Mitophagy and Oxidative Stress in Cancer and Aging: Focus on Sirtuins and Nanomaterials
Identifieur interne : 000711 ( Ncbi/Merge ); précédent : 000710; suivant : 000712Mitophagy and Oxidative Stress in Cancer and Aging: Focus on Sirtuins and Nanomaterials
Auteurs : Enza Vernucci [Italie] ; Carlo Tomino [Italie] ; Francesca Molinari [Italie] ; Dolores Limongi [Italie] ; Michele Aventaggiato [Italie] ; Luigi Sansone [Italie] ; Marco Tafani [Italie] ; Matteo A. Russo [Italie]Source :
- Oxidative Medicine and Cellular Longevity [ 1942-0900 ] ; 2019.
Abstract
Mitochondria are the cellular center of energy production and of several important metabolic processes. Mitochondrion health is maintained with a substantial intervention of mitophagy, a process of macroautophagy that degrades selectively dysfunctional and irreversibly damaged organelles. Because of its crucial duty, alteration in mitophagy can cause functional and structural adjustment in the mitochondria, changes in energy production, loss of cellular adaptation, and cell death. In this review, we discuss the dual role that mitophagy plays in cancer and age-related pathologies, as a consequence of oxidative stress, evidencing the triggering stimuli and mechanisms and suggesting the molecular targets for its therapeutic control. Finally, a section has been dedicated to the interplay between mitophagy and therapies using nanoparticles that are the new frontier for a direct and less invasive strategy.
Url:
DOI: 10.1155/2019/6387357
PubMed: 31210843
PubMed Central: 6532280
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- to stream Pmc, to step Curation: 000A88
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PMC:6532280Le document en format XML
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nuts="2">Latium</region></placeName></affiliation></author><author><name sortKey="Sansone, Luigi" sort="Sansone, Luigi" uniqKey="Sansone L" first="Luigi" last="Sansone">Luigi Sansone</name><affiliation wicri:level="1"><nlm:aff id="I6">Department of Cellular and Molecular Pathology, IRCCS San Raffaele, Via Val Cannuta 247, 00166 Rome, Italy</nlm:aff><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Cellular and Molecular Pathology, IRCCS San Raffaele, Via Val Cannuta 247, 00166 Rome</wicri:regionArea><placeName><settlement type="city">Rome</settlement><region nuts="2">Latium</region></placeName></affiliation></author><author><name sortKey="Tafani, Marco" sort="Tafani, Marco" uniqKey="Tafani M" first="Marco" last="Tafani">Marco Tafani</name><affiliation wicri:level="1"><nlm:aff id="I7">Department of Experimental Medicine, Sapienza University of Rome, Viale Regina Elena 324, 00161 Rome, Italy</nlm:aff><country xml:lang="fr">Italie</country><wicri:regionArea>Department 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Russo</name><affiliation wicri:level="1"><nlm:aff id="I6">Department of Cellular and Molecular Pathology, IRCCS San Raffaele, Via Val Cannuta 247, 00166 Rome, Italy</nlm:aff><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Cellular and Molecular Pathology, IRCCS San Raffaele, Via Val Cannuta 247, 00166 Rome</wicri:regionArea><placeName><settlement type="city">Rome</settlement><region nuts="2">Latium</region></placeName></affiliation><affiliation wicri:level="1"><nlm:aff id="I8">MEBIC Consortium, San Raffaele Rome Open University, Via Val Cannuta 247, 00166 Rome, Italy</nlm:aff><country xml:lang="fr">Italie</country><wicri:regionArea>MEBIC Consortium, San Raffaele Rome Open University, Via Val Cannuta 247, 00166 Rome</wicri:regionArea><placeName><settlement type="city">Rome</settlement><region nuts="2">Latium</region></placeName></affiliation></author></analytic><series><title level="j">Oxidative Medicine and Cellular Longevity</title><idno type="ISSN">1942-0900</idno><idno type="eISSN">1942-0994</idno><imprint><date when="2019">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Mitochondria are the cellular center of energy production and of several important metabolic processes. Mitochondrion health is maintained with a substantial intervention of mitophagy, a process of macroautophagy that degrades selectively dysfunctional and irreversibly damaged organelles. Because of its crucial duty, alteration in mitophagy can cause functional and structural adjustment in the mitochondria, changes in energy production, loss of cellular adaptation, and cell death. In this review, we discuss the dual role that mitophagy plays in cancer and age-related pathologies, as a consequence of oxidative stress, evidencing the triggering stimuli and mechanisms and suggesting the molecular targets for its therapeutic control. Finally, a section has been dedicated to the interplay between mitophagy and therapies using nanoparticles that are the new frontier for a direct and less invasive strategy.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Youle, R J" uniqKey="Youle R">R. J. 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Oxid Med Cell Longev</journal-id><journal-id journal-id-type="iso-abbrev">Oxid Med Cell Longev</journal-id><journal-id journal-id-type="publisher-id">OMCL</journal-id><journal-title-group><journal-title>Oxidative Medicine and Cellular Longevity</journal-title></journal-title-group><issn pub-type="ppub">1942-0900</issn><issn pub-type="epub">1942-0994</issn><publisher><publisher-name>Hindawi</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">31210843</article-id><article-id pub-id-type="pmc">6532280</article-id><article-id pub-id-type="doi">10.1155/2019/6387357</article-id><article-categories><subj-group subj-group-type="heading"><subject>Review Article</subject></subj-group></article-categories><title-group><article-title>Mitophagy and Oxidative Stress in Cancer and Aging: Focus on Sirtuins and Nanomaterials</article-title></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid" authenticated="false">http://orcid.org/0000-0002-9354-6728</contrib-id><name><surname>Vernucci</surname><given-names>Enza</given-names></name><email>enza.vernucci@gmail.com</email><xref ref-type="aff" rid="I1"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Tomino</surname><given-names>Carlo</given-names></name><xref ref-type="aff" rid="I2"><sup>2</sup></xref></contrib><contrib contrib-type="author"><contrib-id contrib-id-type="orcid" authenticated="false">http://orcid.org/0000-0003-0570-7438</contrib-id><name><surname>Molinari</surname><given-names>Francesca</given-names></name><xref ref-type="aff" rid="I3"><sup>3</sup></xref></contrib><contrib contrib-type="author"><name><surname>Limongi</surname><given-names>Dolores</given-names></name><xref ref-type="aff" rid="I4"><sup>4</sup></xref></contrib><contrib contrib-type="author"><name><surname>Aventaggiato</surname><given-names>Michele</given-names></name><xref ref-type="aff" rid="I5"><sup>5</sup></xref></contrib><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid" authenticated="false">http://orcid.org/0000-0003-3150-6461</contrib-id><name><surname>Sansone</surname><given-names>Luigi</given-names></name><email>luigi.sansone@sanraffaele.it</email><xref ref-type="aff" rid="I6"><sup>6</sup></xref></contrib><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid" authenticated="false">http://orcid.org/0000-0001-7128-810X</contrib-id><name><surname>Tafani</surname><given-names>Marco</given-names></name><email>marco.tafani@uniroma1.it</email><xref ref-type="aff" rid="I7"><sup>7</sup></xref></contrib><contrib contrib-type="author"><contrib-id contrib-id-type="orcid" authenticated="false">http://orcid.org/0000-0002-5847-6015</contrib-id><name><surname>Russo</surname><given-names>Matteo A.</given-names></name><xref ref-type="aff" rid="I6"><sup>6</sup></xref><xref ref-type="aff" rid="I8"><sup>8</sup></xref></contrib></contrib-group><aff id="I1"><sup>1</sup>Department of Cardiovascular, Nephrologic, Anesthesiologic and Geriatric Sciences, Sapienza University of Rome, Viale Regina Elena 324, 00161 Rome, Italy</aff><aff id="I2"><sup>2</sup>IRCCS San Raffaele, Scientific Direction, Via Val Cannuta 247, 00166 Rome, Italy</aff><aff id="I3"><sup>3</sup>Department of Experimental Medicine, Sapienza University of Rome, Viale Regina Elena 324, 00161 Rome, Italy</aff><aff id="I4"><sup>4</sup>IRCCS San Raffaele Pisana, Department of Human Sciences and Promotion of the Quality of Life, San Raffaele Roma Open University, Via Val Cannuta 247, 00166 Rome, Italy</aff><aff id="I5"><sup>5</sup>Department of Experimental Medicine, Sapienza University of Rome, Viale Regina Elena 324, 00161 Rome, Italy</aff><aff id="I6"><sup>6</sup>Department of Cellular and Molecular Pathology, IRCCS San Raffaele, Via Val Cannuta 247, 00166 Rome, Italy</aff><aff id="I7"><sup>7</sup>Department of Experimental Medicine, Sapienza University of Rome, Viale Regina Elena 324, 00161 Rome, Italy</aff><aff id="I8"><sup>8</sup>MEBIC Consortium, San Raffaele Rome Open University, Via Val Cannuta 247, 00166 Rome, Italy</aff><author-notes><fn fn-type="other"><p>Guest Editor: Miguel Sanchez-Alvarez</p></fn></author-notes><pub-date pub-type="collection"><year>2019</year></pub-date><pub-date pub-type="epub"><day>9</day><month>5</month><year>2019</year></pub-date><volume>2019</volume><elocation-id>6387357</elocation-id><history><date date-type="received"><day>21</day><month>2</month><year>2019</year></date><date date-type="accepted"><day>8</day><month>4</month><year>2019</year></date></history><permissions><copyright-statement>Copyright © 2019 Enza Vernucci et al.</copyright-statement><copyright-year>2019</copyright-year><license xlink:href="http://creativecommons.org/licenses/by/4.0/"><license-p>This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.</license-p></license></permissions><abstract><p>Mitochondria are the cellular center of energy production and of several important metabolic processes. Mitochondrion health is maintained with a substantial intervention of mitophagy, a process of macroautophagy that degrades selectively dysfunctional and irreversibly damaged organelles. Because of its crucial duty, alteration in mitophagy can cause functional and structural adjustment in the mitochondria, changes in energy production, loss of cellular adaptation, and cell death. In this review, we discuss the dual role that mitophagy plays in cancer and age-related pathologies, as a consequence of oxidative stress, evidencing the triggering stimuli and mechanisms and suggesting the molecular targets for its therapeutic control. Finally, a section has been dedicated to the interplay between mitophagy and therapies using nanoparticles that are the new frontier for a direct and less invasive strategy.</p></abstract><funding-group><award-group><funding-source>Scientifica Ateneo 2017</funding-source></award-group><award-group><funding-source>Fondazione Roma</funding-source></award-group><award-group><funding-source>Ricerca Corrente 2017</funding-source></award-group></funding-group></article-meta></front><floats-group><fig id="fig1" orientation="portrait" position="float"><label>Figure 1</label><caption><p>Autophagosomes accumulate into myocardiocytes due to the presence of chloroquine which blocks the fusion between primary lysosomes and autophagosomes. (a) Large autophagosomes (A) with different cytoplasmic components, mainly degraded lipid membranes, and glycogen. (b) Magnification of the detail indicated in the square. m: mitochondria.</p></caption><graphic xlink:href="OMCL2019-6387357.001"></graphic></fig><fig id="fig2" orientation="portrait" position="float"><label>Figure 2</label><caption><p>Mitochondria (m) have been damaged by different physiopathological conditions. (a) Mutated, misfolded, and fibrillary polymerized mitochondrial proteins may accumulate into the matrix giving rise to giant mitochondria with paracrystalline inclusions. They appear surrounded by endoplasmic reticulum (ER) membranes, indicating a process of segregation for autophagocytosis. (b) Antibiotics affecting bacterial protein synthesis may interfere with mitochondrial protein synthesis producing enlarged mitochondria (m) with paracrystalline inclusions and bizarre shape. Also, in this case, the close interaction with endoplasmic reticulum membranes suggests a process of segregation for mitophagy (N: nucleus). (c) Swollen liver mitochondria (m) after 3 hours of ischemia: they show a number of pathological changes: volume increase, dishomogeneous electron-clear and sometimes vacuolized matrix, fragmented cristae, and sometimes interrupted outer membrane. Indeed, they appear, together with apparently intact peroxisomes (p), surrounded by endoplasmic reticulum (ER) which indicates the autophagocytic process. (d) Mitochondria (m) from the glomerular zone of a suprarenal cortex which has been intensively stimulated by ACTH. The consequent hypertrophy includes also an increase of mitochondrial growth (number and volume) and an accelerated turnover as suggested by the increased mitophagy (A).</p></caption><graphic xlink:href="OMCL2019-6387357.002"></graphic></fig><fig id="fig3" orientation="portrait" position="float"><label>Figure 3</label><caption><p>Sequence and molecular details of the selective mitophagy. When mitochondria undergo decrease in membrane potential (or different stress stimuli), PINK1, localized on the mitochondrial membrane, recruits Parkin that polyubiquitinates MOM protein and induces the autophagosome formation. Then, lysosome fuses with the autophagosome (autophagolysosome) and the degraded material can be recycled or disposed.</p></caption><graphic xlink:href="OMCL2019-6387357.003"></graphic></fig><fig id="fig4" orientation="portrait" position="float"><label>Figure 4</label><caption><p>Electron micrograph of a mitophagic vacuole (A) containing a well-preserved mitochondrion (m). Molecules involved in selective mitophagy are indicated.</p></caption><graphic xlink:href="OMCL2019-6387357.004"></graphic></fig><fig id="fig5" orientation="portrait" position="float"><label>Figure 5</label><caption><p>Schematic representation of all the aspects related to mitophagy. Two basic mechanisms have been elucidated involving a different set of molecules in relation to the prototype damage: the mitochondrial depolarization and hypoxia, starvation, and genes controlled by some master transcription factors (p53, RB/E2F, FoxOS, NFkB, sirtuins, and others).</p></caption><graphic xlink:href="OMCL2019-6387357.005"></graphic></fig><table-wrap id="tab1" orientation="portrait" position="float"><label>Table 1</label><caption><p>Agents affecting mitophagy.</p></caption><table frame="hsides" rules="groups"><thead><tr><th align="left" rowspan="1" colspan="1">Agent</th><th align="center" rowspan="1" colspan="1">Effect on mitophagy</th><th align="center" rowspan="1" colspan="1">Mechanism</th><th align="center" rowspan="1" colspan="1">Reference</th></tr></thead><tbody><tr><td align="left" rowspan="1" colspan="1">Nicotinamide derivatives</td><td align="center" rowspan="1" colspan="1">Increase</td><td align="center" rowspan="1" colspan="1">NAD+ replenishment increases DCT-1- (ortholog to the mammalian BNIP3L/NIX) associated mitophagy in worms</td><td align="center" rowspan="1" colspan="1">[<xref rid="B6" ref-type="bibr">6</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">Spermidine</td><td align="center" rowspan="1" colspan="1">Increase</td><td align="center" rowspan="1" colspan="1">Induces ATM activation that, in turn, promotes the accumulation of PINK1 and translocation of Parkin to mitochondria</td><td align="center" rowspan="1" colspan="1">[<xref rid="B7" ref-type="bibr">7</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">Urolithin A</td><td align="center" rowspan="1" colspan="1">Increase</td><td align="center" rowspan="1" colspan="1">Upregulat<bold>es</bold> of PINK1, DCT-1, and SKN-1<break></break>Mechanism not known</td><td align="center" rowspan="1" colspan="1">[<xref rid="B8" ref-type="bibr">8</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">Rapamycin</td><td align="center" rowspan="1" colspan="1">Increase</td><td align="center" rowspan="1" colspan="1">Increase<bold>s</bold> the translocation of p62 and Parkin to the damaged mitochondria</td><td align="center" rowspan="1" colspan="1">[<xref rid="B9" ref-type="bibr">9</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">Metformin</td><td align="center" rowspan="1" colspan="1">Increase</td><td align="center" rowspan="1" colspan="1">Decrease<bold>s</bold> the inhibitory interaction between Parkin and p53 and increase the degradation of mitofusins</td><td align="center" rowspan="1" colspan="1">[<xref rid="B10" ref-type="bibr">10</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">Chloroquine</td><td align="center" rowspan="1" colspan="1">Inhibition</td><td align="center" rowspan="1" colspan="1">Inhibits phagosome/lysosome fusion</td><td align="center" rowspan="1" colspan="1">[<xref rid="B11" ref-type="bibr">11</xref>, <xref rid="B12" ref-type="bibr">12</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">Mitochondrial toxins:<break></break>FCCP/CCCP, rotenone, antimycin A, valmycin, oligomycin, 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), and 6-hydroxydopamine</td><td align="center" rowspan="1" colspan="1">Increase</td><td align="center" rowspan="1" colspan="1">Perturb mitochondrial ATP production and cause ROS generation</td><td align="center" rowspan="1" colspan="1">[<xref rid="B13" ref-type="bibr">13</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">Ceramides</td><td align="center" rowspan="1" colspan="1">Increase</td><td align="center" rowspan="1" colspan="1">Interact directly with LC3B-II upon Drp1-dependent mitochondrial fission, leading to inhibition of mitochondrial function and oxygen consumption</td><td align="center" rowspan="1" colspan="1">[<xref rid="B14" ref-type="bibr">14</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">Selenite</td><td align="center" rowspan="1" colspan="1">Increase</td><td align="center" rowspan="1" colspan="1">Induces superoxide-mediated mitophagic cell death</td><td align="center" rowspan="1" colspan="1">[<xref rid="B15" ref-type="bibr">15</xref>]</td></tr></tbody></table></table-wrap><table-wrap id="tab2" orientation="portrait" position="float"><label>Table 2</label><caption><p>Mitochondrial receptors and their ligands involved in the mitophagic process.</p></caption><table frame="hsides" rules="groups"><thead><tr><th align="left" rowspan="1" colspan="1">Receptor</th><th align="center" rowspan="1" colspan="1">Localization</th><th align="center" rowspan="1" colspan="1">Ligands (interaction)</th><th align="center" rowspan="1" colspan="1">Species</th><th align="center" rowspan="1" colspan="1">Reference</th></tr></thead><tbody><tr><td align="left" rowspan="1" colspan="1">ATG32</td><td align="center" rowspan="1" colspan="1">Outer mitochondrial membrane</td><td align="center" rowspan="1" colspan="1">Atg8, Atg11</td><td align="center" rowspan="1" colspan="1">Yeast</td><td align="center" rowspan="1" colspan="1">[<xref rid="B22" ref-type="bibr">22</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">NIX/BNIP3L</td><td align="center" rowspan="1" colspan="1">Outer mitochondrial membrane</td><td align="center" rowspan="1" colspan="1">LC3</td><td align="center" rowspan="1" colspan="1">Mammals</td><td align="center" rowspan="1" colspan="1">[<xref rid="B23" ref-type="bibr">23</xref>–<xref rid="B25" ref-type="bibr">25</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">BCL2L13</td><td align="center" rowspan="1" colspan="1">Outer mitochondrial membrane</td><td align="center" rowspan="1" colspan="1">LC3</td><td align="center" rowspan="1" colspan="1">Mammals</td><td align="center" rowspan="1" colspan="1">[<xref rid="B26" ref-type="bibr">26</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">FUNDC1</td><td align="center" rowspan="1" colspan="1">Outer mitochondrial membrane</td><td align="center" rowspan="1" colspan="1">LC3</td><td align="center" rowspan="1" colspan="1">Mammals</td><td align="center" rowspan="1" colspan="1">[<xref rid="B27" ref-type="bibr">27</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">Cardiolipin</td><td align="center" rowspan="1" colspan="1">Mitochondrial inner membrane, any damage to mitochondria, or depolarization of its membrane results in the translocation to outer mitochondrial membrane</td><td align="center" rowspan="1" colspan="1">LC3</td><td align="center" rowspan="1" colspan="1">Mammals</td><td align="center" rowspan="1" colspan="1">[<xref rid="B28" ref-type="bibr">28</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">PHB 2</td><td align="center" rowspan="1" colspan="1">Inner mitochondrial membrane</td><td align="center" rowspan="1" colspan="1">LC3</td><td align="center" rowspan="1" colspan="1">Mammals</td><td align="center" rowspan="1" colspan="1">[<xref rid="B29" ref-type="bibr">29</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">Parkin</td><td align="center" rowspan="1" colspan="1">Normally in the cytosol, it is translocated to the outer mitochondrial membrane upon depolarization</td><td align="center" rowspan="1" colspan="1">AMBRA1, LC3</td><td align="center" rowspan="1" colspan="1">Mammals</td><td align="center" rowspan="1" colspan="1">[<xref rid="B30" ref-type="bibr">30</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">BCL2L13</td><td align="center" rowspan="1" colspan="1">Outer mitochondrial membrane</td><td align="center" rowspan="1" colspan="1">LC3</td><td align="center" rowspan="1" colspan="1">Mammals</td><td align="center" rowspan="1" colspan="1">[<xref rid="B31" ref-type="bibr">31</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">FKBP8</td><td align="center" rowspan="1" colspan="1">Outer mitochondrial membrane</td><td align="center" rowspan="1" colspan="1">LC3</td><td align="center" rowspan="1" colspan="1">Mammals</td><td align="center" rowspan="1" colspan="1">[<xref rid="B32" ref-type="bibr">32</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">SMURF1</td><td align="center" rowspan="1" colspan="1">Cytoplasmatic, colocalized with damaged mitochondria</td><td align="center" rowspan="1" colspan="1">LC3?</td><td align="center" rowspan="1" colspan="1">Mammals</td><td align="center" rowspan="1" colspan="1"></td></tr><tr><td align="left" rowspan="1" colspan="1">BNIP3</td><td align="center" rowspan="1" colspan="1">Outer mitochondrial membrane</td><td align="center" rowspan="1" colspan="1">LC3</td><td align="center" rowspan="1" colspan="1">Mammals</td><td align="center" rowspan="1" colspan="1">[<xref rid="B33" ref-type="bibr">33</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">NLRX1</td><td align="center" rowspan="1" colspan="1">Outer mitochondrial membrane</td><td align="center" rowspan="1" colspan="1">LC3</td><td align="center" rowspan="1" colspan="1">Mammals</td><td align="center" rowspan="1" colspan="1">[<xref rid="B34" ref-type="bibr">34</xref>]</td></tr></tbody></table></table-wrap><table-wrap id="tab3" orientation="portrait" position="float"><label>Table 3</label><caption><p>Markers of mitophagy.</p></caption><table frame="hsides" rules="groups"><thead><tr><th align="left" rowspan="1" colspan="1">Marker</th><th align="center" rowspan="1" colspan="1">Localization</th><th align="center" rowspan="1" colspan="1">Species</th><th align="center" rowspan="1" colspan="1">Reference</th></tr></thead><tbody><tr><td align="left" rowspan="1" colspan="1">Aup1</td><td align="center" rowspan="1" colspan="1">Mitochondrial intermembrane space</td><td align="center" rowspan="1" colspan="1">Yeast</td><td align="center" rowspan="1" colspan="1">[<xref rid="B2" ref-type="bibr">2</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">Uth1</td><td align="center" rowspan="1" colspan="1">Cytoplasmic leaflet of the outer mitochondrial membrane</td><td align="center" rowspan="1" colspan="1">Yeast</td><td align="center" rowspan="1" colspan="1">[<xref rid="B3" ref-type="bibr">3</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">LGG-1</td><td align="center" rowspan="1" colspan="1">Membrane of phagophore and autophagosome</td><td align="center" rowspan="1" colspan="1">Yeast</td><td align="center" rowspan="1" colspan="1">[<xref rid="B51" ref-type="bibr">51</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">PINK1</td><td align="center" rowspan="1" colspan="1">Normally undetectable, stabilized on the outer mitochondrial membrane when mitochondria are depolarized</td><td align="center" rowspan="1" colspan="1">Mammals</td><td align="center" rowspan="1" colspan="1">[<xref rid="B52" ref-type="bibr">52</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">Parkin</td><td align="center" rowspan="1" colspan="1">Normally in cytosol, it is translocated to the outer mitochondrial membrane when mitochondria are depolarized</td><td align="center" rowspan="1" colspan="1">Mammals</td><td align="center" rowspan="1" colspan="1">[<xref rid="B30" ref-type="bibr">30</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">LC3-II</td><td align="center" rowspan="1" colspan="1">Cytosolic, during autophagy, recruited to form autophagosomal membranes</td><td align="center" rowspan="1" colspan="1">Mammals</td><td align="center" rowspan="1" colspan="1">[<xref rid="B53" ref-type="bibr">53</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">p62</td><td align="center" rowspan="1" colspan="1">Parkin recruited to mitochondria</td><td align="center" rowspan="1" colspan="1">Mammals</td><td align="center" rowspan="1" colspan="1">[<xref rid="B54" ref-type="bibr">54</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">TOM20</td><td align="center" rowspan="1" colspan="1">Outer mitochondrial membrane</td><td align="center" rowspan="1" colspan="1">Mammals</td><td align="center" rowspan="1" colspan="1">[<xref rid="B38" ref-type="bibr">38</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">TIM23</td><td align="center" rowspan="1" colspan="1">Inner mitochondrial membrane</td><td align="center" rowspan="1" colspan="1">Mammals</td><td align="center" rowspan="1" colspan="1">[<xref rid="B27" ref-type="bibr">27</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">CypD (cyclophilin D)</td><td align="center" rowspan="1" colspan="1">Mitochondrial matrix</td><td align="center" rowspan="1" colspan="1">Mammals</td><td align="center" rowspan="1" colspan="1">[<xref rid="B55" ref-type="bibr">55</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">HSP60</td><td align="center" rowspan="1" colspan="1">Mitochondrial matrix</td><td align="center" rowspan="1" colspan="1">Mammals</td><td align="center" rowspan="1" colspan="1">[<xref rid="B55" ref-type="bibr">55</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">ULK1</td><td align="center" rowspan="1" colspan="1">Recruited to fragmented mitochondria in response to hypoxia or FCCP</td><td align="center" rowspan="1" colspan="1">Mammals</td><td align="center" rowspan="1" colspan="1">[<xref rid="B56" ref-type="bibr">56</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">SMURF1</td><td align="center" rowspan="1" colspan="1">Cytoplasmatic, colocalized with damaged mitochondria</td><td align="center" rowspan="1" colspan="1">Mammals</td><td align="center" rowspan="1" colspan="1">[<xref rid="B57" ref-type="bibr">57</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">Mitofusins 1/2</td><td align="center" rowspan="1" colspan="1">Mitochondrial outer membrane</td><td align="center" rowspan="1" colspan="1">Mammals</td><td align="center" rowspan="1" colspan="1">[<xref rid="B58" ref-type="bibr">58</xref>]</td></tr></tbody></table></table-wrap></floats-group></pmc><affiliations><list><country><li>Italie</li></country><region><li>Latium</li></region><settlement><li>Rome</li></settlement></list><tree><country name="Italie"><region name="Latium"><name sortKey="Vernucci, Enza" sort="Vernucci, Enza" uniqKey="Vernucci E" first="Enza" last="Vernucci">Enza Vernucci</name></region><name sortKey="Aventaggiato, Michele" sort="Aventaggiato, Michele" uniqKey="Aventaggiato M" first="Michele" last="Aventaggiato">Michele Aventaggiato</name><name sortKey="Limongi, Dolores" sort="Limongi, Dolores" uniqKey="Limongi D" first="Dolores" last="Limongi">Dolores Limongi</name><name sortKey="Molinari, Francesca" sort="Molinari, Francesca" uniqKey="Molinari F" first="Francesca" last="Molinari">Francesca Molinari</name><name sortKey="Russo, Matteo A" sort="Russo, Matteo A" uniqKey="Russo M" first="Matteo A." last="Russo">Matteo A. Russo</name><name sortKey="Russo, Matteo A" sort="Russo, Matteo A" uniqKey="Russo M" first="Matteo A." last="Russo">Matteo A. Russo</name><name sortKey="Sansone, Luigi" sort="Sansone, Luigi" uniqKey="Sansone L" first="Luigi" last="Sansone">Luigi Sansone</name><name sortKey="Tafani, Marco" sort="Tafani, Marco" uniqKey="Tafani M" first="Marco" last="Tafani">Marco Tafani</name><name sortKey="Tomino, Carlo" sort="Tomino, Carlo" uniqKey="Tomino C" first="Carlo" last="Tomino">Carlo Tomino</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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