{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059191/checksum.txt"],"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059191/20240706_Simone_Hari_WT-control3.msf"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059191/20240706_Simone_Hari_R3-IP3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059191/20240706_Simone_Hari_R3-IP1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059191/20240706_Simone_Hari_112-control2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059191/20240706_Simone_Hari_R13-IP2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059191/20240706_Simone_Hari_WT-control3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059191/20240706_Simone_Hari_W3-IP2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059191/20240706_Simone_Hari_WT-control1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059191/20240706_Simone_Hari_112-control3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059191/20240706_Simone_Hari_R13-IP1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059191/20240706_Simone_Hari_112-control1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059191/20240706_Simone_Hari_WT-control2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059191/20240706_Simone_Hari_R13-IP3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059191/20240706_Simone_Hari_W3-IP3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059191/20240706_Simone_Hari_R3-IP2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059191/20240706_Simone_Hari_W3-IP1.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059191/Mouse_SwissProt_March2024.fasta"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["simone.sidoli@einsteinmed.edu"],"submitter":["Simone Sidoli"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Mutations","Prc1","Neurodevelopment","Polycomb","Rnf2"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD059191"],"sample_protocol":["S-trap protein digestion Immunoprecipitates were digested on the beads for mass spectrometry analysis. Specifically, beads were resuspended in 20 µL of 5 mM DTT and 50 mM ammonium bicarbonate (pH = 8), and left on the bench for about 1 hour for disulfide bond reduction. Samples were then alkylated with 20 mM iodoacetamide in the dark for 30 minutes. Afterward, 500 ng of trypsin was added for overnight digestion at room temperature.   Sample desalting Prior to mass spectrometry analysis, samples were desalted using a 96-well plate filter (Orochem) packed with 1 mg of Oasis HLB C-18 resin (Waters). Briefly, the samples were resuspended in 100 µl of 0.1% TFA and loaded onto the HLB resin, which was previously equilibrated using 100 µl of the same buffer. After washing with 100 µl of 0.1% TFA, the samples were eluted with a buffer containing 70 µl of 60% acetonitrile and 0.1% TFA and then dried in a vacuum centrifuge.  LC-MS/MS Acquisition and Analysis Samples were resuspended in 10 µl of 0.1% TFA and loaded onto a Dionex RSLC Ultimate 300 (Thermo Scientific), coupled online with an Orbitrap Fusion Lumos (Thermo Scientific). Chromatographic separation was performed with a two-column system, consisting of a C-18 trap cartridge (300 µm ID, 5 mm length) and a picofrit analytical column (75 µm ID, 25 cm length) packed in-house with reversed-phase Repro-Sil Pur C18-AQ 3 µm resin. Peptides were separated using a 90 min gradient from 4-30% buffer B (buffer A: 0.1% formic acid, buffer B: 80% acetonitrile + 0.1% formic acid) at a flow rate of 300 nl/min. The mass spectrometer was set to acquire spectra in a data-dependent acquisition (DDA) mode. Briefly, the full MS scan was set to 300-1200 m/z in the orbitrap with a resolution of 120,000 (at 200 m/z) and an AGC target of 5x10e5. MS/MS was performed in the ion trap using the top speed mode (2 secs), an AGC target of 1x10e4 and an HCD collision energy of 35."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Proteome raw files were searched using Proteome Discoverer software (v2.5, Thermo Scientific) using SEQUEST search engine and the SwissProt mouse database (updated April 2023). The search for total proteome included variable modification of N-terminal acetylation, and fixed modification of carbamidomethyl cysteine. Trypsin was specified as the digestive enzyme with up to 2 missed cleavages allowed. Mass tolerance was set to 10 pm for precursor ions and 0.2 Da for product ions. Peptide and protein false discovery rate was set to 1%. Following the search, data was processed as previously described. Briefly, proteins were log2 transformed, normalized by the average value of each sample and missing values were imputed using a normal distribution 2 standard deviations lower than the mean. Statistical regulation was assessed using heteroscedastic T-test (if p-value < 0.05).  Data distribution was assumed to be normal but this was not formally tested."],"omics_type":["Proteomics"],"labhead":["Simone Sidoli"],"instrument_platform":[""],"labhead_affiliation":["Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, United States"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"submitter_mail":["simone.sidoli@gmail.com"],"publication":["41653922 Borges RL, González-Blanco G, Arigela H, Huang Y, Caeiro LD, Fattakhov N, Lepore S, Garcia-Martinez L, Maurice M, Mehta PD, Park EJ, MacGillivray K, Nehru J, Chau M, Robayo MC, Abad C, Bilbao-Martinez A, Monteiro F, Luo X, Tan S, Bilbao D, Sidoli S, Di Stefano B, Walz K, Saltzman AL, Verdun RE, Shiekhattar R, Morey L. Unbalanced chromatin binding of Polycomb complexes drives neurodevelopmental disorders. Mol Cell. 2026 86(4):604-624.e16 10.1016/j.molcel.2026.01.023"],"submitter_affiliation":["Albert Einstein College of Medicine"],"submitter_country":["United States"],"pubmed_abstract":["The prevalence of neurodevelopmental disorders (NDDs) in children is increasing, yet their underlying causes remain largely unknown. We identified heterozygous mutations in the Polycomb repressive complex 1 (PRC1) E3 ligases RING1 and RNF2 in individuals with NDDs and revealed distinct mechanisms by which they compromise PRC1 activity. We developed cellular and mouse models carrying the Ring1b<sup>R70H</sup> variant, which disrupts PRC1/PRC2 recruitment balance and mis-regulates Polycomb target genes. Allele-specific profiling showed that Ring1b<sup>R70H</sup> preferentially assembles into canonical PRC1 (cPRC1) via the intrinsically disordered region (IDR) of Pcgf2, reducing variant PRC1 (vPRC1) and PRC2.1 binding to chromatin. In Rnf2<sup>WT/R70H</sup> neuroprecursors, Polycomb complexes aberrantly suppress Wnt signaling, diverting neuroprecursors to non-neuronal lineages and halting neurogenesis. Rnf2<sup>R70H/R70H</sup> mice are perinatally lethal, while heterozygotes exhibit altered axonal organization, hippocampal and medial prefrontal cortex (mPFC) neuronal imbalances, reduced sociability, and increased anxiety. Our findings reveal an epigenetic mechanism essential for neurodevelopmental integrity and brain function and demonstrate how mutations in Rnf2 disrupt PRC1 occupancy at chromatin, contributing to NDDs."],"pubmed_title":["Unbalanced chromatin binding of Polycomb complexes drives neurodevelopmental disorders."],"pubmed_authors":["Borges Rodrigo L RL, González-Blanco Gretter G, Arigela Harikumar H, Huang Yingyu Y, Caeiro Lucas D LD, Fattakhov Nikolai N, Lepore Stefano S, Garcia-Martinez Liliana L, Maurice Matea M, Mehta Pushti D PD, Park Emily J EJ, MacGillivray Kailynn K, Nehru Jevithen J, Chau Matthew M, Robayo Maria C MC, Abad Clemer C, Bilbao-Martinez Alicia A, Monteiro Fabiola F, Luo Xi X, Tan Song S, Bilbao Daniel D, Sidoli Simone S, Di Stefano Bruno B, Walz Katherina K, Saltzman Arneet L AL, Verdun Ramiro E RE, Shiekhattar Ramin R, Morey Lluis L"],"additional_accession":[]},"is_claimable":false,"name":"Unbalanced chromatin binding of PRC1 complexes drives neurodevelopmental disorders","description":"Heterozygous de novo missense mutations in genes encoding Polycomb-group (PcG) proteins can cause diverse neurodevelopmental disorders (NDDs), but the underlying mechanisms are not yet understood. Here, we identified novel mutations in the two E3-ligases of the Polycomb Repressive complex 1 (PRC1), RING1 and RNF2, in individuals with NDDs and uncover distinct mechanisms by which PRC1 activity can be compromised. As a proof of concept, we generated embryonic stem cells (ESCs) and a novel mouse model carrying a heterozygous Rnf2 allele with a missense mutation that produces a deleterious Ring1bR70H variant. This variant causes a cell fate change in neuroprecursors (NPCs) towards the non-neuronal lineages glial and microglia. Allele-specific profiling revealed that Ring1bR70H integrates into canonical PRC1 and displaces variant PRC1 from chromatin. As a result, there is a disruption of the PRC1 balance and a deregulation of PcG target genes. We uncovered that mutant NPCs have an aberrant PcG retention and chromatin compaction pattern at key NPC pioneer factors and Wnt signaling genes. Critically, this heterozygous Rnf2 mutation in mice is sufficient to disrupt neural connectivity and structural organization in key brain regions, including the medial prefrontal cortex and hippocampus. Our findings establish Rnf2 as essential for neurodevelopmental integrity and brain function, shedding light on how PRC1 dysfunction contributes to 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