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de Matos Ferraz FrancoData-dependent acquisitionMass SpectrometryHumanP115Hek293tLc-msmsSec16aUso1https://www.ebi.ac.uk/pride/archive/projects/PXD075617Gel samples were destained with 50% v/v acetonitrile and 50 mM ammonium bicarbonate, reduced with 10 mM DTT, and alkylated with 55 mM iodoacetamide. Digestion was with 6 ng/?l trypsin (Promega, UK) overnight at 37°C, and peptides extracted in 2% v/v formic acid 2% v/v acetonitrile, and analysed by nano-scale capillary LC-MS/MS using an Ultimate U3000 HPLC (ThermoScientific Dionex, San Jose, USA) to deliver a flow of approximately 300 nL/min. A µ-precolumn cartridge C18 Acclaim PepMap 100 (5 µm, 300 µm x 5mm (ThermoScientific Dionex, San Jose, USA), trapped the peptides prior to separation on a C18 Acclaim PepMap100 3 µm, 75 µm x 250 mm (ThermoScientific Dionex, San Jose, USA). Peptides were eluted with a 65 minute gradient of acetonitrile (5 to 40%). The analytical column outlet was directly interfaced via a modified nano-flow electrospray ionisation source, with a hybrid linear quadrupole ion trap mass spectrometer (Orbitrap QExactive, ThermoScientific, San Jose, USA). Data dependent analysis was carried out, using a resolution of 60,000 for the full MS spectrum, followed by ten MS/MS spectra in the linear ion trap. MS spectra were collected over a m/z range of 200?1800. MS/MS scans were collected using threshold energy of 35 for collision induced dissociation.PrideNot availableLC-MS/MS data were then searched against the uniprot database, using the Mascot search engine programme (Matrix Science, UK). Database search parameters were set with a precursor tolerance of 10 ppm and a fragment ion mass tolerance of 0.8 Da. One missed enzyme cleavages were allowed and variable modifications for oxidized methionine and fixed for carbamidomethylated cysteine.ProteomicsSean MunroPARTIALDivision of Cell Biology MRC Laboratory of Molecular Biology Francis Crick Avenue Cambridge CB2 0QH, UKHomo Sapiens (human)42169630 Yakunin I, Gillingham AK, Pereira C, Gershlick DC, Munro S. The Golgi vesicle tether p115/USO1 can bind directly to the ER exit site organiser Sec16A. J Cell Sci. 2026:jcs.264894 10.1242/jcs.264894cffranco@mrclmb.ac.ukMRC Laboratory of Molecular Biology Francis Crick Avenue Cambridge Biomedical Campus Cambridge CB2 0QHUnited KingdomNewly made secretory and membrane proteins exit the endoplasmic reticulum (ER) in COPII vesicles that form at specialised ER exit sites. These exit sites are typically near to the early Golgi compartments that receive these vesicles. A key player in the delivery of vesicles to the early Golgi is p115 (USO1), a homodimer with a folded head domain and a coiled-coil tail that is anchored to Golgi membranes. p115 has been shown to capture vesicles and to bind to SNARE proteins to promote membrane fusion. Here we report that the head domain of human p115 can bind directly to Sec16A, a large scaffolding protein that organises ER sites and promotes COPII vesicle formation. Structural prediction and deletion mapping define the region of interaction to a conserved motif in the unstructured N-terminal region of Sec16A, and mutations in p115 that block motif binding reduce the efficiency of secretion. This interaction could potentially allow a subset of p115 molecules to reach across from the early Golgi to ER exit sites to contribute to the large-scale organisation of the early secretory pathway.The Golgi vesicle tether p115/USO1 can bind directly to the ER exit site organiser Sec16A.Yakunin Igor I, Gillingham Alison K AK, Pereira Conceição C, Gershlick David C DC, Munro Sean SfalseIdentification of p115 interacting proteins from HEK293T cellsThe protein p115 is a key player in the delivery of vesicles from the endoplasmic reticulum to the early Golgi. The protein is a homodimer with a folded head domain and a coiled-coil tail that is anchored to Golgi membranes. p115 has been shown to capture vesicles and to bind to SNARE proteins to promote membrane fusion. This project was to look for more interaction partners of p115 by expressing GFP fusions to the full length protein or to either the head or the tail alone. These fusions were expressed in HEK293T cells and co-precipitating proteins identified by mass-spectrometry and compared to those found with precipitation of GFP alone.2026-06-022026-03-13PXD075617NEWT:1773NEWT:3555NEWT:38783NEWT:1182590NEWT:2NEWT:10090NEWT:935293NEWT:749200NEWT:35554NEWT:4120NEWT:5693NEWT:347515NEWT:1216979NEWT:307972NEWT:92867NEWT:990346NEWT:544496NEWT:5334NEWT:145953NEWT:257309NEWT:284812NEWT:115104NCBITaxon:1313NEWT:43330NEWT:67825NEWT:44544NEWT:13076NEWT:373995NEWT:544404NEWT:3702NEWT:8839NEWT:4232NEWT:990119NEWT:1736309NEWT:4113NEWT:7227NEWT:11298NEWT:7469NEWT:885318NEWT:171101NEWT:876138NEWT:4081NEWT:554NEWT:5691NEWT:408170NEWT:260710NEWT:106592NEWT:237561NEWT:9913NEWT:10036NEWT:4100NEWT:7574NEWT:1351NEWT:1076NEWT:6763NEWT:7215NEWT:803NEWT:8030NEWT:380394NEWT:272563NEWT:507601NEWT:1639NEWT:188229NEWT:4909NCBITaxon:79857NEWT:746360NEWT:6239NEWT:1589NEWT:135588NEWT:135622NEWT:216257NEWT:6915NEWT:9986NEWT:101510NEWT:95486NEWT:3880NEWT:58002NEWT:9103NEWT:4577NEWT:5664NEWT:2157NEWT:146479NEWT:1000589NEWT:145943NEWT:85962NEWT:160488NEWT:317447NEWT:3635NEWT:7955NCBITaxon:2NEWT:235443NEWT:985076NEWT:7959NEWT:2261NEWT:3197NEWT:9615NEWT:884019NEWT:4565NEWT:1264690NEWT:169963NCBITaxon:38727NEWT:36329NEWT:34305NEWT:59729NCBITaxon:183674NEWT:224308NEWT:626528NEWT:139927NEWT:4558NEWT:9606NEWT:367830NEWT:243230NEWT:931281NEWT:373153NEWT:7029NEWT:1283300NEWT:334747NEWT:470NCBITaxon:79824NCBITaxon:4563NEWT:3218NEWT:5759NEWT:9838NCBITaxon:9615NEWT:1736231NEWT:1193501NEWT:6287NEWT:2242NEWT:6326NEWT:9796NEWT:2762NEWT:5476NEWT:562NEWT:260707NEWT:287NEWT:10117NEWT:10239NEWT:10116NEWT:1280NEWT:1836NEWT:1735272NEWT:29760NEWT:260705NEWT:80863NEWT:1148NEWT:4932NEWT:70448NEWT:9825NEWT:3603NEWT:698936NEWT:2759NEWT:39946NEWT:11676NEWT:9823NEWT:100226NCBITaxon:6073NEWT:4530NEWT:4896NEWT:6279NEWT:7370NEWT:573NEWT:6282NEWT:7091NEWT:1134506421696300000-0003-2288-1518