{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T07:55:06Z","timestamp":1790582106089,"version":"4.1.0"},"reference-count":143,"publisher":"Walter de Gruyter GmbH","license":[{"start":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T00:00:00Z","timestamp":1790640000000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Sequestosome 1 (SQSTM1 or p62) is a multi-domain protein that functions as a scaffold for aggregating proteins into cytoplasmic inclusions and mediating their turnover via selective autophagy. However, p62 is more than an autophagy scaffold or adaptor protein; it\u2019s linked with endo\/exosomal protein trafficking and the ubiquitin proteasome system and, through its interactions with many different proteins, plays important roles in regulating cell signaling events (e.g., oxidative stress response). While its core functions are linked to proteostasis maintenance, p62 is also involved in proteostasis-independent mechanisms. In this review, we highlight the well-established role of p62 in selective autophagy in mammalian cells and harmonize known and emerging p62 functions under three main themes: proteostasis regulation, genomic integrity maintenance, and organellar homeostasis. We highlight some open questions on the potentially pivotal role of p62 in bridging these themes, which we believe would herald the next decade of research involving this versatile protein.<\/jats:p>","DOI":"10.1515\/hsz-2026-0146","type":"journal-article","created":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T06:56:03Z","timestamp":1790578563000},"source":"Crossref","is-referenced-by-count":0,"title":["Sequestosome 1 (SQSTM1\/p62) at the nexus of genome integrity maintenance, proteostasis regulation and organellar homeostasis"],"prefix":"10.1515","author":[{"given":"Celina","family":"Hirschelmann","sequence":"first","affiliation":[{"name":"Cellular Protein Homeostasis, RPTU University Kaiserslautern-Landau , Paul-Ehrlich-Stra\u00dfe 24, D-67663 , Kaiserslautern , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5891-5823","authenticated-orcid":false,"given":"Prince Saforo","family":"Amponsah","sequence":"additional","affiliation":[{"name":"Cellular Protein Homeostasis, RPTU University Kaiserslautern-Landau , Paul-Ehrlich-Stra\u00dfe 24, D-67663 , Kaiserslautern , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"374","published-online":{"date-parts":[[2026,9,29]]},"reference":[{"key":"2026092806555689340_j_hsz-2026-0146_ref_001","doi-asserted-by":"crossref","unstructured":"Aleksandrov, A.E., Bankov, B.I., Djeliova, V.L., Antov, G.G., Stoichev, S., Mironova, R.S., and Iliev, D.B. (2025). Synergistic upregulation of extracellular vesicles and cell-free nucleic acids by chloroquine and temozolomide in glioma cell cultures. Int. J.\u00a0Mol. Sci. 26, https:\/\/doi.org\/10.3390\/ijms26199692.","DOI":"10.20944\/preprints202508.1783.v1"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_002","doi-asserted-by":"crossref","unstructured":"Amponsah, P.S., Bokenkamp, J.E., Kurpa, O., Lenhard, S., Myronova, A., Velazquez, D.O.V., Hirschelmann, C., Behrends, C., Herrmann, J.M., Raschle, M., et al.. (2025). Aneuploidy-induced proteostasis disruption impairs mitochondrial functions and mediates aggregation of mitochondrial precursor proteins through SQSTM1\/p62. Nat. Commun. 16: 5328, https:\/\/doi.org\/10.1038\/s41467-025-60857-4.","DOI":"10.1038\/s41467-025-60857-4"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_003","doi-asserted-by":"crossref","unstructured":"Amponsah, P.S. and Storchova, Z. (2025). The proteostasis burden of aneuploidy. Biol. Chem. 406: 331\u2013343, https:\/\/doi.org\/10.1515\/hsz-2024-0163.","DOI":"10.1515\/hsz-2024-0163"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_004","doi-asserted-by":"crossref","unstructured":"Belizario, J.E., Alves, J., Garay-Malpartida, M., and Occhiucci, J.M. (2008). Coupling caspase cleavage and proteasomal degradation of proteins carrying PEST motif. Curr. Protein Pept. Sci. 9: 210\u2013220, https:\/\/doi.org\/10.2174\/138920308784534023.","DOI":"10.2174\/138920308784534023"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_005","doi-asserted-by":"crossref","unstructured":"Berkamp, S., Jungbluth, L., Katranidis, A., Mostafavi, S., Korculanin, O., Lu, P.H., Ickert, L., Dierig, M.M., Sharma, L., Thukral, L., et al.. (2025). Structural organization of p62 filaments and the cellular ultrastructure of calcium-rich p62-enwrapped lipid droplet cargo. Nat. Commun. 16: 10810, https:\/\/doi.org\/10.1038\/s41467-025-66785-7.","DOI":"10.1038\/s41467-025-66785-7"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_006","doi-asserted-by":"crossref","unstructured":"Berkamp, S., Mostafavi, S., and Sachse, C. (2021). Structure and function of p62\/SQSTM1 in the emerging framework of phase separation. FEBS J. 288: 6927\u20136941, https:\/\/doi.org\/10.1111\/febs.15672.","DOI":"10.1111\/febs.15672"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_007","doi-asserted-by":"crossref","unstructured":"Bjorkoy, G., Lamark, T., Brech, A., Outzen, H., Perander, M., Overvatn, A., Stenmark, H., and Johansen, T. (2005). p62\/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J.\u00a0Cell Biol. 171: 603\u2013614, https:\/\/doi.org\/10.1083\/jcb.200507002.","DOI":"10.1083\/jcb.200507002"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_008","doi-asserted-by":"crossref","unstructured":"Bonavita, R., Scerra, G., Di Martino, R., Nuzzo, S., Polishchuk, E., Di Gennaro, M., Williams, S.V., Caporaso, M.G., Caiazza, C., Polishchuk, R., et al.. (2023). The HSPB1-p62\/SQSTM1 functional complex regulates the unconventional secretion and transcellular spreading of the HD-associated mutant huntingtin protein. Hum. Mol. Genet. 32: 2269\u20132291, https:\/\/doi.org\/10.1093\/hmg\/ddad047.","DOI":"10.1093\/hmg\/ddad047"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_009","doi-asserted-by":"crossref","unstructured":"Brangwynne, C.P., Eckmann, C.R., Courson, D.S., Rybarska, A., Hoege, C., Gharakhani, J., Julicher, F., and Hyman, A.A. (2009). Germline P granules are liquid droplets that localize by controlled dissolution\/condensation. Science 324: 1729\u20131732, https:\/\/doi.org\/10.1126\/science.1172046.","DOI":"10.1126\/science.1172046"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_010","doi-asserted-by":"crossref","unstructured":"Carroll, B., Otten, E.G., Manni, D., Stefanatos, R., Menzies, F.M., Smith, G.R., Jurk, D., Kenneth, N., Wilkinson, S., Passos, J.F., et al.. (2018). Oxidation of SQSTM1\/p62 mediates the link between redox state and protein homeostasis. Nat. Commun. 9: 256, https:\/\/doi.org\/10.1038\/s41467-017-02746-z.","DOI":"10.1038\/s41467-017-02746-z"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_011","doi-asserted-by":"crossref","unstructured":"Cenini, G., Rub, C., Bruderek, M., and Voos, W. (2016). Amyloid beta-peptides interfere with mitochondrial preprotein import competence by a coaggregation process. Mol. Biol. Cell 27: 3257\u20133272, https:\/\/doi.org\/10.1091\/mbc.E16-05-0313.","DOI":"10.1091\/mbc.E16-05-0313"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_012","doi-asserted-by":"crossref","unstructured":"Choong, C.J., Okuno, T., Ikenaka, K., Baba, K., Hayakawa, H., Koike, M., Yokota, M., Doi, J., Kakuda, K., Takeuchi, T., et al.. (2021). Alternative mitochondrial quality control mediated by extracellular release. Autophagy 17: 2962\u20132974, https:\/\/doi.org\/10.1080\/15548627.2020.1848130.","DOI":"10.1080\/15548627.2020.1848130"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_013","doi-asserted-by":"crossref","unstructured":"Chunduri, N.K., Menges, P., Zhang, X., Wieland, A., Gotsmann, V.L., Mardin, B.R., Buccitelli, C., Korbel, J.O., Willmund, F., Kschischo, M., et al.. (2021). Systems approaches identify the consequences of monosomy in somatic human cells. Nat. Commun. 12: 5576, https:\/\/doi.org\/10.1038\/s41467-021-25288-x.","DOI":"10.1038\/s41467-021-25288-x"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_014","doi-asserted-by":"crossref","unstructured":"Ciuffa, R., Lamark, T., Tarafder, A.K., Guesdon, A., Rybina, S., Hagen, W.J., Johansen, T., and Sachse, C. (2015). The selective autophagy receptor p62 forms a flexible filamentous helical scaffold. Cell Rep. 11: 748\u2013758, https:\/\/doi.org\/10.1016\/j.celrep.2015.03.062.","DOI":"10.1016\/j.celrep.2015.03.062"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_015","doi-asserted-by":"crossref","unstructured":"Cohen-Kaplan, V., Livneh, I., Avni, N., Fabre, B., Ziv, T., Kwon, Y.T., and Ciechanover, A. (2016). p62- and ubiquitin-dependent stress-induced autophagy of the mammalian 26S proteasome. Proc. Natl. Acad. Sci. USA 113: E7490\u2013E7499, https:\/\/doi.org\/10.1073\/pnas.1615455113.","DOI":"10.1073\/pnas.1615455113"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_016","doi-asserted-by":"crossref","unstructured":"Crotti, S., Secco, V., Morini, M., and Carra, S. (2026). Small heat shock proteins and biomolecular condensates. Cell. Mol. Life Sci. 83, https:\/\/doi.org\/10.1007\/s00018-026-06216-y.","DOI":"10.1007\/s00018-026-06216-y"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_017","doi-asserted-by":"crossref","unstructured":"Danieli, A. and Martens, S. (2018). p62-mediated phase separation at the intersection of the ubiquitin-proteasome system and autophagy. J.\u00a0Cell Sci. 131, https:\/\/doi.org\/10.1242\/jcs.214304.","DOI":"10.1242\/jcs.214304"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_018","doi-asserted-by":"crossref","unstructured":"Decker, S.T. and Funai, K. (2024). Mitochondrial membrane lipids in the regulation of bioenergetic flux. Cell Metab. 36: 1963\u20131978, https:\/\/doi.org\/10.1016\/j.cmet.2024.07.024.","DOI":"10.1016\/j.cmet.2024.07.024"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_019","doi-asserted-by":"crossref","unstructured":"Demishtein, A., Fraiberg, M., Berko, D., Tirosh, B., Elazar, Z., and Navon, A. (2017). SQSTM1\/p62-mediated autophagy compensates for loss of proteasome polyubiquitin recruiting capacity. Autophagy 13: 1697\u20131708, https:\/\/doi.org\/10.1080\/15548627.2017.1356549.","DOI":"10.1080\/15548627.2017.1356549"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_020","doi-asserted-by":"crossref","unstructured":"Denais, C.M., Gilbert, R.M., Isermann, P., McGregor, A.L., te Lindert, M., Weigelin, B., Davidson, P.M., Friedl, P., Wolf, K., and Lammerding, J. (2016). Nuclear envelope rupture and repair during cancer cell migration. Science 352: 353\u2013358, https:\/\/doi.org\/10.1126\/science.aad7297.","DOI":"10.1126\/science.aad7297"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_021","doi-asserted-by":"crossref","unstructured":"Di Bona, M., Chen, Y., Agustinus, A.S., Mazzagatti, A., Duran, M.A., Deyell, M., Bronder, D., Hickling, J., Hong, C., Scipioni, L., et al.. (2024). Micronuclear collapse from oxidative damage. Science 385: eadj8691, https:\/\/doi.org\/10.1126\/science.adj8691.","DOI":"10.1126\/science.adj8691"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_022","doi-asserted-by":"crossref","unstructured":"Dikic, I. (2017). Proteasomal and autophagic degradation systems. Annu. Rev. Biochem. 86: 193\u2013224, https:\/\/doi.org\/10.1146\/annurev-biochem-061516-044908.","DOI":"10.1146\/annurev-biochem-061516-044908"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_023","doi-asserted-by":"crossref","unstructured":"Donnelly, N., Passerini, V., Durrbaum, M., Stingele, S., and Storchova, Z. (2014). HSF1 deficiency and impaired HSP90-dependent protein folding are hallmarks of aneuploid human cells. EMBO J. 33: 2374\u20132387, https:\/\/doi.org\/10.15252\/embj.201488648.","DOI":"10.15252\/embj.201488648"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_024","doi-asserted-by":"crossref","unstructured":"Duran, A., Amanchy, R., Linares, J.F., Joshi, J., Abu-Baker, S., Porollo, A., Hansen, M., Moscat, J., and Diaz-Meco, M.T. (2011). p62 is a key regulator of nutrient sensing in the mTORC1 pathway. Mol. Cell 44: 134\u2013146, https:\/\/doi.org\/10.1016\/j.molcel.2011.06.038.","DOI":"10.1016\/j.molcel.2011.06.038"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_025","doi-asserted-by":"crossref","unstructured":"Duran, A., Hernandez, E.D., Reina-Campos, M., Castilla, E.A., Subramaniam, S., Raghunandan, S., Roberts, L.R., Kisseleva, T., Karin, M., Diaz-Meco, M.T., et al.. (2016). p62\/SQSTM1 by binding to vitamin D receptor inhibits hepatic stellate cell activity, fibrosis, and liver cancer. Can. Cell 30: 595\u2013609, https:\/\/doi.org\/10.1016\/j.ccell.2016.09.004.","DOI":"10.1016\/j.ccell.2016.09.004"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_026","doi-asserted-by":"crossref","unstructured":"Duran, A., Linares, J.F., Galvez, A.S., Wikenheiser, K., Flores, J.M., Diaz-Meco, M.T., and Moscat, J. (2008). The signaling adaptor p62 is an important NF-kappaB mediator in tumorigenesis. Can. Cell 13: 343\u2013354, https:\/\/doi.org\/10.1016\/j.ccr.2008.02.001.","DOI":"10.1016\/j.ccr.2008.02.001"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_027","doi-asserted-by":"crossref","unstructured":"Durrbaum, M., Kuznetsova, A.Y., Passerini, V., Stingele, S., Stoehr, G., and Storchova, Z. (2014). Unique features of the transcriptional response to model aneuploidy in human cells. BMC Genomics 15: 139, https:\/\/doi.org\/10.1186\/1471-2164-15-139.","DOI":"10.1186\/1471-2164-15-139"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_028","doi-asserted-by":"crossref","unstructured":"Emin, D., Zhang, Y.P., Lobanova, E., Miller, A., Li, X., Xia, Z., Dakin, H., Sideris, D.I., Lam, J.Y.L., Ranasinghe, R.T., et al.. (2022). Small soluble \u03b1-synuclein aggregates are the toxic species in Parkinson\u2019s disease. Nat. Commun. 13: 5512, https:\/\/doi.org\/10.1038\/s41467-022-33252-6.","DOI":"10.1038\/s41467-022-33252-6"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_029","doi-asserted-by":"crossref","unstructured":"Ernst, R., Ballweg, S., and Levental, I. (2018). Cellular mechanisms of physicochemical membrane homeostasis. Curr. Opin. Cell Biol. 53: 44\u201351, https:\/\/doi.org\/10.1016\/j.ceb.2018.04.013.","DOI":"10.1016\/j.ceb.2018.04.013"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_030","doi-asserted-by":"crossref","unstructured":"Feng, X., Sun, D., Li, Y., Zhang, J., Liu, S., Zhang, D., Zheng, J., Xi, Q., Liang, H., Zhao, W., et al.. (2023). Local membrane source gathering by p62 body drives autophagosome formation. Nat. Commun. 14: 7338, https:\/\/doi.org\/10.1038\/s41467-023-42829-8.","DOI":"10.1038\/s41467-023-42829-8"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_031","doi-asserted-by":"crossref","unstructured":"Fischer, N., Preusse, C., Radke, J., Pehl, D., Allenbach, Y., Schneider, U., Feist, E., von Casteleyn, V., Hahn, K., Ruck, T., et al.. (2020). Sequestosome-1 (p62) expression reveals chaperone-assisted selective autophagy in immune-mediated necrotizing myopathies. Brain Pathol 30: 261\u2013271, https:\/\/doi.org\/10.1111\/bpa.12772.","DOI":"10.1111\/bpa.12772"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_032","doi-asserted-by":"crossref","unstructured":"Franzmann, T.M. and Alberti, S. (2019). Protein phase separation as a stress survival strategy. Cold Spring Harb. Perspect Biol. 11, https:\/\/doi.org\/10.1101\/cshperspect.a034058.","DOI":"10.1101\/cshperspect.a034058"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_033","doi-asserted-by":"crossref","unstructured":"Fu, A., Cohen-Kaplan, V., Avni, N., Livneh, I., and Ciechanover, A. (2021). p62-containing, proteolytically active nuclear condensates, increase the efficiency of the ubiquitin-proteasome system. Proc. Natl. Acad. Sci. U. S. A. 118, https:\/\/doi.org\/10.1073\/pnas.2107321118.","DOI":"10.1073\/pnas.2107321118"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_034","doi-asserted-by":"crossref","unstructured":"Fu, A., Luo, Z., Ziv, T., Bi, X., Lulu-Shimron, C., Cohen-Kaplan, V., and Ciechanover, A. (2024). Nuclear p62 condensates stabilize the promyelocytic leukemia nuclear bodies by sequestering their ubiquitin ligase RNF4. Proc. Natl. Acad. Sci. USA 121: e2414377121, https:\/\/doi.org\/10.1073\/pnas.2414377121.","DOI":"10.1073\/pnas.2414377121"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_035","doi-asserted-by":"crossref","unstructured":"Funai, K., Summers, S.A., and Rutter, J. (2020). Reign in the membrane: how common lipids govern mitochondrial function. Curr. Opin. Cell Biol. 63: 162\u2013173, https:\/\/doi.org\/10.1016\/j.ceb.2020.01.006.","DOI":"10.1016\/j.ceb.2020.01.006"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_036","doi-asserted-by":"crossref","unstructured":"Geetha, T. and Wooten, M.W. (2002). Structure and functional properties of the ubiquitin binding protein p62. FEBS Lett. 512: 19\u201324, https:\/\/doi.org\/10.1016\/s0014-5793(02)02286-x.","DOI":"10.1016\/S0014-5793(02)02286-X"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_037","doi-asserted-by":"crossref","unstructured":"Geisler, S., Holmstrom, K.M., Skujat, D., Fiesel, F.C., Rothfuss, O.C., Kahle, P.J., and Springer, W. (2010). PINK1\/Parkin-mediated mitophagy is dependent on VDAC1 and p62\/SQSTM1. Nat. Cell Biol. 12: 119\u2013131, https:\/\/doi.org\/10.1038\/ncb2012.","DOI":"10.1038\/ncb2012"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_038","doi-asserted-by":"crossref","unstructured":"Gidalevitz, T., Prahlad, V., and Morimoto, R.I. (2011). The stress of protein misfolding: from single cells to multicellular organisms. Cold Spring Harb. Perspect Biol. 3, https:\/\/doi.org\/10.1101\/cshperspect.a009704.","DOI":"10.1101\/cshperspect.a009704"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_039","doi-asserted-by":"crossref","unstructured":"Hartl, F.U., Bracher, A., and Hayer-Hartl, M. (2011). Molecular chaperones in protein folding and proteostasis. Nature 475: 324\u2013332, https:\/\/doi.org\/10.1038\/nature10317.","DOI":"10.1038\/nature10317"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_040","doi-asserted-by":"crossref","unstructured":"Hatch, E.M., Fischer, A.H., Deerinck, T.J., and Hetzer, M.W. (2013). Catastrophic nuclear envelope collapse in cancer cell micronuclei. Cell 154: 47\u201360, https:\/\/doi.org\/10.1016\/j.cell.2013.06.007.","DOI":"10.1016\/j.cell.2013.06.007"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_041","doi-asserted-by":"crossref","unstructured":"Hewitt, G., Carroll, B., Sarallah, R., Correia-Melo, C., Ogrodnik, M., Nelson, G., Otten, E.G., Manni, D., Antrobus, R., Morgan, B.A., et al. (2016). SQSTM1\/p62 mediates crosstalk between autophagy and the UPS in DNA repair. Autophagy 12: 1917\u20131930, https:\/\/doi.org\/10.1080\/15548627.2016.1210368.","DOI":"10.1080\/15548627.2016.1210368"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_042","doi-asserted-by":"crossref","unstructured":"Hewitt, G. and Korolchuk, V.I. (2017). Repair, reuse, recycle: the expanding role of autophagy in genome maintenance. Trends Cell Biol. 27: 340\u2013351, https:\/\/doi.org\/10.1016\/j.tcb.2016.11.011.","DOI":"10.1016\/j.tcb.2016.11.011"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_043","doi-asserted-by":"crossref","unstructured":"Hwang, S., Gustafsson, H.T., O\u2019Sullivan, C., Bisceglia, G., Huang, X., Klose, C., Schevchenko, A., Dickson, R.C., Cavaliere, P., Dephoure, N., et al. (2017). Serine-dependent sphingolipid synthesis is a metabolic liability of aneuploid cells. Cell Rep. 21: 3807\u20133818, https:\/\/doi.org\/10.1016\/j.celrep.2017.11.103.","DOI":"10.1016\/j.celrep.2017.11.103"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_044","doi-asserted-by":"crossref","unstructured":"Hwang, S., Russo, W., Cormier, J., Johnson, J., Martin, S., Ippolito, M.R., Cordone, S., Li, R., Zhu, L.J., Santaguida, S., et al. (2025). Sphingolipid synthesis maintains nuclear membrane integrity and genome stability during cell division. J.\u00a0Cell Biol. 224, https:\/\/doi.org\/10.1083\/jcb.202407209.","DOI":"10.1083\/jcb.202407209"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_045","doi-asserted-by":"crossref","unstructured":"Hwang, S., Williams, J.F., Kneissig, M., Lioudyno, M., Rivera, I., Helguera, P., Busciglio, J., Storchova, Z., King, M.C., and Torres, E.M. (2019). Suppressing aneuploidy-associated phenotypes improves the fitness of trisomy 21 cells. Cell Rep. 29: 2473\u20132488 e2475, https:\/\/doi.org\/10.1016\/j.celrep.2019.10.059.","DOI":"10.1016\/j.celrep.2019.10.059"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_046","doi-asserted-by":"crossref","unstructured":"Iavazzo, M., Cinque, L., Levantovsky, S., Morrone, C., Monfregola, J., Raimondi, A., Polishchuk, E., De Cegli, R., Carrella, D., Nusco, E., et al. (2026). TFEB coordinates autophagosome biogenesis and ribophagy during starvation via SQSTM1. Sci. Adv. 12: eaea9302, https:\/\/doi.org\/10.1126\/sciadv.aea9302.","DOI":"10.1126\/sciadv.aea9302"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_047","doi-asserted-by":"crossref","unstructured":"Ichimura, Y., Waguri, S., Sou, Y.S., Kageyama, S., Hasegawa, J., Ishimura, R., Saito, T., Yang, Y., Kouno, T., Fukutomi, T., et al. (2013). Phosphorylation of p62 activates the Keap1-Nrf2 pathway during selective autophagy. Mol. Cell 51: 618\u2013631, https:\/\/doi.org\/10.1016\/j.molcel.2013.08.003.","DOI":"10.1016\/j.molcel.2013.08.003"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_048","doi-asserted-by":"crossref","unstructured":"Itakura, E. and Mizushima, N. (2011). p62 targeting to the autophagosome formation site requires self-oligomerization but not LC3 binding. J.\u00a0Cell Biol. 192: 17\u201327, https:\/\/doi.org\/10.1083\/jcb.201009067.","DOI":"10.1083\/jcb.201009067"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_049","doi-asserted-by":"crossref","unstructured":"Jakobi, A.J., Huber, S.T., Mortensen, S.A., Schultz, S.W., Palara, A., Kuhm, T., Shrestha, B.K., Lamark, T., Hagen, W.J.H., Wilmanns, M., et al. (2020). Structural basis of p62\/SQSTM1 helical filaments and their role in cellular cargo uptake. Nat. Commun. 11: 440, https:\/\/doi.org\/10.1038\/s41467-020-14343-8.","DOI":"10.1038\/s41467-020-14343-8"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_050","doi-asserted-by":"crossref","unstructured":"Ji, C.H., Kim, H.Y., Heo, A.J., Lee, S.H., Lee, M.J., Kim, S.B., Srinivasrao, G., Mun, S.R., Cha-Molstad, H., Ciechanover, A., et al. (2019). The N-degron pathway mediates ER-phagy. Mol. Cell 75: 1058\u20131072 e1059, https:\/\/doi.org\/10.1016\/j.molcel.2019.06.028.","DOI":"10.1016\/j.molcel.2019.06.028"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_051","doi-asserted-by":"crossref","unstructured":"Kageyama, S., Gudmundsson, S.R., Sou, Y.S., Ichimura, Y., Tamura, N., Kazuno, S., Ueno, T., Miura, Y., Noshiro, D., Abe, M., et al. (2021). p62\/SQSTM1-droplet serves as a platform for autophagosome formation and anti-oxidative stress response. Nat. Commun. 12: 16, https:\/\/doi.org\/10.1038\/s41467-020-20185-1.","DOI":"10.1038\/s41467-020-20185-1"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_052","doi-asserted-by":"crossref","unstructured":"Kakanj, P., Bonse, M., Kshirsagar, A., Gokmen, A., Gaedke, F., Sen, A., Molla, B., Vogelsang, E., Schauss, A., Wodarz, A., et al. (2025). Retromer promotes the lysosomal turnover of mtDNA. Sci. Adv. 11: eadr6415, https:\/\/doi.org\/10.1126\/sciadv.adr6415.","DOI":"10.1126\/sciadv.adr6415"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_053","doi-asserted-by":"crossref","unstructured":"Kataura, T., Otten, E.G., Rabanal-Ruiz, Y., Adriaenssens, E., Urselli, F., Scialo, F., Fan, L., Smith, G.R., Dawson, W.M., Chen, X., et al. (2023). NDP52 acts as a redox sensor in PINK1\/Parkin-mediated mitophagy. EMBO J. 42: e111372, https:\/\/doi.org\/10.15252\/embj.2022111372.","DOI":"10.15252\/embj.2022111372"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_054","doi-asserted-by":"crossref","unstructured":"Kaushik, P., Herrmann, J.M., and Hansen, K.G. (2025). MitoStores: stress-induced aggregation of mitochondrial proteins. Biol. Chem. 406: 237\u2013249, https:\/\/doi.org\/10.1515\/hsz-2024-0148.","DOI":"10.1515\/hsz-2024-0148"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_055","doi-asserted-by":"crossref","unstructured":"Kim, Y.E., Hipp, M.S., Bracher, A., Hayer-Hartl, M., and Hartl, F.U. (2013). Molecular chaperone functions in protein folding and proteostasis. Annu. Rev. Biochem. 82: 323\u2013355, https:\/\/doi.org\/10.1146\/annurev-biochem-060208-092442.","DOI":"10.1146\/annurev-biochem-060208-092442"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_056","doi-asserted-by":"crossref","unstructured":"Kirkin, V., Lamark, T., Sou, Y.S., Bjorkoy, G., Nunn, J.L., Bruun, J.A., Shvets, E., McEwan, D.G., Clausen, T.H., Wild, P., et al.. (2009). A role for NBR1 in autophagosomal degradation of ubiquitinated substrates. Mol. Cell 33: 505\u2013516, https:\/\/doi.org\/10.1016\/j.molcel.2009.01.020.","DOI":"10.1016\/j.molcel.2009.01.020"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_057","doi-asserted-by":"crossref","unstructured":"Kirkin, V. and Rogov, V.V. (2019). A diversity of selective autophagy receptors determines the specificity of the autophagy pathway. Mol. Cell 76: 268\u2013285, https:\/\/doi.org\/10.1016\/j.molcel.2019.09.005.","DOI":"10.1016\/j.molcel.2019.09.005"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_058","doi-asserted-by":"crossref","unstructured":"Kitamura, A., Kubota, H., Pack, C.G., Matsumoto, G., Hirayama, S., Takahashi, Y., Kimura, H., Kinjo, M., Morimoto, R.I., and Nagata, K. (2006). Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state. Nat. Cell Biol. 8: 1163\u20131170, https:\/\/doi.org\/10.1038\/ncb1478.","DOI":"10.1038\/ncb1478"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_059","doi-asserted-by":"crossref","unstructured":"Kneissig, M., Keuper, K., de Pagter, M.S., van Roosmalen, M.J., Martin, J., Otto, H., Passerini, V., Campos Sparr, A., Renkens, I., Kropveld, F., et al.. (2019). Micronuclei-based model system reveals functional consequences of chromothripsis in human cells. eLife 8, https:\/\/doi.org\/10.7554\/eLife.50292.","DOI":"10.7554\/eLife.50292"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_060","doi-asserted-by":"crossref","unstructured":"Komatsu, M. (2022). p62 bodies: phase separation, NRF2 activation, and selective autophagic degradation. IUBMB Life 74: 1200\u20131208, https:\/\/doi.org\/10.1002\/iub.2689.","DOI":"10.1002\/iub.2689"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_061","doi-asserted-by":"crossref","unstructured":"Kostova, K.K., Hickey, K.L., Osuna, B.A., Hussmann, J.A., Frost, A., Weinberg, D.E., and Weissman, J.S. (2017). CAT-tailing as a fail-safe mechanism for efficient degradation of stalled nascent polypeptides. Sci. 357: 414\u2013417, https:\/\/doi.org\/10.1126\/science.aam7787.","DOI":"10.1126\/science.aam7787"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_062","doi-asserted-by":"crossref","unstructured":"Kramer, L., Dalheimer, N., Raschle, M., Storchova, Z., Pielage, J., Boos, F., and Herrmann, J.M. (2023). MitoStores: chaperone-controlled protein granules store mitochondrial precursors in the cytosol. EMBO J. 42: e112309, https:\/\/doi.org\/10.15252\/embj.2022112309.","DOI":"10.15252\/embj.2022112309"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_063","doi-asserted-by":"crossref","unstructured":"Krivega, M., Stiefel, C.M., Karbassi, S., Andersen, L.L., Chunduri, N.K., Donnelly, N., Pichlmair, A., and Storchova, Z. (2021). Genotoxic stress in constitutive trisomies induces autophagy and the innate immune response via the cGAS-STING pathway. Commun. Biol. 4: 831, https:\/\/doi.org\/10.1038\/s42003-021-02278-9.","DOI":"10.1038\/s42003-021-02278-9"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_064","doi-asserted-by":"crossref","unstructured":"Lallemand-Breitenbach, V. and de The, H. (2010). PML nuclear bodies. Cold Spring Harb. Perspect Biol. 2: a000661, https:\/\/doi.org\/10.1101\/cshperspect.a000661.","DOI":"10.1101\/cshperspect.a000661"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_065","doi-asserted-by":"crossref","unstructured":"Lamark, T., Perander, M., Outzen, H., Kristiansen, K., Overvatn, A., Michaelsen, E., Bjorkoy, G., and Johansen, T. (2003). Interaction codes within the family of mammalian Phox and Bem1p domain-containing proteins. J.\u00a0Biol. Chem. 278: 34568\u201334581, https:\/\/doi.org\/10.1074\/jbc.M303221200.","DOI":"10.1074\/jbc.M303221200"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_066","doi-asserted-by":"crossref","unstructured":"Lazarou, M., Sliter, D.A., Kane, L.A., Sarraf, S.A., Wang, C., Burman, J.L., Sideris, D.P., Fogel, A.I., and Youle, R.J. (2015). The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy. Nature 524: 309\u2013314, https:\/\/doi.org\/10.1038\/nature14893.","DOI":"10.1038\/nature14893"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_067","doi-asserted-by":"crossref","unstructured":"Le Guerroue, F., Eck, F., Jung, J., Starzetz, T., Mittelbronn, M., Kaulich, M., and Behrends, C. (2017). Autophagosomal content profiling reveals an LC3C-dependent piecemeal mitophagy pathway. Mol. Cell 68: 786\u2013796 e786, https:\/\/doi.org\/10.1016\/j.molcel.2017.10.029.","DOI":"10.1016\/j.molcel.2017.10.029"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_068","doi-asserted-by":"crossref","unstructured":"Levy, E., El Banna, N., Baille, D., Heneman-Masurel, A., Truchet, S., Rezaei, H., Huang, M.E., Beringue, V., Martin, D., and Vernis, L. (2019). Causative links between protein aggregation and oxidative stress: a review. Int. J.\u00a0Mol. Sci. 20, https:\/\/doi.org\/10.3390\/ijms20163896.","DOI":"10.3390\/ijms20163896"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_069","doi-asserted-by":"crossref","unstructured":"Li, R., Dalheimer, N., Muller, M.B.D., and Hartl, F.U. (2026). Single-molecule dynamics of the TRiC chaperonin system in\u00a0vivo. Nature 652: 481\u2013489, https:\/\/doi.org\/10.1038\/s41586-025-10073-3.","DOI":"10.1038\/s41586-025-10073-3"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_070","doi-asserted-by":"crossref","unstructured":"Li, M., Xiong, J., Yang, L., Huang, J., Zhang, Y., Liu, M., Wang, L., Ji, J., Zhao, Y., Zhu, W.G., et al.. (2022). Acetylation of p62 regulates base excision repair through interaction with APE1. Cell Rep. 40: 111116, https:\/\/doi.org\/10.1016\/j.celrep.2022.111116.","DOI":"10.1016\/j.celrep.2022.111116"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_071","doi-asserted-by":"crossref","unstructured":"Linares, J.F., Duran, A., Reina-Campos, M., Aza-Blanc, P., Campos, A., Moscat, J., and Diaz-Meco, M.T. (2015). Amino acid activation of mTORC1 by a PB1-domain-driven kinase complex cascade. Cell Rep. 12: 1339\u20131352, https:\/\/doi.org\/10.1016\/j.celrep.2015.07.045.","DOI":"10.1016\/j.celrep.2015.07.045"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_142","doi-asserted-by":"crossref","unstructured":"Liu, Q., Fong, B., Yoo, S., Unruh, J.R., Guo, F., Yu, Z., Chen, J., Si, K., Li, R., and Zhou, C. (2023). Nascent mitochondrial proteins initiate the localized condensation of cytosolic protein aggregates on the mitochondrial surface. Proc. Natl. Acad. Sci. U.S.A. 120: e2300475120.","DOI":"10.1073\/pnas.2300475120"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_072","doi-asserted-by":"crossref","unstructured":"Liu, W.J., Ye, L., Huang, W.F., Guo, L.J., Xu, Z.G., Wu, H.L., Yang, C., and Liu, H.F. (2016). p62 links the autophagy pathway and the ubiqutin-proteasome system upon ubiquitinated protein degradation. Cell. Mol. Biol. Lett. 21: 29, https:\/\/doi.org\/10.1186\/s11658-016-0031-z.","DOI":"10.1186\/s11658-016-0031-z"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_073","doi-asserted-by":"crossref","unstructured":"Lopez, A.R., Jorgensen, M.H., Havelund, J.F., Arendrup, F.S., Kolapalli, S.P., Nielsen, T.M., Pais, E., Beese, C.J., Abdul-Al, A., Vind, A.C., et al.. (2023). Autophagy-mediated control of ribosome homeostasis in oncogene-induced senescence. Cell Rep. 42: 113381, https:\/\/doi.org\/10.1016\/j.celrep.2023.113381.","DOI":"10.1016\/j.celrep.2023.113381"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_074","doi-asserted-by":"crossref","unstructured":"Lorincz, P. and Juhasz, G. (2020). Autophagosome-lysosome fusion. J.\u00a0Mol. Biol. 432: 2462\u20132482, https:\/\/doi.org\/10.1016\/j.jmb.2019.10.028.","DOI":"10.1016\/j.jmb.2019.10.028"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_075","doi-asserted-by":"crossref","unstructured":"Lyu, L., Lin, T.C., and McCarty, N. (2021). TRIM44 mediated p62 deubiquitination enhances DNA damage repair by increasing nuclear FLNA and 53BP1 expression. Oncogene 40: 5116\u20135130, https:\/\/doi.org\/10.1038\/s41388-021-01890-7.","DOI":"10.1038\/s41388-021-01890-7"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_076","doi-asserted-by":"crossref","unstructured":"Mannini, B., Cascella, R., Zampagni, M., van Waarde-Verhagen, M., Meehan, S., Roodveldt, C., Campioni, S., Boninsegna, M., Penco, A., Relini, A., et al.. (2012). Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers. Proc. Natl. Acad. Sci. USA 109: 12479\u201312484, https:\/\/doi.org\/10.1073\/pnas.1117799109.","DOI":"10.1073\/pnas.1117799109"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_077","doi-asserted-by":"crossref","unstructured":"Martin, S., Scorzoni, S., Cordone, S., Mazzagatti, A., Beznoussenko, G.V., Gunn, A.L., Di Bona, M., Eliezer, Y., Leor, G., Ben-Yishay, T., et al.. (2024). A p62-dependent rheostat dictates micronuclei catastrophe and chromosome rearrangements. Science 385: eadj7446, https:\/\/doi.org\/10.1126\/science.adj7446.","DOI":"10.1126\/science.adj7446"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_078","doi-asserted-by":"crossref","unstructured":"Mathew, R., Karp, C.M., Beaudoin, B., Vuong, N., Chen, G., Chen, H.Y., Bray, K., Reddy, A., Bhanot, G., Gelinas, C., et al.. (2009). Autophagy suppresses tumorigenesis through elimination of p62. Cell 137: 1062\u20131075, https:\/\/doi.org\/10.1016\/j.cell.2009.03.048.","DOI":"10.1016\/j.cell.2009.03.048"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_079","doi-asserted-by":"crossref","unstructured":"Mathew, R., Kongara, S., Beaudoin, B., Karp, C.M., Bray, K., Degenhardt, K., Chen, G., Jin, S., and White, E. (2007). Autophagy suppresses tumor progression by limiting chromosomal instability. Genes Dev. 21: 1367\u20131381, https:\/\/doi.org\/10.1101\/gad.1545107.","DOI":"10.1101\/gad.1545107"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_080","doi-asserted-by":"crossref","unstructured":"Miller, M. (2009). The importance of being flexible: the case of basic region leucine zipper transcriptional regulators. Curr. Protein Pept. Sci. 10: 244\u2013269, https:\/\/doi.org\/10.2174\/138920309788452164.","DOI":"10.2174\/138920309788452164"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_081","doi-asserted-by":"crossref","unstructured":"Moscat, J. and Diaz-Meco, M.T. (2009). p62 at the crossroads of autophagy, apoptosis, and cancer. Cell 137: 1001\u20131004, https:\/\/doi.org\/10.1016\/j.cell.2009.05.023.","DOI":"10.1016\/j.cell.2009.05.023"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_082","doi-asserted-by":"crossref","unstructured":"Moscat, J., Diaz-Meco, M.T., Albert, A., and Campuzano, S. (2006). Cell signaling and function organized by PB1 domain interactions. Mol. Cell 23: 631\u2013640, https:\/\/doi.org\/10.1016\/j.molcel.2006.08.002.","DOI":"10.1016\/j.molcel.2006.08.002"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_083","doi-asserted-by":"crossref","unstructured":"Moscat, J., Diaz-Meco, M.T., and Wooten, M.W. (2007). Signal integration and diversification through the p62 scaffold protein. Trends Biochem. Sci. 32: 95\u2013100, https:\/\/doi.org\/10.1016\/j.tibs.2006.12.002.","DOI":"10.1016\/j.tibs.2006.12.002"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_084","doi-asserted-by":"crossref","unstructured":"Narendra, D., Kane, L.A., Hauser, D.N., Fearnley, I.M., and Youle, R.J. (2010). p62\/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both. Autophagy 6: 1090\u20131106, https:\/\/doi.org\/10.4161\/auto.6.8.13426.","DOI":"10.4161\/auto.6.8.13426"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_085","doi-asserted-by":"crossref","unstructured":"Ngo, J.M., Williams, J.K., Temoche-Diaz, M.M., Murugupandiyan, A., and Schekman, R. (2026). p62 sorts Lupus La and selected microRNAs into breast cancer-derived exosomes. J.\u00a0Cell Biol. 225, https:\/\/doi.org\/10.1083\/jcb.202503087.","DOI":"10.1083\/jcb.202503087"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_086","doi-asserted-by":"crossref","unstructured":"Ohashi, A., Ohori, M., Iwai, K., Nakayama, Y., Nambu, T., Morishita, D., Kawamoto, T., Miyamoto, M., Hirayama, T., Okaniwa, M., et al.. (2015). Aneuploidy generates proteotoxic stress and DNA damage concurrently with p53-mediated post-mitotic apoptosis in SAC-impaired cells. Nat. Commun. 6: 7668, https:\/\/doi.org\/10.1038\/ncomms8668.","DOI":"10.1038\/ncomms8668"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_087","doi-asserted-by":"crossref","unstructured":"Padmanabhan, S. and Manjithaya, R. (2020). Facets of autophagy based unconventional protein secretion\u00a0\u2013\u00a0the road less traveled. Front. Mol. Biosci. 7: 586483, https:\/\/doi.org\/10.3389\/fmolb.2020.586483.","DOI":"10.3389\/fmolb.2020.586483"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_088","doi-asserted-by":"crossref","unstructured":"Pankiv, S., Clausen, T.H., Lamark, T., Brech, A., Bruun, J.A., Outzen, H., Overvatn, A., Bjorkoy, G., and Johansen, T. (2007). p62\/SQSTM1 binds directly to Atg8\/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy. J.\u00a0Biol. Chem. 282: 24131\u201324145, https:\/\/doi.org\/10.1074\/jbc.M702824200.","DOI":"10.1074\/jbc.M702824200"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_089","doi-asserted-by":"crossref","unstructured":"Pankiv, S., Lamark, T., Bruun, J.A., Overvatn, A., Bjorkoy, G., and Johansen, T. (2010). Nucleocytoplasmic shuttling of p62\/SQSTM1 and its role in recruitment of nuclear polyubiquitinated proteins to promyelocytic leukemia bodies. J.\u00a0Biol. Chem. 285: 5941\u20135953, https:\/\/doi.org\/10.1074\/jbc.M109.039925.","DOI":"10.1074\/jbc.M109.039925"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_090","doi-asserted-by":"crossref","unstructured":"Park, I., Chung, J., Walsh, C.T., Yun, Y., Strominger, J.L., and Shin, J. (1995). Phosphotyrosine-independent binding of a 62-kDa protein to the src homology 2 (SH2) domain of p56lck and its regulation by phosphorylation of Ser-59 in the lck unique N-terminal region. Proc. Natl. Acad. Sci. USA 92: 12338\u201312342, https:\/\/doi.org\/10.1073\/pnas.92.26.12338.","DOI":"10.1073\/pnas.92.26.12338"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_091","doi-asserted-by":"crossref","unstructured":"Pfanner, N., den Brave, F., and Becker, T. (2025). Mitochondrial protein import stress. Nat. Cell Biol. 27: 188\u2013201, https:\/\/doi.org\/10.1038\/s41556-024-01590-w.","DOI":"10.1038\/s41556-024-01590-w"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_092","doi-asserted-by":"crossref","unstructured":"Pfanner, N., Warscheid, B., and Wiedemann, N. (2019). Mitochondrial proteins: from biogenesis to functional networks. Nat. Rev. Mol. Cell Biol. 20: 267\u2013284, https:\/\/doi.org\/10.1038\/s41580-018-0092-0.","DOI":"10.1038\/s41580-018-0092-0"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_093","doi-asserted-by":"crossref","unstructured":"Ponpuak, M., Mandell, M.A., Kimura, T., Chauhan, S., Cleyrat, C., and Deretic, V. (2015). Secretory autophagy. Curr. Opin. Cell Biol. 35: 106\u2013116, https:\/\/doi.org\/10.1016\/j.ceb.2015.04.016.","DOI":"10.1016\/j.ceb.2015.04.016"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_094","doi-asserted-by":"crossref","unstructured":"Ramesh Babu, J., Lamar Seibenhener, M., Peng, J., Strom, A.L., Kemppainen, R., Cox, N., Zhu, H., Wooten, M.C., Diaz-Meco, M.T., Moscat, J., et al.. (2008). Genetic inactivation of p62 leads to accumulation of hyperphosphorylated tau and neurodegeneration. J.\u00a0Neurochem. 106: 107\u2013120, https:\/\/doi.org\/10.1111\/j.1471-4159.2008.05340.x.","DOI":"10.1111\/j.1471-4159.2008.05340.x"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_095","doi-asserted-by":"crossref","unstructured":"Reinhard, J., Starke, L., Klose, C., Haberkant, P., Hammaren, H., Stein, F., Klein, O., Berhorst, C., Stumpf, H., Saenz, J.P., et al.. (2024). MemPrep, a new technology for isolating organellar membranes\u00a0provides fingerprints of lipid bilayer stress. EMBO J. 43: 1653\u20131685, https:\/\/doi.org\/10.1038\/s44318-024-00063-y.","DOI":"10.1038\/s44318-024-00063-y"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_096","doi-asserted-by":"crossref","unstructured":"Rello-Varona, S., Lissa, D., Shen, S., Niso-Santano, M., Senovilla, L., Marino, G., Vitale, I., Jemaa, M., Harper, F., Pierron, G., et al.. (2012). Autophagic removal of micronuclei. Cell Cycle 11: 170\u2013176, https:\/\/doi.org\/10.4161\/cc.11.1.18564.","DOI":"10.4161\/cc.11.1.18564"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_097","doi-asserted-by":"crossref","unstructured":"Richter-Dennerlein, R., Oeljeklaus, S., Lorenzi, I., Ronsor, C., Bareth, B., Schendzielorz, A.B., Wang, C., Warscheid, B., Rehling, P., and Dennerlein, S. (2016). Mitochondrial protein synthesis adapts to influx of nuclear-encoded protein. Cell 167: 471\u2013483 e410, https:\/\/doi.org\/10.1016\/j.cell.2016.09.003.","DOI":"10.1016\/j.cell.2016.09.003"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_098","doi-asserted-by":"crossref","unstructured":"Rinauro, D.J., Chiti, F., Vendruscolo, M., and Limbocker, R. (2024). Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases. Mol. Neurodegener 19: 20, https:\/\/doi.org\/10.1186\/s13024-023-00651-2.","DOI":"10.1186\/s13024-023-00651-2"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_099","doi-asserted-by":"crossref","unstructured":"Romanauska, A. and Kohler, A. (2023). Lipid saturation controls nuclear envelope function. Nat. Cell Biol. 25: 1290\u20131302, https:\/\/doi.org\/10.1038\/s41556-023-01207-8.","DOI":"10.1038\/s41556-023-01207-8"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_141","doi-asserted-by":"crossref","unstructured":"Ruan, L., Zhou, C., Jin, E., Kucharavy, A., Zhang, Y., Wen, Z., Florens, L., and Li, R. (2017). Cytosolic proteostasis through importing of misfolded proteins into mitochondria. Nature 543: 443\u2013446.","DOI":"10.1038\/nature21695"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_100","doi-asserted-by":"crossref","unstructured":"Santaguida, S., Vasile, E., White, E., and Amon, A. (2015). Aneuploidy-induced cellular stresses limit autophagic degradation. Genes Dev. 29: 2010\u20132021, https:\/\/doi.org\/10.1101\/gad.269118.115.","DOI":"10.1101\/gad.269118.115"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_101","doi-asserted-by":"crossref","unstructured":"Sanz, L., Diaz-Meco, M.T., Nakano, H., and Moscat, J. (2000). The atypical PKC-interacting protein p62 channels NF-\u03baB activation by the IL-1-TRAF6 pathway. EMBO J. 19: 1576\u20131586, https:\/\/doi.org\/10.1093\/emboj\/19.7.1576.","DOI":"10.1093\/emboj\/19.7.1576"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_102","doi-asserted-by":"crossref","unstructured":"Sanz, L., Sanchez, P., Lallena, M.J., Diaz-Meco, M.T., and Moscat, J. (1999). The interaction of p62 with RIP links the atypical PKCs to NF-\u03baB activation. EMBO J. 18: 3044\u20133053, https:\/\/doi.org\/10.1093\/emboj\/18.11.3044.","DOI":"10.1093\/emboj\/18.11.3044"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_103","doi-asserted-by":"crossref","unstructured":"Schuck, S., Prinz, W.A., Thorn, K.S., Voss, C., and Walter, P. (2009). Membrane expansion alleviates endoplasmic reticulum stress independently of the unfolded protein response. J.\u00a0Cell Biol. 187: 525\u2013536, https:\/\/doi.org\/10.1083\/jcb.200907074.","DOI":"10.1083\/jcb.200907074"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_104","doi-asserted-by":"crossref","unstructured":"Seibenhener, M.L., Babu, J.R., Geetha, T., Wong, H.C., Krishna, N.R., and Wooten, M.W. (2004). Sequestosome 1\/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation. Mol. Cell. Biol. 24: 8055\u20138068, https:\/\/doi.org\/10.1128\/MCB.24.18.8055-8068.2004.","DOI":"10.1128\/MCB.24.18.8055-8068.2004"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_105","doi-asserted-by":"crossref","unstructured":"Seibenhener, M.L., Du, Y., Diaz-Meco, M.T., Moscat, J., Wooten, M.C., and Wooten, M.W. (2013). A role for sequestosome 1\/p62 in mitochondrial dynamics, import and genome integrity. Biochim. Biophys. Acta 1833: 452\u2013459, https:\/\/doi.org\/10.1016\/j.bbamcr.2012.11.004.","DOI":"10.1016\/j.bbamcr.2012.11.004"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_106","doi-asserted-by":"crossref","unstructured":"Sen, A., Kallabis, S., Gaedke, F., Jungst, C., Boix, J., Nuchel, J., Maliphol, K., Hofmann, J., Schauss, A.C., Kruger, M., et al.. (2022). Mitochondrial membrane proteins and VPS35 orchestrate selective removal of mtDNA. Nat. Commun. 13: 6704, https:\/\/doi.org\/10.1038\/s41467-022-34205-9.","DOI":"10.1038\/s41467-022-34205-9"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_107","doi-asserted-by":"crossref","unstructured":"Shin, J. (1998). P62 and the sequestosome, a novel mechanism for protein metabolism. Arch Pharm. Res. 21: 629\u2013633, https:\/\/doi.org\/10.1007\/BF02976748.","DOI":"10.1007\/BF02976748"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_108","doi-asserted-by":"crossref","unstructured":"Shin, W.H., Park, J.H., and Chung, K.C. (2020). The central regulator p62\u00a0between ubiquitin proteasome system and autophagy and its\u00a0role in the mitophagy and Parkinson\u2019s disease. BMB Rep. 53: 56\u201363, https:\/\/doi.org\/10.5483\/BMBRep.2020.53.1.283.","DOI":"10.5483\/BMBRep.2020.53.1.283"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_109","doi-asserted-by":"crossref","unstructured":"Singla, S., Iwamoto-Stohl, L.K., Zhu, M., and Zernicka-Goetz, M. (2020). Autophagy-mediated apoptosis eliminates aneuploid cells in a mouse model of chromosome mosaicism. Nat. Commun. 11: 2958, https:\/\/doi.org\/10.1038\/s41467-020-16796-3.","DOI":"10.1038\/s41467-020-16796-3"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_110","doi-asserted-by":"crossref","unstructured":"Sitron, C.S. and Brandman, O. (2019). CAT tails drive degradation of stalled polypeptides on and off the ribosome. Nat. Struct. Mol. Biol. 26: 450\u2013459, https:\/\/doi.org\/10.1038\/s41594-019-0230-1.","DOI":"10.1038\/s41594-019-0230-1"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_111","doi-asserted-by":"crossref","unstructured":"Stingele, S., Stoehr, G., Peplowska, K., Cox, J., Mann, M., and Storchova, Z. (2012). Global analysis of genome, transcriptome and proteome reveals the response to aneuploidy in human cells. Mol. Syst. Biol. 8: 608, https:\/\/doi.org\/10.1038\/msb.2012.40.","DOI":"10.1038\/msb.2012.40"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_112","doi-asserted-by":"crossref","unstructured":"Sun, D., Wu, R., Zheng, J., Li, P., and Yu, L. (2018). Polyubiquitin chain-induced p62 phase separation drives autophagic cargo segregation. Cell Res. 28: 405\u2013415, https:\/\/doi.org\/10.1038\/s41422-018-0017-7.","DOI":"10.1038\/s41422-018-0017-7"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_113","doi-asserted-by":"crossref","unstructured":"Sun, S., Xin, J., Zhang, Y., Yang, B., Su, D., Ni, R., Ma, Q., Li, N., Ma, G., Peng, Q., et al.. (2026). p62\/SQSTM1 condensation modulates mitochondrial clustering to participate in mitochondrial quality control. Aging Cell 25: e70402, https:\/\/doi.org\/10.1111\/acel.70402.","DOI":"10.1111\/acel.70402"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_114","doi-asserted-by":"crossref","unstructured":"Tabara, L.C., Burr, S.P., Frison, M., Chowdhury, S.R., Paupe, V., Nie, Y., Johnson, M., Villar-Azpillaga, J., Viegas, F., Segawa, M., et al.. (2024). MTFP1 controls mitochondrial fusion to regulate inner membrane quality control and maintain mtDNA levels. Cell 187: 3619\u20133637 e3627, https:\/\/doi.org\/10.1016\/j.cell.2024.05.017.","DOI":"10.1016\/j.cell.2024.05.017"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_115","doi-asserted-by":"crossref","unstructured":"Todoric, J., Antonucci, L., Di Caro, G., Li, N., Wu, X., Lytle, N.K., Dhar, D., Banerjee, S., Fagman, J.B., Browne, C.D., et al.. (2017). Stress-activated NRF2-MDM2 cascade controls neoplastic progression in pancreas. Cancer Cell 32: 824\u2013839 e828, https:\/\/doi.org\/10.1016\/j.ccell.2017.10.011.","DOI":"10.1016\/j.ccell.2017.10.011"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_116","doi-asserted-by":"crossref","unstructured":"Turco, E., Witt, M., Abert, C., Bock-Bierbaum, T., Su, M.Y., Trapannone, R., Sztacho, M., Danieli, A., Shi, X., Zaffagnini, G., et al.. (2019). FIP200 claw domain binding to p62 promotes autophagosome formation at ubiquitin condensates. Mol. Cell 74: 330\u2013346 e311, https:\/\/doi.org\/10.1016\/j.molcel.2019.01.035.","DOI":"10.1016\/j.molcel.2019.01.035"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_117","doi-asserted-by":"crossref","unstructured":"Vigan\u00f2, S., Ippolito, M.R., Scorzoni, S., Barrio, L., Loffreda, A., Rodriguez-Mu\u00f1oz, M., Donzel, D., Eliezer, Y., Pontano Vaites, L., Paulo, J.A., et al.. (2026). Ribosome quality control mitigates proteotoxic stress in aneuploid cells. bioRxiv 2001.2019.700285. https:\/\/doi.org\/10.64898\/2026.01.19.700285.","DOI":"10.64898\/2026.01.19.700285"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_118","doi-asserted-by":"crossref","unstructured":"Wagh, A.R. and Glickman, M.H. (2025). Molecular mechanisms underlying p62-dependent secretion of the Alzheimer-associated ubiquitin variant UBB(+1). Proc. Natl. Acad. Sci. USA 122: e2504528122, https:\/\/doi.org\/10.1073\/pnas.2504528122.","DOI":"10.1073\/pnas.2504528122"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_119","doi-asserted-by":"crossref","unstructured":"Wang, L., Howell, M.E.A., Sparks-Wallace, A., Hawkins, C., Nicksic, C.A., Kohne, C., Hall, K.H., Moorman, J.P., Yao, Z.Q., and Ning, S., et al.. (2019). p62-mediated selective autophagy endows virus-transformed cells with insusceptibility to DNA damage under oxidative stress. PLoS Pathog. 15: e1007541, https:\/\/doi.org\/10.1371\/journal.ppat.1007541.","DOI":"10.1371\/journal.ppat.1007541"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_143","doi-asserted-by":"crossref","unstructured":"Wang, Y., Ruan, L., Zhu, J., Zhang, X., Chang, A.C.-C., Tomaszewski, A., and Li, R. (2024). Metabolic regulation of misfolded protein import into mitochondria. eLife 12. https:\/\/doi.org\/10.7554\/elife.87518.","DOI":"10.7554\/eLife.87518"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_120","doi-asserted-by":"crossref","unstructured":"Wang, Y., Zhang, N., Zhang, L., Li, R., Fu, W., Ma, K., Li, X., Wang, L., Wang, J., Zhang, H., et al.. (2016). Autophagy regulates chromatin ubiquitination in DNA damage response through elimination of SQSTM1\/p62. Mol. Cell 63: 34\u201348, https:\/\/doi.org\/10.1016\/j.molcel.2016.05.027.","DOI":"10.1016\/j.molcel.2016.05.027"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_121","doi-asserted-by":"crossref","unstructured":"Wang, Y., Zhu, W.G., and Zhao, Y. (2017). Autophagy substrate SQSTM1\/p62 regulates chromatin ubiquitination during the DNA damage response. Autophagy 13: 212\u2013213, https:\/\/doi.org\/10.1080\/15548627.2016.1245262.","DOI":"10.1080\/15548627.2016.1245262"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_122","doi-asserted-by":"crossref","unstructured":"Wankhede, N.L., Kale, M.B., Upaganlawar, A.B., Taksande, B.G., Umekar, M.J., Behl, T., Abdellatif, A.A.H., Bhaskaran, P.M., Dachani, S.R., Sehgal, A., et al.. (2022). Involvement of molecular chaperone in protein-misfolding brain diseases. Biomed. Pharmacother 147: 112647, https:\/\/doi.org\/10.1016\/j.biopha.2022.112647.","DOI":"10.1016\/j.biopha.2022.112647"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_123","doi-asserted-by":"crossref","unstructured":"Watanabe, Y. and Tanaka, M. (2011). p62\/SQSTM1 in autophagic clearance of a non-ubiquitylated substrate. J.\u00a0Cell Sci. 124: 2692\u20132701, https:\/\/doi.org\/10.1242\/jcs.081232.","DOI":"10.1242\/jcs.081232"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_124","doi-asserted-by":"crossref","unstructured":"Wu, Z., Tantray, I., Lim, J., Chen, S., Li, Y., Davis, Z., Sitron, C., Dong, J., Gispert, S., Auburger, G., et al.. (2019). MISTERMINATE mechanistically links mitochondrial dysfunction with proteostasis failure. Mol. Cell 75: 835\u2013848 e838, https:\/\/doi.org\/10.1016\/j.molcel.2019.06.031.","DOI":"10.1016\/j.molcel.2019.06.031"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_125","doi-asserted-by":"crossref","unstructured":"Wu, Z., Wang, Y., Lim, J., Liu, B., Li, Y., Vartak, R., Stankiewicz, T., Montgomery, S., and Lu, B. (2018). Ubiquitination of ABCE1 by NOT4 in response to mitochondrial damage links co-translational quality control to PINK1-directed mitophagy. Cell Metab. 28: 130\u2013144 e137, https:\/\/doi.org\/10.1016\/j.cmet.2018.05.007.","DOI":"10.1016\/j.cmet.2018.05.007"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_126","doi-asserted-by":"crossref","unstructured":"Wurzer, B., Zaffagnini, G., Fracchiolla, D., Turco, E., Abert, C., Romanov, J., and Martens, S. (2015). Oligomerization of p62 allows for selection of ubiquitinated cargo and isolation membrane during selective autophagy. eLife 4: e08941, https:\/\/doi.org\/10.7554\/eLife.08941.","DOI":"10.7554\/eLife.08941"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_127","doi-asserted-by":"crossref","unstructured":"Xiao, S., Yu, Y., Liao, M., Song, D., Xu, X., Tian, L., Zhang, R., Lyu, H., Guo, D., Zhang, Q., et al.. (2025). Post-translational modification of p62: roles and regulations in autophagy. Cells 14, https:\/\/doi.org\/10.3390\/cells14131016.","DOI":"10.3390\/cells14131016"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_128","doi-asserted-by":"crossref","unstructured":"Xu, J., Yang, K.C., Go, N.E., Colborne, S., Ho, C.J., Hosseini-Beheshti, E., Lystad, A.H., Simonsen, A., Guns, E.T., Morin, G.B., et al.. (2022). Chloroquine treatment induces secretion of autophagy-related proteins and inclusion of Atg8-family proteins in distinct extracellular vesicle populations. Autophagy 18: 2547\u20132560, https:\/\/doi.org\/10.1080\/15548627.2022.2039535.","DOI":"10.1080\/15548627.2022.2039535"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_129","doi-asserted-by":"crossref","unstructured":"Yam, A.Y., Xia, Y., Lin, H.T., Burlingame, A., Gerstein, M., and Frydman, J. (2008). Defining the TRiC\/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies. Nat. Struct. Mol. Biol. 15: 1255\u20131262, https:\/\/doi.org\/10.1038\/nsmb.1515.","DOI":"10.1038\/nsmb.1515"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_130","doi-asserted-by":"crossref","unstructured":"Yamada, T., Murata, D., Adachi, Y., Itoh, K., Kameoka, S., Igarashi, A., Kato, T., Araki, Y., Huganir, R.L., Dawson, T.M., et al.. (2018). Mitochondrial stasis reveals p62-mediated ubiquitination in parkin-independent mitophagy and mitigates nonalcoholic fatty liver disease. Cell Metab. 28: 588\u2013604 e585, https:\/\/doi.org\/10.1016\/j.cmet.2018.06.014.","DOI":"10.1016\/j.cmet.2018.06.014"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_131","doi-asserted-by":"crossref","unstructured":"Yang, H., Ni, H.M., Guo, F., Ding, Y., Shi, Y.H., Lahiri, P., Frohlich, L.F., Rulicke, T., Smole, C., Schmidt, V.C., et al.. (2016). Sequestosome 1\/p62 protein is associated with autophagic removal of excess hepatic endoplasmic reticulum in mice. J.\u00a0Biol. Chem. 291: 18663\u201318674, https:\/\/doi.org\/10.1074\/jbc.M116.739821.","DOI":"10.1074\/jbc.M116.739821"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_132","doi-asserted-by":"crossref","unstructured":"Yang, X., Zhou, Y., Zhang, B., Tao, X., Qi, W., and Wu, H. (2025). Irradiation-induced increase in nuclear p62 levels contributes to chromosomal fragmentation and chromothripsis. Int. J.\u00a0Surg. 111: 5660\u20135663, https:\/\/doi.org\/10.1097\/JS9.0000000000002643.","DOI":"10.1097\/JS9.0000000000002643"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_133","doi-asserted-by":"crossref","unstructured":"You, Z., Jiang, W.X., Qin, L.Y., Gong, Z., Wan, W., Li, J., Wang, Y., Zhang, H., Peng, C., Zhou, T., et al.. (2019). Requirement for p62 acetylation in the aggregation of ubiquitylated proteins under nutrient stress. Nat. Commun. 10: 5792, https:\/\/doi.org\/10.1038\/s41467-019-13718-w.","DOI":"10.1038\/s41467-019-13718-w"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_134","doi-asserted-by":"crossref","unstructured":"Yu, X., Eischeid-Scholz, H., Meder, L., Kondylis, V., Buttner, R., and Odenthal, M. (2022). SQSTM1\/p62 promotes miR-198 loading into extracellular vesicles and its autophagy-related secretion. Hum. Cell. 35: 1766\u20131784, https:\/\/doi.org\/10.1007\/s13577-022-00765-7.","DOI":"10.1007\/s13577-022-00765-7"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_135","doi-asserted-by":"crossref","unstructured":"Zaffagnini, G., Savova, A., Danieli, A., Romanov, J., Tremel, S., Ebner, M., Peterbauer, T., Sztacho, M., Trapannone, R., Tarafder, A.K., et al.. (2018). p62 filaments capture and present ubiquitinated cargos for\u00a0autophagy. EMBO J. 37, https:\/\/doi.org\/10.15252\/embj.201798308.","DOI":"10.15252\/embj.201798308"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_136","doi-asserted-by":"crossref","unstructured":"Zellner, S., Schifferer, M., and Behrends, C. (2021). Systematically defining selective autophagy receptor-specific cargo using autophagosome content profiling. Mol. Cell 81: 1337\u20131354 e1338, https:\/\/doi.org\/10.1016\/j.molcel.2021.01.009.","DOI":"10.1016\/j.molcel.2021.01.009"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_137","doi-asserted-by":"crossref","unstructured":"Zeng, X., Zhang, Y.D., Ma, R.Y., Chen, Y.J., Xiang, X.M., Hou, D.Y., Li, X.H., Huang, H., Li, T., and Duan, C.Y., et al.. (2022). Activated Drp1 regulates p62-mediated autophagic flux and aggravates inflammation in cerebral ischemia-reperfusion via the ROS-RIP1\/RIP3-exosome axis. Mil. Med. Res. 9: 25, https:\/\/doi.org\/10.1186\/s40779-022-00383-2.","DOI":"10.1186\/s40779-022-00383-2"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_138","doi-asserted-by":"crossref","unstructured":"Zhang, J., He, X., and Mi, N. (2024). A lipid membrane-centric role of the SQSTM1\/p62 body during autophagosome formation. Autophagy 20: 1192\u20131193, https:\/\/doi.org\/10.1080\/15548627.2023.2297622.","DOI":"10.1080\/15548627.2023.2297622"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_139","doi-asserted-by":"crossref","unstructured":"Zhang, Y., Mun, S.R., Linares, J.F., Ahn, J., Towers, C.G., Ji, C.H., Fitzwalter, B.E., Holden, M.R., Mi, W., Shi, X., et al.. (2018). ZZ-dependent regulation of p62\/SQSTM1 in autophagy. Nat. Commun. 9: 4373, https:\/\/doi.org\/10.1038\/s41467-018-06878-8.","DOI":"10.1038\/s41467-018-06878-8"},{"key":"2026092806555689340_j_hsz-2026-0146_ref_140","doi-asserted-by":"crossref","unstructured":"Zhong, Z., Umemura, A., Sanchez-Lopez, E., Liang, S., Shalapour, S., Wong, J., He, F., Boassa, D., Perkins, G., Ali, S.R., et al.. (2016). NF-\u03baB restricts inflammasome activation via elimination of damaged mitochondria. Cell 164: 896\u2013910, https:\/\/doi.org\/10.1016\/j.cell.2015.12.057.","DOI":"10.1016\/j.cell.2015.12.057"}],"container-title":["Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.degruyterbrill.com\/document\/doi\/10.1515\/hsz-2026-0146\/xml","content-type":"application\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.degruyterbrill.com\/document\/doi\/10.1515\/hsz-2026-0146\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T06:56:53Z","timestamp":1790578613000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.degruyterbrill.com\/document\/doi\/10.1515\/hsz-2026-0146\/html"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,29]]},"references-count":143,"alternative-id":["10.1515\/hsz-2026-0146"],"URL":"https:\/\/doi.org\/10.1515\/hsz-2026-0146","relation":{},"ISSN":["1431-6730","1437-4315"],"issn-type":[{"value":"1431-6730","type":"print"},{"value":"1437-4315","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,9,29]]}}}