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Bender"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Chemical cross-linking coupled with mass spectrometry proteomics"],"software":["Not available"],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD076857"],"sample_protocol":["Please provide a short description on the sample preparation steps, separation, enrichment strategies and mass spectrometry protocols includedProtein samples were diluted to a final concentration of 21 µM, using crosslinking buffer that contained 50 mM HEPES (pH 7.5) and 150 mM NaCl at 10°C. For each crosslinking reaction 6 µL protein solution was mixed with a second solution of the same protein at the same concentration. After 10 min incubation time, 0.5 µL crosslinking reagent S-SDA (Thermo Fisher Scientific, #26173) dissolved in ultrapure water was added to the protein solution, to achieve a final molar excess of crosslinker over protein of 11.5. N-hydroxy succinimide ester (NHS)-based crosslinking was performed at RT for 30 min. Next, diazirine-based crosslinking was performed using an in-house build LED UV light source (∼ 30 x103 µW/cm2) for 20 min on ice. For separating crosslinking reaction products by SDS-PAGE, 3.125 µL of the five-times diluted sample buffer containing 10% [w/v] SDS, 25% [v/v] β-mercaptoethanol, 50% [v/v] glycerol, 1.25 M Tris/HCl (pH 6.8), and 0,01% [w/v] bromophenol blue was added and the mixture was incubated for 8 min at 95°C. Coomassie-stained protein bands were excised and destained by alternating incubations with 10 mM ammonium bicarbonate (AmBic) or 5 mM AmBic / 50% [v/v] ethanol for 10 min at room temperature (RT). Gel slices were dehydrated in 100% ethanol for 10 min at RT, followed by a reduction with 5 mM TCEP in 10 mM AmBic for 45 min at 56°C, and alkylation with 50 mM iodoacetamide (IAA), in 10 mM AmBic for 15 min at RT in the dark. Excess IAA was washed out using 10 mM AmBic and 5 mM AmBic / 50% [v/v] ethanol for 10 min at RT. For subsequent proteolytic digestion, gel slices were dried using a vacuum centrifuge at 30°C for 45 min. Trypsin (Promega) was added at a protease:protein mass ratio of 1:20 and the mixture was digested for 16 h at 37°C. Peptides were eluted using a solution of 50% (v/v) acetonitrile and 50% (v/v) ethanol, and sonicated in an ice-cooled water bath sonicator for 10 min. Eluted peptides were dried in a vacuum centrifuge and either stored at – 80°C or directly resuspended for desalting prior to the LC-MS analysis.  For LC-MS analysis peptides were resuspended in 0.1% (v/v) trifluoroacetic acid and precipitates were pelleted by centrifugation for 6 min at 12,000 rpm at RT). Peptides were separated on a UltimateTM 3000 RSLCnano system (Thermo Fisher Scientific), equipped with a PepMapTM (C18,0.3 mm ID x 5 mm L) precolumn (Thermo Fisher Scientific) and an Acclaim PepMapTM (C18, 75 μm ID x 500 mm L, 100 Å pore size) analytical column (Thermo Fisher Scientific), using a binary solvent system consisting of 0.1% [v/v] formic acid (solvent A) and 86% [v/v] acetonitrile/0.1% [v/v] formic acid (solvent B) at 40°C.  Peptides were loaded at 1% solvent B for 3 min at a flow rate of 10 µL x min-1 and were eluted by applying a three-step gradient, starting after 4 min with 2% solvent B at a flow rate of 0.3 µL x min-1 over 24% solvent B at 67 min, 31% at 80 min, and reaching 47% solvent B after 91 min. Subsequently, the column was flushed with 95% solvent B for 5 min.  Finally, the column was equilibrated for 20 min at 1% solvent B with a flow rate of 0.35 µL x min-1. Separated peptides were measured on a Q Exactive Plus mass spectrometer (Thermo Fisher Scientific), equipped with a nano electrospray ion source and a stainless steel emitter, using a data-dependent acquisition mode with a scan range of m/z 400 to 1,450 at a maximum resolution of 140,000 at m/z 400, an automatic gain control (AGC) of 3 x 106 ions and a maximum fill time of 50 ms for MS1 scans. The 10 most intense precursor ions with charge states between 2+ and 8+ were selected for higher-energy collisional dissociation (HCD) with stepped normalized collision energies of 24%, 28% and 30%. MS2 data were acquired within a scan range of m/z 200 to 2,000 at a resolution of 70,000, with an AGC of 5 x 104 and a maximum fill time of 120 ms. A dynamic exclusion time of 30 s was set for already fragmented precursor ions."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Please provide a couple of sentences on the bioinformatics pipeline used, main search parameters, quantitative analysis, software tools and versions included. Think something similar in scope to the Data Analysis section of your manuscriptCrosslinked peptides were identified using the software pLink2 (version 2.3.9). Searches were performed against the forward and reverse sequences of protein samples, including tryptic peptides 5-60 amino acids in length and allowing a maximum of three missed cleavages. Oxidation of methionine was set as variable and carbamidomethylating of cysteine was treated as a fixed modification. Lysine, tyrosine, serine, threonine and the N-terminus were set as one crosslinked site, and any other residue as second crosslinked site. The mass tolerance of the search of MS1 and MS2 spectra was set to 20 ppm, and identified MS1 spectra were subsequently filtered by a mass tolerance of 10 ppm and a false discovery rate (FDR) of 5% at peptide-spectrum match (PSM) level. pLink2 results were subsequently filtered by the following criteria: PSMs having E-values above 1 x 10-2 or comprising adjacent tryptic peptides of the same protein were rejected. Additionally, crosslinks covering the protein N-terminus were omitted. Only crosslinked residue pairs that were identified in 3 out 4 replicates were retained for further interpretation. The resulting crosslinking data were then visualized using XiNET (version 2.0.0)."],"omics_type":["Proteomics"],"labhead":["Dr Bettina"],"instrument_platform":[""],"labhead_affiliation":["Lab head's affiliation, such as: depChair of Biochemistry II, Theodor Boveri-Institute, Biocenter, University of Würzburg, Würzburg, Germanyartment, lab, institute and country"],"submission_type":["PARTIAL"],"species":["Komagataella Phaffii"],"submitter_mail":["julian.bender@uni-wuerzburg.de"],"publication":["10.1101/2025.08.30.673231"],"submitter_affiliation":["University of Wuerzburg\nChair of Biochemistry II\nAm Hubland\n97074 Würzburg"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"Structure of Pex8 in complex with peroxisomal receptor Pex5 reveals its essential role in peroxisomal cargo translocationSMS","description":"Please provide an overall description of your study, think something similar in scope to the manuscript abstractPeroxisomes are essential cellular organelles that enable the sequestered execution of a broad range of metabolic processes. Due to the lack of an internal protein synthesis machinery, they entirely depend on the import of target proteins to carry out their functions within peroxisomes. While the process of cargo/receptor recognition is well understood, knowledge about the molecular mechanisms of the subsequent translocation steps, including cargo release and receptor recycling, is lacking behind. Here, we provide structural and functional evidence on the role of Pex8 in these processes. First, we show that Pex8 in yeast is essential for peroxisomal cargo translocation, irrespective of the mechanism of receptor/cargo recognition. Next, we reveal that Pex8 binds through an irregular twelvefold HEAT repeat array to a short three-helical bundle within the otherwise unfolded N-terminal domain of the Pex5 receptor. Impairing this interaction abolishes peroxisomal protein translocation. It is complemented by a secondary autonomous Pex8 cargo-like interaction site with the C-terminal domain of Pex5, thus generating a bipartite interaction between the two proteins.  Our data support a model in which Pex5/Pex8 complex formation allows assembly with the peroxisomal Pex2/Pex10/Pex12 E3-ubiquitin ligase complex to initiate recycling of the receptor. In summary, our findings provide in-depth insight into the transition from cargo release into peroxisomes to receptor recycling, which is essential to uncover the overall process of the peroxisomal cargo translocation.","dates":{"publication":"2026-04-17","submission":"2026-04-10"},"accession":"PXD076857","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:108018","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:592321","NEWT:1073882","NEWT:6819","NEWT:112509","NEWT:46429","NEWT:475174","NEWT:111205","NEWT:1599","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:2736291","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:294671","NEWT:376619","NEWT:1748418","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:1907535","NEWT:135622","NEWT:4615","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:2086595","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:381198","NEWT:418106","NCBITaxon:12721","NEWT:166340","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:3357","NEWT:111225","NEWT:7719","NEWT:29073","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:2767846","NEWT:108061","NEWT:60711","NEWT:2020713","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:2502409","NEWT:212790","NEWT:110368","NEWT:55350","NEWT:1916073","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:468822","NEWT:1912919","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:370038","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:37919","NEWT:342808","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:329854","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:2649329","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:709964","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:156974","NEWT:3714","NCBITaxon:37162","NEWT:270643","NEWT:3715","NEWT:1538","NEWT:2065263","NEWT:199225","NEWT:177437","NEWT:717966","NEWT:9014","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:29022","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:1883426","NEWT:8165","NEWT:96794","NEWT:10401","NEWT:10886","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:1955249","NEWT:215451","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:2714896","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:1608994","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:329032","NEWT:56636","NEWT:2709072","NEWT:2499525","NEWT:55307","NEWT:1122981","NEWT:2853422","NEWT:1122984","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:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:31345","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:141469","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:1578","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:1922344","NEWT:108458","NEWT:5936","NEWT:85692","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:279010","NEWT:291146","NEWT:29466","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:415978","NEWT:235455","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:9054","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:911022","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:717989","NEWT:33952","NEWT:1255232","NEWT:11723","NEWT:445","NEWT:153009","NEWT:1004879","NEWT:261756","NEWT:166314","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:1871049","NEWT:215402","NEWT:1547","NEWT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