{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076805/231211_IGasic_004_DirectDIA_PARvsKO_Human_QuanID_NoImp_NoSingleHit_Report.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076805/231211_IGasic_004_DirectDIA_PARvsKO_Human_QuanID_NoImp_NoSingleHit_candidates_table.tsv"],"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076805/231211_IGasic_004_DirectDIA_PARvsKO_Human_QuanID_NoImp_NoSingleHit_Report_full.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076805/231211_IGasic_004_DirectDIA_PARvsKO_Human_QuanID_NoImp_NoSingleHit_SettingsSchema_BGS_Factory_Settings.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076805/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076805/231211_IGasic_004_00756_KO_3_SW_600ng.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076805/231211_IGasic_004_00753_PAR_3_SW_600ng.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076805/231211_IGasic_004_00752_PAR_2_SW_600ng.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076805/231211_IGasic_004_00754_KO_1_SW_600ng.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076805/231211_IGasic_004_00751_PAR_1_SW_600ng.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076805/231211_IGasic_004_00755_KO_2_SW_600ng.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076805/uniprotkb_proteome_UP000005640_AND_revi_2026_01_31.fasta"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076805/goa_human.gaf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076805/231211_IGasic_004_DirectDIA_PARvsKO_Human_QuanID_NoImp_NoSingleHit.sne","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076805/231211_IGasic_004_DirectDIA_PARvsKO_Human_QuanID_NoImp_NoSingleHit_Report.params"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["ivana.gasic@unige.ch"],"submitter":["Ana Coelho Almeida"],"technology_type":["Mass Spectrometry","Bottom-up proteomics","Data-independent acquisition"],"software":[""],"submitter_keywords":["Lc-ms","Hela","Tubulin","Cytoskeleton","Human cells","Spheroids"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD076805"],"tissue":["Cell Suspension Culture","Cell Culture","Hela Cell"],"sample_protocol":["Samples were prepared for liquid chromatography/mass spectrometry (LC/MS) using the phase-transfer surfactant method, with minor modifications. First, proteins were extracted and solubilized using buffer containing 12 mM sodium deoxycholate, 12 mM sodium N-dodecanoylsarcosinate, and 100 mM Tris pH 9.0, with EDTA-free Protease Inhibitor Cocktail (Roche). Samples were sonicated for 4 minutes using a Bandelin Sonorex ultrasonic bath (FAUST) with 20-seconds on/20-seconds off cycles. Cell debris was removed after centrifugation at 18,000 × g for 20 minutes at 4°C. Samples were reduced with 10 mM TCEP at 37°C for 30 minutes and alkylated with 20 mM iodoacetamide in the dark at room temperature for 30 minutes. Alkylation reactions were quenched with 75 mM cysteine at room temperature for 10 minutes. Samples were diluted with 3.1 volumes of 50 mM ammonium bicarbonate. Lysyl endopeptidase and trypsin (Promega) were added at a 50:1 ratio of sample protein:enzyme (w/w) and samples were digested for 16 hours at 37 °C. Afterward, 1.77 volumes of ethyl acetate were added, and samples were acidified with trifluoroacetic acid (TFA), which was added to 0.46% (v/v). Following centrifugation at 12,000 × g for 5 minutes at room temperature, samples separated into two phases. The upper organic phase containing sodium deoxycholate was removed, and the lower aqueous phase containing digested tryptic peptides was dried using a centrifugal vacuum concentrator. Digested peptides were dissolved in 300 μL of 0.1% (v/v) TFA in 3% acetonitrile (v/v). Samples were sonicated for 1 minute, centrifuged at 15,000 × g for 15 minutes, and desalted using MonoSpin C18 columns (GL Sciences Inc.). Peptides were eluted from C18 columns using 0.1% TFA in 50% acetonitrile and dried in a vacuum concentrator. Tryptic peptides were dissolved in 0.1% (v/v) formic acid in 2% (v/v) acetonitrile for mass spectrometry analysis. Samples were measured on an EASY nLC 1000 - Orbitrap Fusion Tribrid mass spectrometer equipped with a nanospray Flex™ ion source (ThermoFisher Scientific). Peptides were separated on a self-packed 1.9-μm particle, 75-μm inner diameter, 15 to 20-cm filling length homemade C18 column. A flow rate of 300 nL/min was used with a 114-minute gradient (2–25% solvent B in 100 minutes, 25–45% solvent B in 7 minutes, 45–75% solvent B in 7 minutes). The gradient was followed with two rounds of washing steps, in each step, the gradient switched to 98% solvent B in 1 minute and remained for 2 ×, then switched to 2% solvent B in 1 minute and remained for 2 minutes. After the second round of washing, 2% solvent B was reached in 1 minute and remained for 14 minutes for system equilibration. Solvent A was 0.1% (v/v) formic acid in LC/MS grade water and solvent B was 0.1% (v/v) formic acid in 100% (v/v) acetonitrile. The ion source settings from Tune were used for the mass spectrometer ion source properties."],"repository":["pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["For data-independent acquisition (DIA), data were acquired with 1 full MS and 38 overlapping isolation windows constructed covering the precursor mass range of 350–1200 m/z. For full mass spectrometry, Orbitrap resolution was set to 120,000. AGC target was set to 250% with a maximum injection time (IT) of 60 ms. DIA segments were acquired at resolution of 30,000. AGC target was set to 2000% with a dynamic maximum IT. HCD fragmentation was set to normalized collision energy of 27% covering a fragment ion mass range of 200-2000 m/z. For protein identification and quantification raw files were analyzed using the directDIA+ (Deep) workflow in Spectronaut 20 software (release 20.3.251119, Biognosys) with default settings unless otherwise stated. Briefly, identification was performed using the UniProt reference proteome for human (release 2026_01 - 20’416 entries). Digestion enzyme specificity was set to Trypsin/P considering peptides between 7 and 52 residues with a maximum of two missed cleavages. Modification included carbamidomethylation of cysteine as a fixed modification, and oxidation of methionine and acetyl (protein N-terminus) as variable modifications (maximum of 5). False discovery rate (FDR) control was set to 1% at the PSM, peptide and protein group levels. MS1 and MS2 mass tolerances were set to dynamic with the ideal mass tolerance determined after a first-pass calibration (± 40 ppm). Between 3 to 6 best fragment ions were used per peptide. Single hit proteins were defined by stripped sequence and were excluded. Identified precursor quantification was based on peak area at the MS2 level without imputation of missing values. Protein group quantity is the average of the three best peptides. Cross-run normalization was carried out using normalization based on a retention dependent local regression model65. Protein inference was computed with the parsimony approach using the IDPicker algorithm66. For two-group comparison, differential abundance testing was performed with unpaired t-test. Q-values were the multiple testing corrected p-values. Data processing and visualization were done in R/RStudio (v2022.12.0+353)."],"omics_type":["Proteomics"],"labhead":["Ivana Gasic"],"instrument_platform":[""],"labhead_affiliation":["Department of Molecular and Cellular Biology, University of Geneva, Geneva, Switzerland"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["ana.almeida@unige.ch"],"publication":["Not available"],"submitter_affiliation":["Department of Molecular and Cellular Biology, University of Geneva, Geneva, Switzerland"],"submitter_country":["Switzerland"],"additional_accession":[]},"is_claimable":false,"name":"Tubulin autoregulation tunes microtubule dynamics to support multicellular architecture and viability","description":"Abstract Alpha- and beta-tubulin heterodimers dynamically assemble into microtubules, key cytoskeletal elements involved in intracellular trafficking, cell adhesion, and division. The availability of free tubulins regulates the synthesis of new subunits. In response to excessive soluble αβ-tubulins, tetratricopeptide protein 5 (TTC5) selectively recognizes nascent tubulins at the ribosome, recruiting downstream effectors that degrade their encoding messenger RNAs, in a process known as tubulin autoregulation. Despite its well-characterized molecular framework, the biological relevance of this regulatory pathway remains unknown. Here, using human 3D cellular models, advanced optics, and genetic perturbation of tubulin biosynthesis, we reveal that loss of TTC5-dependent tubulin autoregulation elevates soluble tubulin levels, increasing microtubule stability and disrupting cytoskeletal organization. These defects impair the localization of adhesion molecules at cell-cell junctions and extracellular matrix interfaces, compromising tissue architecture and reducing overall cell viability. Our findings establish tubulin autoregulation as a critical mechanism that tunes microtubule dynamics to sustain cellular integrity and tissue homeostasis.   Note: quantitative mass spectrometry was used to determine the relative abundance of alpha- and beta-tubulin isotypes, as well as, adhesion proteins in TTC5 KO versus parental 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