9 Vesicles. Nat Commun, 7: 12420.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B74" content-type="article"><label>74</label><element-citation publication-type="journal"><p>Orsi A, Razi M, Dooley HC, et al., 2012, Dynamic and Transient Interactions of Atg9 with Autophagosomes, but Not Membranes Involved in Secretion or Endocytosis. Mol Biol Cell, 23(10): 1860–1873.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B75" content-type="article"><label>75</label><element-citation publication-type="journal"><p>Yamamoto H, Kakuta S, Watanabe TM, et al., 2012, Atg9 Vesicles Are an Important Membrane Source during Early Steps of Autophagosome Formation. J Cell Biol, 198(2): 219–233.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B76" content-type="article"><label>76</label><element-citation publication-type="journal"><p>Takahashi Y, Takabatake Y, Kimura T, et al., 2011, Loss of Autophagy in Dopaminergic Neurons Causes Lewy Body Formation and Motor Dysfunction in Mice. J Clin Invest, 121(7): 2395–2407.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B77" content-type="article"><label>77</label><element-citation publication-type="journal"><p>Funderburk SF, Wang QJ, Yue Z, 2010, The Beclin 1–VPS34 Complex—At the Crossroads of Autophagy and Endocytic Trafficking. Autophagy, 6(5): 680–689.</p><pub-id pub-id-type="doi"/></element-citation></ref><ref id="B78" content-type="article"><label>78</label><element-citation publication-type="journal"><p>Razi M, Chan EYW, Tooze SA, 2009, Early Endosomes and Endosome-Associated ER Subdomains Are Required for Autophagosome Formation. J Cell Biol, 185(2): 305–321.</p><pub-id pub-id-type="doi"/></element-citation></ref></ref-list></back></article>
