{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T01:23:51Z","timestamp":1785547431332,"version":"3.56.0"},"reference-count":97,"publisher":"MDPI AG","issue":"21","license":[{"start":{"date-parts":[[2025,10,27]],"date-time":"2025-10-27T00:00:00Z","timestamp":1761523200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"C.N.R.S."},{"name":"AFM grants","award":["15137"],"award-info":[{"award-number":["15137"]}]},{"name":"AFM grants","award":["15661"],"award-info":[{"award-number":["15661"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cells"],"abstract":"<jats:p>Mitochondria play a central role in cellular bioenergetics. They contribute significantly to ATP production, which is essential for maintaining cells. They are also key mediators of various types of cell death, including apoptosis, necroptosis, and ferroptosis. Additionally, they are one of the main regulators of autophagy. This brief review focuses on BID, a molecule of the BCL-2 family that is often overlooked. The importance of the cardiolipin\/caspase-8\/BID-FL platform, which is located on the surface of the outer mitochondrial membrane and generates tBID, will be emphasized. tBID is responsible for BAX\/BAK delocalization and oligomerization, as well as the transmission of death signals. New insights into the regulation of caspase-8 and BID have emerged, and this review will highlight their originality in the context of activation and function. The focus will be on results from biophysical studies of artificial membranes, such as lipid-supported monolayers and giant unilamellar vesicles containing cardiolipin. We will present the destabilization of mitochondrial bioenergetics caused by the insertion of tBID at the mitochondrial contact site, as well as the marginal but additive role of the MTCH2 protein, not forgetting the new players.<\/jats:p>","DOI":"10.3390\/cells14211678","type":"journal-article","created":{"date-parts":[[2025,10,28]],"date-time":"2025-10-28T11:47:19Z","timestamp":1761652039000},"page":"1678","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Caspase-8 and BID Caught in the Act with Cardiolipin: A New Platform to Provide Mitochondria with Microdomains of Apoptotic Signals"],"prefix":"10.3390","volume":"14","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5038-9101","authenticated-orcid":false,"given":"Patrice X.","family":"Petit","sequence":"first","affiliation":[{"name":"National Center for Scientific Research, CNRS UMR 8003, Paris City University, Saint-P\u00e8res, Paris Institute for Neuroscience (SSPIN), Team \u201cMitochondria, Apoptosis and Autophagy Signalling\u201d, Campus Saint-Germain, 75006 Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,10,27]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1016\/S0092-8674(00)81590-1","article-title":"Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis","volume":"94","author":"Li","year":"1998","journal-title":"Cell"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1016\/S0092-8674(00)81589-5","article-title":"Bid, a bcl-2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface receptors","volume":"94","author":"Luo","year":"1998","journal-title":"Cell"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/S0092-8674(00)00008-8","article-title":"Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition","volume":"102","author":"Du","year":"2000","journal-title":"Cell"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1038\/35083620","article-title":"Endonuclease G is an apoptotic DNase when released from mitochondria","volume":"412","author":"Li","year":"2001","journal-title":"Nature"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1038\/35083608","article-title":"Mitochondrial endonuclease G is important for apoptosis in C. elegans","volume":"412","author":"Parrish","year":"2001","journal-title":"Nature"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"48404","DOI":"10.1074\/jbc.M108461200","article-title":"Action of recombinant human apoptotic endonuclease G on naked DNA and chromatin substrates: Cooperation with exonuclease and DNase I","volume":"276","author":"Widlak","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"19414","DOI":"10.1074\/jbc.M101590200","article-title":"Bcl-xL promotes the open configuration of the voltage-dependent anion channel and metabolite passage through the outer mitochondrial membrane","volume":"276","author":"Li","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/S1097-2765(00)80307-X","article-title":"Bcl-xL prevents cell death following growth factor withdrawal by facilitating mitochondrial ATP\/ADP exchange","volume":"3","author":"Chandel","year":"1999","journal-title":"Mol. Cell"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1093\/emboj\/20.4.661","article-title":"A reversible component of mitochondrial respiratory dysfunction in apoptosis can be rescued by exogenous cytochrome c","volume":"20","author":"Mootha","year":"2001","journal-title":"EMBO J."},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Lutter, M., Perkins, G.A., and Wang, X. (2001). The pro-apoptotic Bcl-2 family member tBid localizes to mitochondrial contact sites. BMC Cell Biol., 2.","DOI":"10.1186\/1471-2121-2-22"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"754","DOI":"10.1038\/35036395","article-title":"Cardiolipin provides specificity for targeting of tBid to mitochondria","volume":"2","author":"Lutter","year":"2000","journal-title":"Nat. Cell Biol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"878","DOI":"10.1016\/S0006-291X(05)80868-X","article-title":"Further characterization of mitochondrial contact sites: Effect of short-chain alcohols on membrane fluidity and activity","volume":"173","author":"Ardail","year":"1990","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"18797","DOI":"10.1016\/S0021-9258(17)30583-5","article-title":"Mitochondrial contact sites. Lipid composition and dynamics","volume":"265","author":"Ardail","year":"1990","journal-title":"J. Biol. Chem."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"7268","DOI":"10.1128\/MCB.21.21.7268-7276.2001","article-title":"Bid, a widely expressed proapoptotic protein of the Bcl-2 family, displays lipid transfer activity","volume":"21","author":"Esposti","year":"2001","journal-title":"Mol. Cell Biol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"1300","DOI":"10.1038\/sj.cdd.4401306","article-title":"Proapoptotic Bid binds to monolysocardiolipin, a new molecular connection between mitochondrial membranes and cell death","volume":"10","author":"Esposti","year":"2003","journal-title":"Cell Death Differ."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"614","DOI":"10.1038\/sj.cdd.4401571","article-title":"tBid interaction with cardiolipin primarily orchestrates mitochondrial dysfunctions and subsequently activates Bax and Bak","volume":"12","author":"Gonzalvez","year":"2005","journal-title":"Cell Death Differ."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1083\/jcb.200803129","article-title":"Cardiolipin provides an essential activating platform for caspase-8 on mitochondria","volume":"183","author":"Gonzalvez","year":"2008","journal-title":"J. Cell Biol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"2447","DOI":"10.1016\/j.febslet.2009.07.018","article-title":"Cardiolipin-enriched raft-like microdomains are essential activating platforms for apoptotic signals on mitochondria","volume":"583","author":"Sorice","year":"2009","journal-title":"FEBS Lett."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"877","DOI":"10.1007\/s10495-007-0718-8","article-title":"Cardiolipin: Setting the beat of apoptosis","volume":"12","author":"Gonzalvez","year":"2007","journal-title":"Apoptosis"},{"key":"ref_20","first-page":"989","article-title":"Mechanism of activation of cytochrome C peroxidase activity by cardiolipin","volume":"71","author":"Vladimirov","year":"2006","journal-title":"Biochemistry"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"1057","DOI":"10.1016\/j.bbamem.2018.01.009","article-title":"Structural characterization of cardiolipin-driven activation of cytochrome c into a peroxidase and membrane perturbation","volume":"1860","author":"Mohammadyani","year":"2018","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"806","DOI":"10.1016\/j.str.2019.02.007","article-title":"Surface-Binding to Cardiolipin Nanodomains Triggers Cytochrome c Pro-apoptotic Peroxidase Activity via Localized Dynamics","volume":"27","author":"Li","year":"2019","journal-title":"Structure"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1439","DOI":"10.1016\/j.freeradbiomed.2009.03.004","article-title":"Cytochrome c\/cardiolipin relations in mitochondria: A kiss of death","volume":"46","author":"Kagan","year":"2009","journal-title":"Free Radic. Biol. Med."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"558","DOI":"10.1016\/j.bbamcr.2011.01.026","article-title":"Caspase-8 and Bid: Caught in the act between death receptors and mitochondria","volume":"1813","author":"Kantari","year":"2011","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1038\/ncb2057","article-title":"MTCH2\/MIMP is a major facilitator of tBID recruitment to mitochondria","volume":"12","author":"Zaltsman","year":"2010","journal-title":"Nat. Cell Biol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1016\/j.molcel.2015.08.008","article-title":"ATR Plays a Direct Antiapoptotic Role at Mitochondria, which Is Regulated by Prolyl Isomerase Pin1","volume":"60","author":"Hilton","year":"2015","journal-title":"Mol. Cell"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1016\/j.cell.2005.06.014","article-title":"Proapoptotic BID is an ATM effector in the DNA-damage response","volume":"122","author":"Kamer","year":"2005","journal-title":"Cell"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1194","DOI":"10.1016\/j.bbadis.2013.03.005","article-title":"Barth syndrome: Cellular compensation of mitochondrial dysfunction and apoptosis inhibition due to changes in cardiolipin remodeling linked to tafazzin (TAZ) gene mutation","volume":"1832","author":"Gonzalvez","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_29","doi-asserted-by":"crossref","unstructured":"Saric, A., Andreau, K., Armand, A.S., Moller, I.M., and Petit, P.X. (2015). Barth Syndrome: From Mitochondrial Dysfunctions Associated with Aberrant Production of Reactive Oxygen Species to Pluripotent Stem Cell Studies. Front. Genet., 6.","DOI":"10.3389\/fgene.2015.00359"},{"key":"ref_30","doi-asserted-by":"crossref","unstructured":"Wyzewski, Z., Gregorczyk-Zboroch, K.P., Mielcarska, M.B., Switlik, W., and Niedzielska, A. (2025). Bid Protein: A Participant in the Apoptotic Network with Roles in Viral Infections. Int. J. Mol. Sci., 26.","DOI":"10.3390\/ijms26062385"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1038\/s41586-023-06866-z","article-title":"A break in mitochondrial endosymbiosis as a basis for inflammatory diseases","volume":"626","author":"Murphy","year":"2024","journal-title":"Nature"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1016\/j.chemphyslip.2016.04.005","article-title":"Cardiolipin as key lipid of mitochondria in health and disease. 2016, 2nd Edition, Florence, Italy, September 30\u2013October 1, 2015","volume":"198","author":"Corcelli","year":"2016","journal-title":"Chem. Phys. Lipids"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1038\/sj.cdd.4400997","article-title":"Lipids, cardiolipin and apoptosis: A greasy licence to kill","volume":"9","author":"Esposti","year":"2002","journal-title":"Cell Death Differ."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"101195","DOI":"10.1016\/j.plipres.2022.101195","article-title":"Studies of the cardiolipin interactome","volume":"88","author":"Fox","year":"2022","journal-title":"Prog. Lipid Res."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1515\/hsz-2020-0103","article-title":"The MICOS complex, a structural element of mitochondria with versatile functions","volume":"401","author":"Khosravi","year":"2020","journal-title":"Biol. Chem."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1515\/revneuro-2024-0004","article-title":"Mitochondria and MICOS\u2013Function and modeling","volume":"35","author":"Benaroya","year":"2024","journal-title":"Rev. Neurosci."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1038\/42408","article-title":"Functional rafts in cell membranes","volume":"387","author":"Simons","year":"1997","journal-title":"Nature"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"470","DOI":"10.1016\/S0955-0674(00)00238-6","article-title":"Roles of lipid rafts in membrane transport","volume":"13","author":"Ikonen","year":"2001","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1016\/j.bbagen.2007.08.015","article-title":"Structure and function of glycosphingolipids and sphingolipids: Recollections and future trends","volume":"1780","author":"Hakomori","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1038\/35036052","article-title":"Lipid rafts and signal transduction","volume":"1","author":"Simons","year":"2000","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"8309","DOI":"10.1074\/jbc.M207618200","article-title":"Association of the death-inducing signaling complex with microdomains after triggering through CD95\/Fas. Evidence for caspase-8-ganglioside interaction in T cells","volume":"278","author":"Garofalo","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1675","DOI":"10.1093\/emboj\/17.6.1675","article-title":"Two CD95 (APO-1\/Fas) signaling pathways","volume":"17","author":"Scaffidi","year":"1998","journal-title":"EMBO J."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"884","DOI":"10.1038\/sj.cdd.4400419","article-title":"Activation of the CD95 (APO-1\/Fas) pathway in drug- and gamma-irradiation-induced apoptosis of brain tumor cells","volume":"5","author":"Fulda","year":"1998","journal-title":"Cell Death Differ."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/S0076-6879(08)01406-7","article-title":"Analyzing lipid raft dynamics during cell apoptosis","volume":"442","author":"Malorni","year":"2008","journal-title":"Methods Enzymol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"e103","DOI":"10.1038\/cddis.2010.81","article-title":"Giant unilamellar vesicles (GUVs) as a new tool for analysis of caspase-8\/Bid-FL complex binding to cardiolipin and its functional activity","volume":"1","author":"Jalmar","year":"2010","journal-title":"Cell Death Dis."},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Jalmar, O., Francois-Moutal, L., Garcia-Saez, A.J., Perry, M., Granjon, T., Gonzalvez, F., Gottlieb, E., Ayala-Sanmartin, J., Klosgen, B., and Schwille, P. (2013). Caspase-8 binding to cardiolipin in giant unilamellar vesicles provides a functional docking platform for bid. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0055250"},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Bleicken, S., Garcia-Saez, A.J., Conte, E., and Bordignon, E. (2012). Dynamic interaction of cBid with detergents, liposomes and mitochondria. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0035910"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/j.bbamem.2016.10.007","article-title":"Pro-apoptotic cBid and Bax exhibit distinct membrane remodeling activities: An AFM study","volume":"1859","author":"Unsay","year":"2017","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"538","DOI":"10.1038\/cdd.2010.135","article-title":"BID is cleaved by caspase-8 within a native complex on the mitochondrial membrane","volume":"18","author":"Schug","year":"2011","journal-title":"Cell Death Differ."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"e108690","DOI":"10.15252\/embj.2021108690","article-title":"BCL-2-family protein tBID can act as a BAX-like effector of apoptosis","volume":"41","author":"Hohorst","year":"2022","journal-title":"EMBO J."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"33241","DOI":"10.1074\/jbc.M113.512087","article-title":"Proapoptotic Bax and Bak form stable protein-permeable pores of tunable size","volume":"15","author":"Bleicken","year":"2013","journal-title":"J Biol Chem."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"e1735","DOI":"10.1038\/cddis.2015.105","article-title":"Bid chimeras indicate that most BH3-only proteins can directly activate Bak and Bax, and show no preference for Bak versus Bax","volume":"6","author":"Hockings","year":"2015","journal-title":"Cell Death Dis."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1038\/nsmb.2563","article-title":"BID-induced structural changes in BAK promote apoptosis","volume":"20","author":"Moldoveanu","year":"2013","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1016\/j.molcel.2013.08.048","article-title":"BID preferentially activates BAK while BIM preferentially activates BAX, affecting chemotherapy response","volume":"51","author":"Sarosiek","year":"2013","journal-title":"Mol. Cell"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"6338","DOI":"10.1111\/j.1742-4658.2009.07345.x","article-title":"Interaction of the alpha-helical H6 peptide from the pro-apoptotic protein tBid with cardiolipin","volume":"276","author":"Petit","year":"2009","journal-title":"FEBS J."},{"key":"ref_56","doi-asserted-by":"crossref","unstructured":"Gonzalvez, F., Pariselli, F., Jalmar, O., Dupaigne, P., Sureau, F., Dellinger, M., Hendrickson, E.A., Bernard, S., and Petit, P.X. (2010). Mechanistic issues of the interaction of the hairpin-forming domain of tBid with mitochondrial cardiolipin. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0009342"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1016\/j.molcel.2004.10.028","article-title":"The first alpha helix of Bax plays a necessary role in its ligand-induced activation by the BH3-only proteins Bid and PUMA","volume":"16","author":"Cartron","year":"2004","journal-title":"Mol. Cell"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"637","DOI":"10.4161\/cc.4.5.1671","article-title":"Activation of Bax by BH3 domains during apoptosis: The unfolding of a deadly plot","volume":"4","author":"Juin","year":"2005","journal-title":"Cell Cycle"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"10930","DOI":"10.1021\/bi036044c","article-title":"Membrane-insertion fragments of Bcl-xL, Bax, and Bid","volume":"43","author":"Mingarro","year":"2004","journal-title":"Biochemistry"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"3976","DOI":"10.1529\/biophysj.104.058008","article-title":"Peptides derived from apoptotic Bax and Bid reproduce the poration activity of the parent full-length proteins","volume":"88","author":"Coraiola","year":"2005","journal-title":"Biophys. J."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.febslet.2004.10.080","article-title":"Impact of pH on Bax alpha conformation, oligomerisation and mitochondrial integration","volume":"578","author":"Cartron","year":"2004","journal-title":"FEBS Lett."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1126\/science.add1856","article-title":"MTCH2 is a mitochondrial outer membrane protein insertase","volume":"378","author":"Guna","year":"2022","journal-title":"Science"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1016\/j.str.2024.01.012","article-title":"Insertases scramble lipids: Molecular simulations of MTCH2","volume":"32","author":"Bartos","year":"2024","journal-title":"Structure"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"2203","DOI":"10.2147\/DDDT.S460448","article-title":"MTCH2 in Metabolic Diseases, Neurodegenerative Diseases, Cancers, Embryonic Development and Reproduction","volume":"18","author":"Peng","year":"2024","journal-title":"Drug Des. Devel. Ther."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"1165","DOI":"10.1038\/cdd.2015.166","article-title":"Cardiolipin or MTCH2 can serve as tBID receptors during apoptosis","volume":"23","author":"Raemy","year":"2016","journal-title":"Cell Death Differ."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"616","DOI":"10.1038\/nrm2450","article-title":"ATR: An essential regulator of genome integrity","volume":"9","author":"Cimprich","year":"2008","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1038\/ncb2897","article-title":"Causes and consequences of replication stress","volume":"16","author":"Zeman","year":"2014","journal-title":"Nat. Cell Biol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1146\/annurev.biochem.73.011303.073723","article-title":"Molecular mechanisms of mammalian DNA repair and the DNA damage checkpoints","volume":"73","author":"Sancar","year":"2004","journal-title":"Annu. Rev. Biochem."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"864","DOI":"10.1038\/nature03482","article-title":"DNA damage response as a candidate anti-cancer barrier in early human tumorigenesis","volume":"434","author":"Bartkova","year":"2005","journal-title":"Nature"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"1160","DOI":"10.1126\/science.1140321","article-title":"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage","volume":"316","author":"Matsuoka","year":"2007","journal-title":"Science"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"1713","DOI":"10.1126\/science.1065521","article-title":"ATR and ATRIP: Partners in checkpoint signaling","volume":"294","author":"Cortez","year":"2001","journal-title":"Science"},{"key":"ref_72","doi-asserted-by":"crossref","unstructured":"Singh, P., Ravanan, P., and Talwar, P. (2016). Death Associated Protein Kinase 2016, 1 (DAPK1): A Regulator of Apoptosis and Autophagy. Front. Mol. Neurosci., 9.","DOI":"10.3389\/fnmol.2016.00046"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1016\/j.cell.2005.06.022","article-title":"A role for proapoptotic BID in the DNA-damage response","volume":"122","author":"Zinkel","year":"2005","journal-title":"Cell"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1038\/ncb2468","article-title":"The ATM-BID pathway regulates quiescence and survival of haematopoietic stem cells","volume":"14","author":"Maryanovich","year":"2012","journal-title":"Nat. Cell Biol."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"752","DOI":"10.1016\/j.stem.2016.08.007","article-title":"DNA Damage-Induced HSPC Malfunction Depends on ROS Accumulation Downstream of IFN-1 Signaling and Bid Mobilization","volume":"19","author":"Tasdogan","year":"2016","journal-title":"Cell Stem Cell"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1016\/j.taap.2006.10.031","article-title":"p53-Dependent but ATM-independent inhibition of DNA synthesis and G2 arrest in cadmium-treated human fibroblasts","volume":"218","author":"Cao","year":"2007","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"ref_77","doi-asserted-by":"crossref","unstructured":"Bar-Lev, Y., Moshitch-Moshkovitz, S., Tsarfaty, G., Kaufman, D., Horev, J., Resau, J.H., and Tsarfaty, I. (2016). Mimp\/Mtch2, an Obesity Susceptibility Gene, Induces Alteration of Fatty Acid Metabolism in Transgenic Mice. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0157850"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"1602","DOI":"10.1016\/j.celrep.2016.01.046","article-title":"Loss of Muscle MTCH2 Increases Whole-Body Energy Utilization and Protects from Diet-Induced Obesity","volume":"14","author":"Kuperman","year":"2016","journal-title":"Cell Rep."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"616","DOI":"10.1002\/oby.21751","article-title":"MTCH2 is a conserved regulator of lipid homeostasis","volume":"25","author":"Rottiers","year":"2017","journal-title":"Obesity"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"5132","DOI":"10.1038\/s41467-018-07519-w","article-title":"MTCH2-mediated mitochondrial fusion drives exit from naive pluripotency in embryonic stem cells","volume":"9","author":"Bahat","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1038\/s44319-023-00009-1","article-title":"MTCH2 cooperates with MFN2 and lysophosphatidic acid synthesis to sustain mitochondrial fusion","volume":"25","author":"Goldman","year":"2024","journal-title":"EMBO Rep."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"1007","DOI":"10.1038\/s44318-024-00335-7","article-title":"MTCH2 controls energy demand and expenditure to fuel anabolism during adipogenesis","volume":"44","author":"Chourasia","year":"2025","journal-title":"EMBO J."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"e2416598","DOI":"10.1002\/advs.202416598","article-title":"MTCH2 Suppresses Thermogenesis by Regulating Autophagy in Adipose Tissue","volume":"12","author":"Zhao","year":"2025","journal-title":"Adv. Sci."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"338","DOI":"10.1002\/hep.23672","article-title":"Bid agonist regulates murine hepatocyte proliferation by controlling endoplasmic reticulum calcium homeostasis","volume":"52","author":"Ni","year":"2010","journal-title":"Hepatology"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"3349","DOI":"10.1002\/hep4.2052","article-title":"Promotion of diet-induced obesity and metabolic syndromes by BID is associated with gut microbiota","volume":"6","author":"Yan","year":"2022","journal-title":"Hepatol. Commun."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1016\/S0005-2728(02)00187-1","article-title":"Sequence and functional similarities between pro-apoptotic Bid and plant lipid transfer proteins","volume":"1553","year":"2002","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"8831","DOI":"10.1038\/s41467-025-63880-7","article-title":"MTCH2 modulates CPT1 activity to regulate lipid metabolism of adipocytes","volume":"16","author":"Wu","year":"2025","journal-title":"Nat. Commun."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1038\/s41419-025-07618-9","article-title":"MTCH2 regulates NRF2-mediated RRM1 expression to promote melanoma proliferation and dacarbazine insensitivity","volume":"16","author":"Zhang","year":"2025","journal-title":"Cell Death Dis."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1038\/nature01627","article-title":"Humanin peptide suppresses apoptosis by interfering with Bax activation","volume":"423","author":"Guo","year":"2003","journal-title":"Nature"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1016\/S1734-1140(10)70337-6","article-title":"Humanins, the neuroprotective and cytoprotective peptides with antiapoptotic and anti-inflammatory properties","volume":"62","author":"Zapala","year":"2010","journal-title":"Pharmacol. Rep."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"19055","DOI":"10.1074\/jbc.RA119.011297","article-title":"Humanin induces conformational changes in the apoptosis regulator BAX and sequesters it into fibers, preventing mitochondrial outer-membrane permeabilization","volume":"294","author":"Morris","year":"2019","journal-title":"J. Biol. Chem."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"18226","DOI":"10.1074\/jbc.RA120.013023","article-title":"Humanin selectively prevents the activation of pro-apoptotic protein BID by sequestering it into fibers","volume":"295","author":"Morris","year":"2020","journal-title":"J. Biol. Chem."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"15098","DOI":"10.1021\/la102689v","article-title":"Detection of association and fusion of giant vesicles using a fluorescence-activated cell sorter","volume":"26","author":"Sunami","year":"2010","journal-title":"Langmuir"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1038\/nm0196-80","article-title":"Bcl-2 protects from lethal hepatic apoptosis induced by an anti-Fas antibody in mice","volume":"2","author":"Lacronique","year":"1996","journal-title":"Nat. Med."},{"key":"ref_95","first-page":"G702","article-title":"Differential protective effects of Bcl-xL and Bcl-2 on apoptotic liver injury in transgenic mice","volume":"277","author":"Fabre","year":"1999","journal-title":"Am. J. Physiol."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"2057","DOI":"10.1194\/jlr.M026062","article-title":"Raft-like microdomains play a key role in mitochondrial impairment in lymphoid cells from patients with Huntington\u2019s disease","volume":"53","author":"Ciarlo","year":"2012","journal-title":"J. Lipid Res."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1007\/s10495-015-1100-x","article-title":"Role of mitochondrial raft-like microdomains in the regulation of cell apoptosis","volume":"20","author":"Garofalo","year":"2015","journal-title":"Apoptosis"}],"container-title":["Cells"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2073-4409\/14\/21\/1678\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,28]],"date-time":"2025-10-28T12:00:10Z","timestamp":1761652810000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2073-4409\/14\/21\/1678"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,10,27]]},"references-count":97,"journal-issue":{"issue":"21","published-online":{"date-parts":[[2025,11]]}},"alternative-id":["cells14211678"],"URL":"https:\/\/doi.org\/10.3390\/cells14211678","relation":{},"ISSN":["2073-4409"],"issn-type":[{"value":"2073-4409","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,10,27]]}}}