{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062948/Shintaro_20220701_QE_Aur1hr_proteins_N.xlsx"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062948/Shintaro_20220701_QE_Aur1hr_GFP-Fis1-N1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062948/Shintaro_20220701_QE_Aur1hr_OMP25-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062948/Shintaro_20220701_QE_Aur1hr_GFP-Fis1-N3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062948/Shintaro_20220701_QE_Aur1hr_GFP-Fis1-N2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062948/Shintaro_20220701_QE_Aur1hr_OMP25-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062948/Shintaro_20220701_QE_Aur1hr_OMP25-3.raw"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["tfchou@caltech.edu"],"submitter":["Ting-Yu Wang"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Fis1","Mitochondria","Actin filaments","Mitophagy","Fascin1"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD062948"],"tissue":["Fibroblast"],"sample_protocol":["Cells expressing EGFP-tagged OMP25 or Fis1 were harvested with a cell scraper and lysed in immunoprecipitation (IP) buffer (20 mM Tris-HCl pH 7.5, 150 mM NaCl, 1 mM EDTA pH8.0, 5% glycerol, 1% Igepal CA-630, and Halt Protease inhibitor cocktail (78427; Thermo Scientific)). The lysates were cleared by centrifugation at 14,000 rpm for 10 min at 4°C, and protein concentrations were measured with the DC protein assay (Bio-Rad). Cell lysates were mixed with GFP-nanobody conjugated beads for 1 hour at 4°C. The beads were washed three times with IP buffer, and SENPEuB protease was added to the beads for elution of the GFP-nanobody-EGFP-bait protein complexes. For mass spectrometry, 1% Igepal CA-630 was replaced with 1% n-dodecyl-β-D-maltoside. Digestion and desalting of IP samples IP eluates were denatured in 8 M urea, reduced in 4 mM Tris (2-carboxyethyl) phosphine (TCEP, C4706, Sigma) at 37°C for 20 min, and alkylated in 4 mM 2-chloroacetamide (CAA, 79-07-2, Millipore Sigma), 50 mM HEPES (pH7.5) at 37°C for 15 min. Peptides were then digested with 0.2 μg of Lys-C (Wako) at 37°C for 2 h with 750 rpm shaking, diluted to 2 M urea with 50 mM HEPES (pH 7.5). CaCl2 was added to 1 mM, and samples were digested with 0.4 μg trypsin (90305, Thermo Fisher Scientific) overnight at 37°C with 750 rpm shaking. Digested peptides were acidified by addition of trifluoroacetic acid (TFA) to 0.5%. The final pH was checked using a pH strip (pH< 2). The acidified peptides were desalted using C18 Spin Columns (Thermo Scientific) according to the manufacturer’s instructions and lyophilized prior to mass spectrometry analysis. LC-MS/MS analysis was performed with an EASY-nLC 1200 (T 370 hermoFisher Scientific, San Jose, CA) coupled to a Q Exactive HF hybrid quadrupole-Orbitrap mass spectrometer (ThermoFisher Scientific, San Jose, CA). Peptides were separated on an Aurora UHPLC Column (25 cm × 75 μm, 1.7 μm C18, AUR3-25075C18-TS, Ion Opticks) with a flow rate of 0.35 μL/min for a total duration of 40 min and ionized at 1.6 kV in the positive ion mode. The gradient was composed of 6% solvent B (2.0 min), 6-25% B (22.5 min), 25-40% B (7.5 min), 40–98% B (1 min) and 98% B (7 min); solvent A: 2% ACN and 0.2% FA in water; solvent B: 80% ACN and 0.2% FA. MS1 scans were acquired at the resolution of 60,000 from 375 to 1500 m/z, AGC target 3e6, and maximum injection time 15 ms. The 12 most abundant ions in MS2 scans were acquired at a resolution of 30,000, AGC target 1e5, maximum injection time 60 ms, and normalized collision energy of 28. Dynamic exclusion was set to 30 s and ions with charge +1, +7, +8 and >+8 were excluded. The temperature of ion transfer tube was 275°C and the S-lens RF level was set to 60."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["MS2 fragmentation spectra were searched with Proteome Discoverer SEQUEST (version 2.5, Thermo Scientific) against in silico tryptic digested the UniProt Human proteome Swiss-Prot database. The maximum missed cleavages was set to 2. Dynamic modifications were set to oxidation on methionine (M, +15.995 Da) and protein N-terminal acetylation (+42.011 Da). Carbamidomethylation on cysteine residues (C, +57.021 Da) was set as a fixed modification. The maximum parental mass error was set to 10 ppm, and the MS2 mass tolerance was set to 0.03 Da. The false discovery threshold was set strictly to 0.01 using the Percolator Node validated by q-value. The relative abundance of parental peptides was calculated by integration of the area under the curve of the MS1 peaks using the Minora LFQ node."],"omics_type":["Proteomics"],"labhead":["Tsui-Fen Chou"],"instrument_platform":[""],"labhead_affiliation":["Proteome Exploration Laboratory, Beckman Institute, California Institute of Technology, Pasadena,CA 91125, USA."],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"publication":["41742405 Nakajima S, Wang TY, Chou TF, Chakrabarty Y, Chan DC. Regulation of mitophagy by Fis1 and Fascin1-organized actin. Curr Biol. 2026 36(5):1205-1219.e8 10.1016/j.cub.2026.01.062"],"submitter_mail":["tywang@caltech.edu"],"submitter_affiliation":["Caltech"],"submitter_country":["United States"],"pubmed_abstract":["Mitophagy, the autophagic degradation of mitochondria, plays a central role in controlling the quality and quantity of mitochondria, thereby ensuring cellular health. The mitochondrial outer membrane protein Fis1 is important for several types of mitophagy, but its mechanism of action remains unclear. F-actin is recruited to autophagic cargo and is important for autophagic progression, but the mechanism for its recruitment is poorly understood. To address the molecular function of Fis1, we performed affinity purification of Fis1 and mass spectrometry and identified the actin-bundling protein Fascin1 as a physical interactor. We demonstrate that Fis1 is required for recruitment of Fascin1 as well as F-actin to mitochondria under stress conditions, including mitochondrial depolarization and iron chelation. Iron chelation also triggers mitophagy that is independent of the Parkinson's associated gene Parkin, and we show that Fis1 enables recruitment of Fascin1-organized F-actin to facilitate proper morphogenesis of autophagosomes and the ensuing mitochondrial degradation. In contrast, although Parkin-mediated mitophagy also relies on Fis1, it is unaffected by loss of Fascin1 or F-actin recruitment. These findings indicate that Fis1 has distinct modes of action in mitophagy, depending on the triggering cellular stress. They establish Fis1 as a key driver of Fascin1 and F-actin recruitment to mitochondria, events that are critical for autophagosome morphogenesis during iron-chelation-induced mitophagy."],"pubmed_title":["Regulation of mitophagy by Fis1 and Fascin1-organized actin."],"pubmed_authors":["Nakajima Shintaro S, Wang Ting-Yu TY, Chou Tsui-Fen TF, Chakrabarty Yogaditya Y, Chan David C DC"],"additional_accession":[]},"is_claimable":false,"name":"Regulation of mitophagy by Fis1 and Fascin1-organized actin","description":"Mitophagy, the autophagic degradation of mitochondria, plays a central role in controlling the quality and quantity of mitochondria, thereby ensuring cellular health. The mitochondrial outer membrane protein Fis1 is important for several types of mitophagy, but its mechanism of action remains unclear. F-actin is recruited to autophagic cargo and is important for autophagic progression, but the mechanism for its recruitment is poorly understood. To address the molecular function of Fis1, we performed affinity purification of Fis1 and mass spectrometry and identified the actin-bundling protein Fascin1 as a physical interactor. We demonstrate that Fis1 is required for recruitment of Fascin1 as well as F-actin to mitochondria under stress conditions, including mitochondrial depolarization and iron chelation. Iron chelation also triggers mitophagy that is independent of the Parkinson's associated gene Parkin, and we show that Fis1 enables recruitment of Fascin1-organized F-actin to facilitate proper morphogenesis of autophagosomes and the ensuing mitochondrial degradation. In contrast, although Parkin-mediated mitophagy also relies on Fis1, it is unaffected by loss of Fascin1 or F-actin recruitment. These findings indicate that Fis1 has distinct modes of action in mitophagy, depending on the triggering cellular stress. They establish Fis1 as a key driver of Fascin1 and F-actin recruitment to mitochondria, events that are critical for autophagosome morphogenesis during iron-chelation-induced mitophagy.","dates":{"publication":"2026-07-07","submission":"2025-04-14"},"accession":"PXD062948","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:247480","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:111205","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:4615","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:111225","NEWT:7719","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:55350","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:1912919","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:345076","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:200795","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:717966","NEWT:10891","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2709072","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:2836","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:108458","NEWT:5936","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:548","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:2126348","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:542","NEWT:2903","NEWT:185579","NEWT:872227","NEWT:13076","NEWT:2587410","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:2126337","NEWT:550","NEWT:33941","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:575412","NEWT:28112","NEWT:49012","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063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