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Following treatment, cells were harvested, washed with DPBS without calcium and magnesium and lysed in lysis buffer (50mM Hepes pH 7.5, 150mM NaCl, 1 mM EDTA, 0.1% SDS, 1% NP-40). After Protein concentration measurement 10 µg of the protein extracts were used for sample preparation for MS using the single-pot, solid-phase-enhanced sample-preparation (SP3) strategy (Hughes et al 2019 ). All buffers and solutions were prepared with mass spectrometry (MS)-grade water (Honywell). 10 µg of the protein extract was brought to a final volume of 37.5 µL with water and then supplemented with 4× SP3 lysis buffer (200 mM Hepes pH 8.0, 4% (wt/v) SDS, 40 mM TCEP, 160 mM chloroacetamide). The samples were then heated at 90°C for 6 min and cooled down to room temperature. In order to degrade nucleic acid, the samples were then incubated with 2 µL 3.5 U/µL Benzonase in dilution buffer (20 mM Hepes pH 8.0, 2 mM MgCl2) at 37 °C for 30 min with gentle agitation at 1500 rpm. After Benzonase treatment 3 µL of a 50 µg/µL 1:1 mixture of hydrophilic and hydrophobic carboxylate modified Sera-Mag SpeedBeads, that were washed twice with MS-grade water, were added to the samples and mixed by gently pipetting up and down. Protein binding to the beads was induced by the addition of an equal volume of pure ethanol (10 min, 1000 rpm, 24 °C). After incubation beads were collected by a brief centrifugation step (10 sec, 200 ×g) and the reaction vessels placed on a magnetic stand. Beads were allowed to migrate to the vessel wall for at least 5 min before the supernatant was removed. The beads were then taken up in 180 µL 80% ethanol and transferred to a fresh vessel. Subsequently the beads were washed four times with 180 µL 80% (v/v) ethanol prior to the addition of 100 µL digestion enzyme mix (0.6 μg of trypsin and 0.6 µg LysC in 25 mM ammonium bicarbonate. Samples were incubated at 37 °C for 19 h while shaking (1300 rpm). On the next day, the samples were briefly centrifuged (10 s, 200 ×g) and placed on a magnet for 5 min. The clear solution containing the tryptic peptides was transferred to a new reaction vessel. The beads were taken up in 47 µL 25 mM ammonium bicarbonate and incubated while shaking (2 min, 1000 rpm). The reaction vessels were then again placed on a magnetic stand and after 5 min the cleared supernatant was collected and combined with the recovered first peptide mix, followed by the addition of formic acid (FA) to a final concentration of 2% (v/v) for trypsin inactivation. Sample preparation for proximity-dependent Biotinylation samples : Pull-down samples were prepared following the SP3 strategy (Hughes et al 2019 ).  The samples were washed on bead and then taken up in a slightly modified SP3 Lysis buffer (final concentrations; 1% SDS, 10 mM TCEP, 40 mM Chloracetamide, 50 mM HEPES, 2 mM biotin, final volume 100 µL).  Samples were heated at 90°C for 5 min and cleared by centrifugation. Supernatant was transferred to a fresh reaction vessel. Then, 3 µL of a 50 µg/µL 1:1 mixture of hydrophilic and hydrophobic carboxylate modified Sera-Mag SpeedBeads, that were washed twice with MS-grade water, were added to the samples. Afterwards, the samples were mixed shortly (1 min, 1000 rpm) and collected by short centrifugation (10 s, 200 ×g). Protein binding was induced by the addition of an equal volume of pure ethanol (10 min, 1000 rpm), the beads were collected by a brief centrifugation step (10 sec, 200 ×g) and the reaction vessels placed on a magnetic stand. Beads were allowed to migrate to the vessel wall for at least 5 min before the supernatant was removed. The beads were then taken up in 180 µL 80% ethanol and transferred to a fresh reaction vessel. Subsequently the beads were washed four times with 180 µL 80% (v/v) ethanol prior to the addition of 100 µL digestion enzyme mix (0.6 μg of trypsin and 0.6 µg LysC in 25 mM ammonium bicarbonate). Samples were incubated at 37 °C for 19 h while shaking (1300 rpm). On the next day, the samples were briefly centrifuged (10 s, 200  ×g) and placed on a magnet for 5 min. The clear solution containing the tryptic peptides was transferred to a fresh reaction vessel. The beads were taken up in 47 µL 25 mM ammonium bicarbonate and incubated while shaking (2 min, 1000 rpm). The vessels were then placed on a magnetic stand and after 5 min the cleared supernatant was collected and combined with the recovered first peptide mix, followed by the addition of formic acid (FA) to a final concentration of 2% (v/v) for trypsin inactivation. Sample clean-up for LC-MS/MS: All digests were desalted on home-made C18 StageTips containing two layers of an octadecyl silica membrane (Rappsilber et al 2007 ).  LC-MS settings have been deposited in the Sample_Legend_and_LC-MS_Settings_v01.docx file (part of this submission)"],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["RAW spectra were submitted to an Andromeda (Cox  et al. 2011) search in MaxQuant (v1.6.10.43 or v2.0.3.0) using the default settings (Cox  & Mann 2008). Label-free quantification and match-between-runs was activated (Cox et al. 2014 ). The MS/MS spectra data were searched against the H. sapiens reference databases UP000005640_9606.fasta (one protein per gene 20621 entries, downloaded 10.2020) or UP000005640_2-HomoSapiens(08-2022).fasta (79759 entries, downloaded 08.2022). For PDB experiments we also included the dedicated database ACE_0798_SOI_v01.fasta containing only the APEX2 sequence. All searches included a contaminants database search (as implemented in MaxQuant, 245 entries). The contaminants database contains known MS contaminants and was included to estimate the level of contamination. Andromeda searches allowed oxidation of methionine residues (16 Da) and acetylation of the protein N-terminus (42 Da) as dynamic modifications and the static modification of cysteine (57 Da, alkylation with iodoacetamide). Enzyme specificity was set to “Trypsin/P” with two missed cleavages allowed. The instrument type in Andromeda searches was set to Orbitrap and the precursor mass tolerance was set to ±20 ppm (first search) and ±4.5 ppm (main search). The MS/MS match tolerance was set to ±0.5 Da. The peptide spectrum match FDR and the protein FDR were set to 0.01 (based on target-decoy approach). Minimum peptide length was 7 amino acids. For protein quantification unique and razor peptides were allowed. Modified peptides were allowed for quantification. The minimum score for modified peptides was 40. Label-free protein quantification was switched on, and unique and razor peptides were considered for quantification with a minimum ratio count of 2. Retention times were recalibrated based on the built-in nonlinear time-rescaling algorithm. MS/MS identifications were transferred between LC-MS/MS runs with the “match between runs” option in which the maximal match time window was set to 0.7 min and the alignment time window set to 20 min. The quantification is based on the “value at maximum” of the extracted ion current. At least two quantitation events were required for a quantifiable protein. Further analysis and filtering of the results was done in Perseus v1.6.10.0. (Tyanova et al. 2016 ). For quantification we combined related biological replicates to categorical groups and investigated only those proteins that were found in at least one categorical group in a minimum of 4 out of 5 biological replicates. Comparison of protein group quantities (relative quantification) between different MS runs is based solely on the LFQ’s as calculated by MaxQuant, MaxLFQ algorithm (Cox et al. 2014 )."],"omics_type":["Proteomics"],"labhead":["Farnusch Kaschani"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Analytics Core Facility Essen (ACE), Chemische Biologie, Universität Duisburg-Essen, ZMB, Germany"],"species":["Homo Sapiens (human)"],"publication":["10.1242/JCS.264535"],"submitter_mail":["farnusch.kaschani@uni-due.de"],"submitter_affiliation":["University Duisburg-Essen"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"Analysis of Golgi stress signalling pathways in HeLa cells","description":"Effect of Nigericin on HeLa cells and identification of interaction partners of FAM129A under basal conditions and upon Golgi stress 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