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Wright"],"technology_type":["Affinity purification coupled with mass spectrometry proteomics","Mass Spectrometry","Shotgun proteomics"],"software":[""],"submitter_keywords":["Er stress","Ire1a","Gpr89","Triple negative breast cancer"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD031422"],"tissue":["Cell Culture"],"sample_protocol":["Whole cell lysates were incubated with anti-GPR89 antibody coupled to Protein A Dynabeads. On bead digestion was performed as previously described (Hillier et al., Cell Reports 2019).   Mass spectrometry analysis: Peptides from large-scale inmunoprecipitations were analyzed with online nanoLC-MS/MS on an Orbitrap Fusion Tribrid mass spectrometer coupled with an Ultimate 3000 RSLCnano System. Samples were first loaded and desalted on a nanotrap (100 µm id x 2 cm) (PepMap C18, 5 µ) at 10 µl/min with 0.1% formic acid for 10 min and then separated on an analytical column (75 µm id x 50 cm) (PepMap C18, 2µ) over a 90 min linear gradient of 8-32% CH3CN/0.1% formic acid at 300 nl/min, and the total cycle time was 120 min. The Orbitrap Fusion was operated in standard data-dependent acquisition. The survey scans (m/z 375-1500) were acquired in the Orbitrap at a resolution of 12000 at m/z 200. Multiply charged ions (z = 2 – 6) with intensity threshold at 8,000 counts were fragmented in HCD (higher collision dissociation) cell at 32% collision energy, with AGC at 10,000 and 50 ms maximum injection time, and isolation window at 1.6. The dynamic exclusion time was set at 45s with ±10ppm.  Whole Proteome Analysis  Preparation and TMT Labelling. Cell pellets and tissue samples were dissolved in 150 μL lysis buffer containing 1% sodium deoxycholate (SDC), 100 mM triethylammonium bicarbonate (TEAB), 10% isopropanol, 50 mM NaCl and Halt protease and phosphatase inhibitor cocktail (100X) (Thermo, #78442) on ice, assisted with pulsed probe sonication for 15 sec and 30 sec respectively. Lysates were centrifuged at 12,000 rpm for 10 min and the supernatant was boiled at 90 °C for 5 min on a thermomixer and sonicated for another 5 sec. Protein concentration was measured with the Coomassie Plus Bradford Protein Assay (Pierce) according to manufacturer’s instructions. Protein aliquots of 100 μg were reduced with 5 mM tris-2-carboxyethyl phosphine (TCEP) for 1 h at 60 °C and alkylated with 10 mM Iodoacetamide (IAA) for 30 min in the dark, followed by overnight trypsin digestion (trypsin final concentration 75 ng/μL, Pierce). Peptides were labelled with the TMT 11plex reagents (Thermo) according to manufacturer’s instructions. The mixture was acidified with 1% formic acid and the precipitated SDC was removed by centrifugation. Sample was finally dried with a centrifugal vacuum concentrator. High-pH Reversed-Phase Peptide Fractionation and LC-MS Analysis. Peptides were fractionated offline with high-pH Reversed-Phase (RP) chromatography using the XBridge C18 column (2.1 x 150 mm, 3.5 μm, Waters) on a Dionex UltiMate 3000 HPLC system. Mobile phase A was 0.1% ammonium hydroxide and mobile phase B was acetonitrile, 0.1% ammonium hydroxide. The TMT labelled peptide mixture was fractionated with a multi-step gradient elution method at 0.2 mL/min as follows: for 5 minutes isocratic at 5% B, for 35 min gradient to 35% B, gradient to 80% B in 5 min, isocratic for 5 minutes and re-equilibration to 5% B. Fractions were collected every 42 sec, combined in 28 fractions and vacuum dried. LC-MS analysis was performed on a Dionex UltiMate 3000 UHPLC system coupled with the Orbitrap Lumos Mass Spectrometer (Thermo Scientific). Each peptide fraction was reconstituted in 40 μL 0.1% formic acid and 10 μL were loaded to the Acclaim PepMap 100, 100 μm × 2 cm C18, 5 μm, trapping column at 10 μL/min flow rate. Samples were analysed with the EASY-Spray C18 capillary column (75 μm × 50 cm, 2 μm) at 45 °C. Mobile phase A was 0.1% formic acid and mobile phase B was 80% acetonitrile, 0.1% formic acid. The gradient method was: for 90 min gradient 5%-38% B, for 10 min up to 95% B, for 5 min isocratic at 95% B, re-equilibration to 5% B in 5 min, for 10 min isocratic at 5% B at flow rate 300 nL/min. Precursor ions were selected in the range of 375-1,500 m/z with mass resolution of 120 k, AGC 4×105 and max IT 50 ms with the top speed mode in 3 sec and were isolated for CID fragmentation with quadrupole isolation width 0.7 Th. Collision energy was 35% with AGC 1×104 and max IT 50 ms. Quantification was obtained at the MS3 level with HCD fragmentation of the top 5 most abundant CID fragments isolated with Synchronous Precursor Selection (SPS). Quadrupole isolation width was 0.7 Th, collision energy was 65% and AGC setting 1×105 with 105 ms max IT. The HCD MS3 spectra were acquired for the mass range 100-500 with 50k resolution. Targeted precursors were dynamically excluded for further fragmentation for 45 seconds with 7 ppm mass tolerance."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Raw files were processed with Proteome Discoverer v2.3 (Thermo Fisher Scientific). Database searches were performed with Mascot (Matrix Science) against the human SwissProt database (v. January 2018) appended with the cRAP database. The search parameters were: trypsin/P digestion, 2 missed cleavages, 20 ppm mass tolerance for MS, 0.5 Da mass tolerance for MS/MS, with variable modifications of acetyl (N-terminal), oxidation (M), and deamidation (N, Q). Database search results were refined through processing with Percolator (significance threshold < 0.05, FDR < 1%).  Whole Proteome:  Database search and protein quantification. The mass spectra were analysed in Proteome Discoverer 2.2 (Thermo Scientific) with the SequestHT search engine for protein identification and quantification. The precursor and fragment ion mass tolerances were 20 ppm and 0.5 Da respectively. Spectra were searched for fully tryptic peptides with maximum 2 missed-cleavages. TMT6plex at N-terminus/K and Carbamidomethyl at C were selected as static modifications. Oxidation of M and Deamidation of N/Q were selected as dynamic modifications. Peptide confidence was estimated with the Percolator node and peptides were filtered at q-value<0.01 based on decoy database search. All spectra were searched against reviewed UniProt human or mouse protein entries. The reporter ion quantifier node included a TMT 11plex quantification method with an integration window tolerance of 15 ppm at the MS3 level. Only unique peptides were used for quantification, considering protein groups for peptide uniqueness. Only peptides with average reporter signal-to-noise>3 were used for protein quantification."],"omics_type":["Proteomics"],"labhead":["Jyoti Choudhary"],"instrument_platform":[""],"labhead_affiliation":["The Institute of Cancer Research"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["james.wright@icr.ac.uk"],"publication":["Not available"],"submitter_affiliation":["The Institute of Cancer Research"],"submitter_country":["United Kingdom"],"additional_accession":[]},"is_claimable":false,"name":"Localisation of the Golgi pH regulator GPR89 extends to the endoplasmic reticulum and confers selective dependency in breast cancer","description":"Identification of targetable biology in breast cancer is an important unmet need, particularly for triple negative breast cancer (TNBC) where outcomes are poor and there are few licensed targeted therapies. Here, we identify the anion channel GPR89 as a novel breast cancer oncogene relevant in TNBC and other subtypes. We demonstrate that GPR89 extends its usual localisation from the Golgi in non-malignant cells to Endoplasmic Reticulum (ER)/Golgi in breast cancer cells where it regulates ER pH. Extended localisation of GPR89, to include mitochondria-ER associated membranes (MAMs), is also associated with GPR89 dependency. We further demonstrate that GPR89 helps breast cancer cells survive ER stress through modulation of the unfolded protein response and helps support cancer cells to rewire their metabolism towards glycolysis by extending localisation to the MAMs. This suggests the GPR89 anion channel as a potential novel drug target relevant to aggressive breast cancers with limited targeted therapy 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