{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075073/Orbi5546_Proteins_Report.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075073/checksum.txt"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075073/20250225_TTOF_Evo10_DIA_SA_5546_Sample12_S1-B12_1_1175.d.7z","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075073/20250225_TTOF_Evo10_DIA_SA_5546_Sample02_S1-B2_1_1165.d.7z","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075073/20250225_TTOF_Evo10_DIA_SA_5546_Sample03_S1-B3_1_1166.d.7z","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075073/20250225_TTOF_Evo10_DIA_SA_5546_Sample09_S1-B9_1_1172.d.7z","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075073/20250225_TTOF_Evo10_DIA_SA_5546_Sample04re_S1-B4_1_1167.d.7z","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075073/20250225_TTOF_Evo10_DIA_SA_5546_Sample08_S1-B8_1_1171.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075073/20250225_TTOF_Evo10_DIA_SA_5546_Sample06_S1-B6_1_1169.d.7z","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075073/20250225_TTOF_Evo10_DIA_SA_5546_Sample10_S1-B10_1_1173.d.7z","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075073/20250225_TTOF_Evo10_DIA_SA_5546_Sample07_S1-B7_1_1170.d.7z","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075073/20250225_TTOF_Evo10_DIA_SA_5546_Sample05_S1-B5_1_1168.d.7z","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075073/20250225_TTOF_Evo10_DIA_SA_5546_Sample01re_S1-B1_1_1164.d.7z","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075073/20250225_TTOF_Evo10_DIA_SA_5546_Sample11_S1-B11_1_1174.d.7z"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["danieldeltoro@ub.edu"],"submitter":["Barbara Steigenberger"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Neuronal migration","Repulsion","Teneurin","Cortex development","Adhesion"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD075073"],"tissue":["Brain"],"sample_protocol":["Sample preparation Total mouse brain lysates were supplemented with 60 µL of SDC buffer containing 1% sodium deoxycholate (SDC; Sigma-Aldrich), 40 mM 2‑chloroacetamide (CAA; Sigma-Aldrich), 10 mM tris(2‑carboxyethyl)phosphine (TCEP; Thermo Fisher Scientific), and 100 mM Tris (pH 8.0). Samples were sonicated using a Bioruptor Plus (Diagenode) for 10 cycles of 30 seconds at high intensity. Protein digestion was initiated by adding 1 µg Lys‑C (Wako) and incubating the samples for 2 hours at 37 °C, followed by overnight digestion at 37 °C with 1 µg trypsin (Promega). The resulting peptide mixtures were acidified to a final concentration of 1% trifluoroacetic acid (TFA; Merck), and approximately 300 ng of peptides were loaded onto Evosep Pure tips (Evosep).  LC‑MS data acquisition Peptides were eluted from Evotips onto a 15 cm PepSep C18 column (1.5 µm, Bruker Daltonics) using an Evosep One HPLC system (Evosep). The column temperature was maintained at 50 °C, and peptide separation was performed using the 30 SPD method. Eluted peptides were ionized by electrospray and introduced directly into a timsTOF HT mass spectrometer (Bruker). Data were acquired in DIA‑PASEF mode using timsControl. The MS scan range was 100–1700 m/z, with an ion mobility range of 1/K0 = 0.70–1.30 Vs·cm². The dual TIMS analyzer operated with equal ion accumulation and ramp times of 100 ms, yielding a spectra rate of 9.52 Hz. For DIA‑PASEF, precursor masses were scanned from 350.2 to 1199.9 Da, and the same ion mobility range was applied. Collision energy was linearly ramped according to ion mobility, from 45 eV at 1/K0 = 1.30 Vs·cm² to 27 eV at 1/K0 = 0.85 Vs·cm². Forty‑two DIA‑PASEF windows were acquired per TIMS scan using alternating precursor isolation windows, resulting in an estimated cycle time of 2.21 seconds."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Data analysis Raw data were processed in Spectronaut 19.0 (Biognosys) using the directDIA+ library‑free workflow. Spectra were searched against a predicted Mus musculus UniProt database (SwissProt and TrEMBL; downloaded 2023). Cysteine carbamidomethylation was specified as a fixed modification, while methionine oxidation and protein N‑terminal acetylation were included as variable modifications. Protein quantification across samples was performed using MS²‑level label‑free quantification (MaxLFQ)"],"omics_type":["Proteomics"],"labhead":["Daniel del Toro1"],"instrument_platform":[""],"labhead_affiliation":["Dept Biomedical Sciences, School of Medicine and Health Sciences, Institute of Neurosciences, Universitat de Barcelona, E-08036 Barcelona"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"submitter_mail":["steigenberger@biochem.mpg.de"],"publication":["41991904 Berbeira-Santana M, Peregrina C, Okuda K, Zhou JC, Carrasquero-Ordaz M, Roberts AV, Thomas AE, Haanappel E, Chavent M, El Omari K, Baker LA, Pederick DT, Pardon E, Steyaert J, Nägerl UV, Del Toro D, Seiradake E. Structurally exclusive Teneurin complexes orchestrate divergent programs in early cortical development. Nat Commun. 2026 17(1):5292 10.1038/s41467-026-71619-1"],"submitter_affiliation":["MPI of Biochemistry"],"submitter_country":["Germany"],"pubmed_abstract":["Cortical migration is a complex process in which neurons migrate along radial glial cells (RGC) to form functional layers. Teneurins (Ten1-4) play a role by interacting with Latrophilins (Lphn/ADGRL1-3). Teneurins are also known as cell adhesion molecules, but how homophilic and heterophilic Teneurin interactions are integrated is unknown. Here, single-particle-cryo-EM data of Ten2 shows that canonical Latrophilin-binding is sterically incompatible with Ten2-dimerisation, making these interactions exclusive. We engineered surface mutations that specifically disrupt Ten2-Ten2 or Ten2-Latrophilin interactions. These are transferrable to Ten4, suggesting conserved binding mechanisms. Proteomics, in-vivo-gene-editing and super-resolution-microscopy show that Ten4 is expressed along RGC fibres and that migrating neurons switch from low-to-high Ten4-expression. Ten4 expression is highest in the cortical plate where Ten4-Ten4 interactions reduce RGC-attachment. In the intermediate zone, Ten4-Latrophilin interactions are required to promote neuron-RGC association. The results show how Ten4 orchestrates different stages of cortical migration by using a structural/functional switch between high-affinity Lphn interactions and low-affinity homophilic interactions, underpinning the integration of distinct migration programmes."],"pubmed_title":["Structurally exclusive Teneurin complexes orchestrate divergent programs in early cortical development."],"pubmed_authors":["Berbeira-Santana Miguel M, Peregrina Claudia C, Okuda Kosuke K, Zhou Jin Chuan JC, Carrasquero-Ordaz Maria M, Roberts Amy V AV, Thomas Anne E AE, Haanappel Evert E, Chavent Matthieu M, El Omari Kamel K, Baker Lindsay A LA, Pederick Daniel T DT, Pardon Els E, Steyaert Jan J, Nägerl U Valentin UV, Del Toro Daniel D, Seiradake Elena E"],"additional_accession":[]},"is_claimable":false,"name":"Teneurin-4 switches between self-recognition and canonical Latrophilin binding to direct neuronal migration","description":"Cortical migration is a complex process in which neurons migrate along radial glial cells (RGC) to form functional layers. Teneurins (Ten1-4) play a role by interacting with Latrophilins (Lphn/ADGRL1-3). Teneurins are also known as cell adhesion molecules, but how homophilic and heterophilic Teneurin interactions are integrated is unknown. Here, single-particle-cryo-EM data of Ten2 shows that canonical Latrophilin-binding is sterically incompatible with Ten2-dimerisation, making these interactions exclusive. We engineered surface mutations that specifically disrupt Ten2-Ten2 or Ten2-Latrophilin interactions. These are transferrable to Ten4, suggesting conserved binding mechanisms. Proteomics, in-vivo-gene-editing and super-resolution-microscopy show that Ten4 is expressed along RGC fibres and that migrating neurons switch from low-to-high Ten4-expression. Ten4 expression is highest in the cortical plate where Ten4-Ten4 interactions reduce RGC-attachment. In the intermediate zone, Ten4-Latrophilin interactions are required to promote neuron-RGC association. The results show how Ten4 orchestrates cortical migration by exclusive structural mechanisms, underpinning the integration of distinct migration 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