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Three 10-cm dishes containing 70% confluent HEK293T cells are transfected with FMRP-miniTurbo using PEI (1 μg/ml) for 24 h, 50 μM biotin is added to cells for 18 h, and cells are collected and lysed in 1 ml of lysis buffer. After centrifugation at 14,000 × g for 15 min, supernatant is collected and incubated with 25 μl Pierce™ High Capacity NeutrAvidin™ Agarose (29202, Thermofisher) at 4°C overnight. Beads are collected by centrifuging at 500 × g for 5 min and washed twice with lysis buffer. Finally, beads are resuspended in loading buffer and boiled for 10 min followed by Western blot analysis. The proteins are enriched by SDS-PAGE, and Coomassie blue staining is performed. The gel slice is digested by trypsin, and peptides are detected by LC-MS/MS in Stanford University Mass Spectrometry."],"repository":["Pride"],"labhead":["Bingwei Lu"],"instrument_platform":[""],"submission_type":["COMPLETE"],"labhead_affiliation":["Pathology, Stanford University"],"publication":["41061044 Geng J, Wang X, Pan J, Khan D, Pimcharoen S, Zhang Y, Mosammaparast N, Hirose S, Petrucelli L, Brandman O, Qi LS, Lu B. CRISPR activation of the ribosome-associated quality control factor ASCC3 ameliorates fragile X syndrome phenotypes in mice. Sci Transl Med. 2025 17(819):eadq3551 10.1126/scitranslmed.adq3551"],"submitter_affiliation":["Stanford Univeristy"],"labhead_mail":["bingwei@stanford.edu"],"technology_type":["Mass Spectrometry","Top-down proteomics"],"disease":["Fragile X Syndrome"],"submitter_keywords":["Hek293t"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067852"],"quantification_method":[""],"modification":[""],"data_protocol":["Samples from solution or polyacrylamide gels are digested using trypsin; peptides are purified, concentrated, and loaded onto a nanoLC C18 analytical column. Multiply charged peptides are selected by abundance for sequencing by the mass spectrometer. Multiple fragmentation modes can be used. Samples containing these detergents/surfactants must be run on a 1D PAGE gel. The amount of time the mass spectrometer spends interrogating the sample can be adjusted to sample complexity; in many instances we can identify >500 proteins in 1hr acquisition time. The MS data is converted to the necessary format and database searched (Sequest and/or Byonic) against the appropriate database"],"omics_type":["Proteomics"],"species":["Homo Sapiens (human)"],"submitter_mail":["jigeng@stanford.edu"],"submitter_country":["United States"],"doi":["10.6019/PXD067852"],"pubmed_abstract":["Loss of fragile X messenger ribonucleoprotein (FMRP) causes fragile X syndrome (FXS), an inherited neurodevelopmental disorder resulting in intellectual disability and autism spectrum disorder; however, the molecular function of FMRP remains uncertain. Here, using cell lines and fibroblasts and induced pluripotent stem cell-derived neurons from healthy individuals and patients with FXS, we showed that FMRP regulates collided ribosomes by recruiting activating signal cointegrator 1 complex subunit 3 (ASCC3), an early-acting ribosome-associated quality control (RQC) factor to collided ribosomes, and either positively or negatively regulating translation, depending on transcript context. Disease-associated <i>ASCC3</i> variants that perturbed ASCC3-FMRP interaction were also found to be defective in ribosome association and handling of collided ribosomes. In cells of a patient with FXS and the <i>Fmr1</i> KO mouse model, ASCC3 abundance was reduced, and overexpression of ASCC3 in the brains of fetal <i>Fmr1</i> KO mice promoted neuronal migration. In addition, CRISPR-mediated activation of ASCC3 by lateral ventricular injection of adeno-associated virus (AAV) ameliorated synaptic defects and improved locomotor activity, cognitive deficits, obsessive-compulsive-like behavior, and social interaction deficits after 1 month in 2-month-old <i>Fmr1</i> KO mice compared with untreated <i>Fmr1</i> KO controls. In conclusion, these data implicated FMRP in the handling of collided ribosomes to maintain protein homeostasis during neurodevelopment and synaptogenesis and demonstrated proof of concept that targeting RQC may offer alternative treatment strategies for FXS."],"pubmed_title":["CRISPR activation of the ribosome-associated quality control factor ASCC3 ameliorates fragile X syndrome phenotypes in mice."],"pubmed_authors":["Geng Ji J, Wang Xiying X, Pan Jie J, Khan Danish D, Pimcharoen Sopida S, Zhang Yongjie Y, Mosammaparast Nima N, Hirose Susumu S, Petrucelli Leonard L, Brandman Onn O, Qi Lei S LS, Lu Bingwei B"],"additional_accession":[]},"is_claimable":false,"name":"CRISPR activation of the ribosome-associated quality control factor ASCC3 ameliorates fragile X syndrome phenotypes in mice","description":"Loss of fragile X messenger ribonucleoprotein (FMRP) causes fragile X syndrome (FXS), an inherited neurodevelopmental disorder  resulting in intellectual disability and autism-spectrum disorder. Despite the prevalence of the FXS, the molecular function of FMRP remains uncertain. Here, we showed that FMRP regulates collided ribosomes. Activating signal cointegrator 1 complex subunit 3 (ASCC3), an early-acting ribosome-associated quality control (RQC) factor, was identified as an FMRP-interacting protein. Mechanistically, FMRP recruits ASCC3 to collided ribosomes and either positively or negatively regulates translation, depending on transcript context. Disease-associated ASCC3 variants that perturbed ASCC3-FMRP interaction were defective in ribosome association and handling of collided ribosomes. In FXS patient cells and mouse models of FXS, ASCC3 abundance was reduced, and Clustered Regularly Interspaced Short Palindromic Repeats-mediated activation (CRISPRa) of ASCC3 overcame challenges to conventional gene delivery approaches presented by the sheer size of ASCC3  and rescued synaptic defects and behavioral deficits. In conclusion, these data implicated FMRP in the handling of collided ribosomes to maintain protein homeostasis during neurodevelopment and synaptogenesis and showed. Proof-of-concept that targeting RQC may offer alternative treatment strategies for 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