Prohibitins, Phb1 and Phb2, function as Atg8 receptors to support yeast mitophagy and also play a negative regulatory role in Atg32 processing

References

• Nijtmans LGJ. Prohibitins act as a membrane-bound chaperone for the stabilization of mitochondrial proteins. Embo J. 2000;19(11):2444–2451. doi: 10.1093/emboj/19.11.2444
   PubMed Web of Science ®Google Scholar
• Tatsuta T, Model K, Langer T. Formation of membrane-bound ring complexes by prohibitins in mitochondria. Mol Biol Cell. 2005;16(1):248–259. doi: 10.1091/mbc.e04-09-0807
   PubMed Web of Science ®Google Scholar
• Berger KH, Yaffe MP. Prohibitin family members interact genetically with mitochondrial inheritance components in Saccharomyces cerevisiae. Mol Cell Biol. 1998;18(7):4043–4052. doi: 10.1128/MCB.18.7.4043
   PubMed Web of Science ®Google Scholar
• Wei Y, Chiang WC, Sumpter R, et al. Prohibitin 2 Is an inner mitochondrial membrane mitophagy receptor. Cell. 2017;168(1–2):224–238.e10. doi: 10.1016/j.cell.2016.11.042
   PubMed Web of Science ®Google Scholar
• Alula KM, Delgado-Deida Y, Callahan R, et al. Inner mitochondrial membrane protein prohibitin 1 mediates Nix-induced, Parkin-independent mitophagy. Sci Rep. 2023;13(1):18. doi: 10.1038/s41598-022-26775-x
   PubMed Web of Science ®Google Scholar
• Yan C, Gong L, Chen L, et al. PHB2 (prohibitin 2) promotes PINK1-PRKN/Parkin-dependent mitophagy by the PARL-PGAM5-PINK1 axis. Autophagy. 2020;16(3):419–434. doi: 10.1080/15548627.2019.1628520
   PubMed Web of Science ®Google Scholar
• Choubey V, Zeb A, Kaasik A. Molecular mechanisms and regulation of mammalian mitophagy. Cells. 2021;11(1):38. doi: 10.3390/cells11010038
   PubMed Web of Science ®Google Scholar
• Yamano K, Youle RJ. PINK1 is degraded through the N-end rule pathway. Autophagy. 2013;9(11):1758–1769. doi: 10.4161/auto.24633
   PubMed Web of Science ®Google Scholar
• Sekine S, Youle RJ. PINK1 import regulation; a fine system to convey mitochondrial stress to the cytosol. BMC Biol. 2018;16(1):2. doi: 10.1186/s12915-017-0470-7
   PubMed Web of Science ®Google Scholar
• Jin SM, Lazarou M, Wang C, et al. Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL. J Cell Bio. 2010;191(5):933–942. doi: 10.1083/jcb.201008084
   PubMed Web of Science ®Google Scholar
• Vives-Bauza C, Zhou C, Huang Y, et al. PINK1-dependent recruitment of parkin to mitochondria in mitophagy. Proc Natl Acad Sci, USA. 2010;107(1):378–383. doi: 10.1073/pnas.0911187107
   PubMed Web of Science ®Google Scholar
• Lazarou M, Narendra DP, Jin SM, et al. PINK1 drives Parkin self-association and HECT-like E3 activity upstream of mitochondrial binding. J Cell Bio. 2013;200(2):163–172. doi: 10.1083/jcb.201210111
   PubMed Web of Science ®Google Scholar
• Kazlauskaite A, Kondapalli C, Gourlay R, et al. Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65. Biochem J. 2014;460(1):127–139. doi: 10.1042/BJ20140334
   PubMed Web of Science ®Google Scholar
• Yoshii SR, Kishi C, Ishihara N, et al. Parkin mediates proteasome-dependent protein degradation and rupture of the outer mitochondrial membrane. J Biol Chem. 2011;286(22):19630–19640. doi: 10.1074/jbc.M110.209338
   PubMed Web of Science ®Google Scholar
• Coates PJ, Jamieson DJ, Smart K, et al. The prohibitin family of mitochondrial proteins regulate replicative lifespan. Curr Biol. 1997;7(8):607–610. doi: 10.1016/S0960-9822(06)00261-2
   PubMed Web of Science ®Google Scholar
• Bernhardt D, Müller M, Reichert AS, et al. Simultaneous impairment of mitochondrial fission and fusion reduces mitophagy and shortens replicative lifespan. Sci Rep. 2015;5(1):7885. doi: 10.1038/srep07885
   PubMedGoogle Scholar
• Sanz MA, Tsang WY, Willems EM, et al. The mitochondrial prohibitin complex is essential for embryonic viability and germline function in caenorhabditis elegans. J Biol Chem. 2003;278(34):32091–32099. doi: 10.1074/jbc.M304877200
   PubMed Web of Science ®Google Scholar
• Okamoto K, Kondo-Okamoto N, Ohsumi Y. Mitochondria-anchored receptor Atg32 mediates degradation of mitochondria via selective autophagy. Dev Cell. 2009;17(1):87–97. doi: 10.1016/j.devcel.2009.06.013
   PubMed Web of Science ®Google Scholar
• Noda NN, Ohsumi Y, Inagaki F. Atg8-family interacting motif crucial for selective autophagy. FEBS Lett. 2010;584(7):1379–1385. doi: 10.1016/j.febslet.2010.01.018
   PubMed Web of Science ®Google Scholar
• Alemu EA, Lamark T, Torgersen KM, et al. ATG8 family proteins act as scaffolds for assembly of the ULK complex: sequence requirements for LC3-interacting region (LIR) motifs. J Biol Chem. 2012;287(47):39275–39290. doi: 10.1074/jbc.M112.378109
   PubMed Web of Science ®Google Scholar
• Kalvari I, Tsompanis S, Mulakkal NC, et al. iLIR: a web resource for prediction of Atg8-family interacting proteins. Autophagy. 2014;10(5):913. doi: 10.4161/auto.28260
   PubMed Web of Science ®Google Scholar
• Kondo-Okamoto N, Noda NN, Suzuki SW, et al. Autophagy-related protein 32 acts as autophagic degron and directly initiates mitophagy. J Biol Chem. 2012;287(13):10631–10638. doi: 10.1074/jbc.M111.299917
   PubMed Web of Science ®Google Scholar
• Kanki T, Wang K, Cao Y, et al. Atg32 is a mitochondrial protein that confers selectivity during mitophagy. Dev Cell. 2009;17(1):98–109. doi: 10.1016/j.devcel.2009.06.014
   PubMed Web of Science ®Google Scholar
• Aoki Y, Kanki T, Hirota Y, et al. Phosphorylation of serine 114 on Atg32 mediates mitophagy. Mol Biol Cell. 2011;22(17):3206–3217. doi: 10.1091/mbc.e11-02-0145
   PubMed Web of Science ®Google Scholar
• Deas E, Plun-Favreau H, Gandhi S, et al. PINK1 cleavage at position A103 by the mitochondrial protease PARL. Hum Mol Genet. 2011;20(5):867–879. doi: 10.1093/hmg/ddq526
   PubMed Web of Science ®Google Scholar
• McQuibban GA, Saurya S, Freeman M. Mitochondrial membrane remodelling regulated by a conserved rhomboid protease. Nature. 2003;423(6939):537–541. doi: 10.1038/nature01633
   PubMed Web of Science ®Google Scholar
• Duvezin-Caubet S, Koppen M, Wagener J, et al. OPA1 processing reconstituted in yeast depends on the subunit composition of the m-AAA protease in mitochondria. Mol Biol Cell. 2007;18(9):3582–3590. doi: 10.1091/mbc.e07-02-0164
   PubMed Web of Science ®Google Scholar
• Wang K, Jin M, Liu X, et al. Proteolytic processing of Atg32 by the mitochondrial i-AAA protease Yme1 regulates mitophagy. Autophagy. 2013;9(11):1828–1836. doi: 10.4161/auto.26281
   PubMed Web of Science ®Google Scholar
• Yan Y, Tang J, Yuan Q, et al. Mitochondrial prohibitin complex regulates fungal virulence via ATG24-assisted mitophagy. Commun Biol. 2022;5(1):298. doi: 10.1038/s42003-022-03666-5
   PubMed Web of Science ®Google Scholar
• Müller M, Kötter P, Behrendt C, et al. Synthetic quantitative array technology identifies the Ubp3-Bre5 deubiquitinase complex as a negative regulator of mitophagy. Cell Rep. 2015;10(7):1215–1225. doi: 10.1016/j.celrep.2015.01.044
   PubMed Web of Science ®Google Scholar
• Ha Y. Structure and mechanism of intramembrane protease. Semin Cell Dev Biol. 2009;20(2):240–250. doi: 10.1016/j.semcdb.2008.11.006
   PubMed Web of Science ®Google Scholar
• Wai T, Saita S, Nolte H, et al. The membrane scaffold SLP2 anchors a proteolytic hub in mitochondria containing PARL and the i-AAA protease YME1L. EMBO Rep. 2016;17(1):1844–1856. doi: 10.15252/embr.201642698
   PubMedGoogle Scholar
• Jumper J, Evans R, Pritzel A, et al. Highly accurate protein structure prediction with AlphaFold. Nature. 2021;596(7873):583–589. doi: 10.1038/s41586-021-03819-2
   PubMed Web of Science ®Google Scholar
• Varadi M, Anyango S, Deshpande M, et al. AlphaFold protein structure database: massively expanding the structural coverage of protein-sequence space with high-accuracy models. Nucleic Acids Res. 2022;50(D1):D439–44. doi: 10.1093/nar/gkab1061
   PubMed Web of Science ®Google Scholar
• Kanki T, Kang D, Klionsky DJ. Monitoring mitophagy in yeast: the Om45-GFP processing assay. Autophagy. 2009;5(8):1186–1189. doi: 10.4161/auto.5.8.9854
   PubMed Web of Science ®Google Scholar
• Kanki T, Klionsky DJ. Mitophagy in yeast occurs through a selective mechanism. J Biol Chem. 2008;283(47):32386. doi: 10.1074/jbc.M802403200
   PubMed Web of Science ®Google Scholar
• Kolitsida P, Abeliovich H. Methods for studying mitophagy in yeast. Methods Mol Biol. 2019;1880:669–678.
   PubMedGoogle Scholar