Prideapplication/xmlftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/10/PXD077066/BackExchange_CnnC.xlsxftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/10/PXD077066/File_Description_Pride.xlsxftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/10/PXD077066/HDXresults_CnnC_StateData.csvftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/10/PXD077066/20251029_S_SBr_CnnC_78-208_Nep2Pep_Low_01_IA_final_peptide.csvftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/10/PXD077066/20251028_S_SBr_CnnC-1-208_Nep2Pep_Med_01_IA_final_peptide.csvftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/10/PXD077066/20251029_S_SBr_CnnC_78-208_Nep2Pep_High_01_IA_final_peptide.csvftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/10/PXD077066/20251029_S_SBr_CnnC_78-208_Nep2Pep_Med_01_IA_final_peptide.csvftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/10/PXD077066/20251028_S_SBr_CnnC-1-208_Nep2Pep_Low_01_IA_final_peptide.csvftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/10/PXD077066/HDXresults_CnnC_ClusterData.csvftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/10/PXD077066/20251029_S_SBr_CnnC_1-77_Nep2Pep_Low_01_IA_final_peptide.csvftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/10/PXD077066/20251029_S_SBr_CnnC_1-208_Nep2Pep_High_01_IA_final_peptide.csvftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/10/PXD077066/Raw_Data_CnnC.zipprimary200OKsebastien.brier@pasteur.frSébastien BrierMass SpectrometryMSENot availableHdx-msNmrAutoinhibitionCm1 domainSaxsΓ-turcshttps://www.ebi.ac.uk/pride/archive/projects/PXD077066Sample processing protocol Sample preparation for HDX-MS: Protein samples (10 µM) were equilibrated at 20°C for 30 min before initiating continuous labelling. Exchange was triggered by diluting 18.0 µL of protein with 112 µL of deuterated buffer (50 mM Tris, 300 mM NaCl, 0.5 mM TCEP, pD 7.5), resulting in a final deuterium excess of 86%. Labelling was performed at 20°C for various time intervals (10 s, 1 min, 10 min, 30 min, 60 min, and 120 min). At each time point, the reaction was quenched by mixing 20 µL of the sample with 40 µL of ice-cold quench buffer (0.3% formic acid, 4°C), achieving a final pH of 2.5 to minimize back-exchange. Quenched samples were immediately snap-frozen in liquid nitrogen and stored at -80°C. Undeuterated controls were prepared following the same protocol. Fully deuterated controls were prepared as described in Petrele et al. All samples were prepared in triplicate. HDX-MS data acquisition: Frozen samples were rapidly thawed and injected into a nanoACQUITY UPLC system with an HDX manager maintained at 0°C. Online digestion was performed using a Nep2/pepsin immobilized column (Affipro) for 2 min at 20°C. Resulting peptides were trapped on a C18 VanGuard BEH column and separated over 10 min using an ACQUITY UPLC BEH C18 analytical column (Waters Corp) with an 5 to 40% acetonitrile gradient in 8 min at 40 µL/min. To prevent carry-over, the pepsin column was washed with 1% formic acid, 5% acetonitrile, 1.5 M guanidinium chloride (pH 2.0) followed by blank injections between runs. Mass spectra (m/z 50–1950) were acquired on a Synapt G2-Si HDMS mass spectrometer (Waters Corp) with source parameters optimized for peptide analysis: capillary voltage 2.6 kV, sampling cone 30 V, and desolvation temperature 150°C. Peptides were identified in undeuterated samples using MSE data-independent acquisition. To maximize sequence coverage, fragmentation was conducted using three distinct collision energy ramps (Low: 10–30 V; Med: 15–35 V; High: 20–45 V).PrideNot availableData processing protocol Peptide maps for aa 1–208, aa1-77, and aa78-208 were generated using ProteinLynx Global SERVER (PLGS) 3.0 with a 4% false discovery rate. Maps were refined in DynamX 3.0 using the following PLGS filters: minimum intensity of 10,000, 0.4 products per amino acid, and a maximum mass error of 5.0 ppm. This yielded 82 peptides covering 96.6% of the aa1-208 sequence with a redundancy of 5.82, 28 peptides covering 100% of the aa1-77 sequence with a 4.23 redundancy, and 46 peptides covering 93% of the aa78-208 sequence with a redundancy of 5.71. Centroid masses were extracted for all time points, and results are reported as relative deuterium uptake or fractional exchange (normalized to the theoretical maximum number of exchangeable backbone amides in 86% deuterium excess), without correction for back-exchange.ProteomicsSébastien BrierBiological NMR and HDX-MS Platform, Institut Pasteur, Université Paris Cité, CNRS UMR 3528, 75015 Paris, FrancePARTIALDrosophila Melanogaster (fruit Fly)42814412 Elfarkouchi A,Vitard A,Mammri L,Brier S,Tanneur L,Hu C,Thureau A,Joly N,Ochsenbein F,Conduit PT A structural model for the autoinhibition of the γ-TuRC-activating CM1 domain. J Cell Biol. 2026 Nov 2 225(11) 10.1083/jcb.202605160sebastien.brier@pasteur.frHydrogen deuterium exchange (hdx-ms)Institut Pasteur, Université Paris Cité, BioNMR and HDX-MS facility, Center for Technological Resources and Research, Chemistry and Structural Biology Department, UMR CNRS 3528, F-75015 Paris, FranceFranceMicrotubule nucleation by γ-tubulin ring complexes (γ-TuRCs) must be spatiotemporally controlled to avoid major cell division errors. γ-TuRCs are activated by the centrosome-specific binding of a highly conserved centrosomin motif 1 (CM1) domain, but how binding is prevented in the cytosol remains unclear. We provide the first structural explanation for CM1 autoinhibition, revealing that stable intramolecular interactions mediate cooperative folding to block γ-TuRC-binding interfaces. Using various structural approaches, we show that CM1 forms a conserved dimeric coiled-coil hairpin that sequesters a key phenylalanine residue essential for γ-TuRC binding. This appears sufficient for autoinhibition in humans, but in flies autoinhibition requires the association of an upstream CM1 autoinhibition (CAI) domain, which forms a 4-helix dimer that covers the opposite phenylalanine residue of the hairpin dimer. Collectively, the data provide the first structural model for CM1 autoinhibition and reveal evolutionary differences across species.A structural model for the autoinhibition of the γ-TuRC-activating CM1 domain.Elfarkouchi Abir A, Vitard Arthur A, Mammri Léa L, Brier Sébastien S, Tanneur Lola L, Hu Cécile C, Thureau Aurélien A, Joly Nicolas N, Ochsenbein Francoise F, Conduit Paul T PTfalseA structural model for the autoinhibition of the γ-TuRC-activating CM1 domainMicrotubule nucleation by γ-tubulin ring complexes (γ-TuRCs) must be spatiotemporally controlled to avoid major cell division errors. γ-TuRCs are activated by the centrosome-specific binding of a highly conserved Centrosomin Motif 1 (CM1) domain, but how binding is prevented in the cytosol remains unclear. We provide the first structural explanation for CM1 autoinhibition, revealing that stable intramolecular interactions mediate cooperative folding to block γ-TuRC binding interfaces. Using various structural approaches, we show that the CM1 forms a conserved dimeric coiled-coil hairpin that sequesters a key phenylalanine residue essential for γ-TuRC binding. This appears sufficient for autoinhibition in humans, but in flies autoinhibition requires the additional association of an upstream “CM1 autoinhibition” (CAI) domain, which covers the opposite phenylalanine residue of the dimer. Collectively, the data provide the first structural model for CM1 autoinhibition and reveal evolutionary differences across 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