{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070615/proteinGroups.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070615/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070615/250403_WZ_1_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070615/250403_WZ_SC_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070615/250403_WZ_1_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070615/250403_WZ_1_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070615/250403_WZ_SC_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070615/250403_WZ_SC_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070615/250403_WZ_1_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070615/250403_WZ_SC_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070615/250403_WZ_1_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070615/250403_WZ_SC_2.raw"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["bwolozin@bu.edu"],"submitter":["Sophie van der Spek"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Translation","Gemin5","Circpde4b","Alzheimer's disease","Stress"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070615"],"tissue":["Neural Progenitor Cell"],"sample_protocol":["Neuroprogenitor cells were grown in 6-well plates until 100% confluency. For affinity-purification (AP) of circ-PDE4B:protein complexes, cells were crosslinked by UV (4000 x 100 μJ/cm2, three times) (Stratalinker 2400 UV Crosslinker, Stratalinker) before lysis. APs were performed as previously described by Li et. al, 2022 with several adaptations29. In short, per AP experiment, 2 wells were washed with phosphate buffered saline, lysed in 1 mL total lysis buffer (150 mM NaCl, 1 mM EDTA, 0.5% NP40, 20 mM Tris, pH 7.5, supplemented with 250 U/AP RNAse inhibitor (NEB, Cat#M0314L) and 0.5x protease inhibitor (HaltTM, ThermoFisher, Cat#78429)) and transferred to a collection tube. Lysate was then sonicated three times at constant speed for 10 seconds followed by 1 minute cooling on ice (60 Sonic dismembrator, ThermoFisher, setting 6), and additional RNAse and protease inhibitor was spiked in (to a 500U/AP and 1x end-concentration, respectively). Per AP experiment, 400 pmol biotinylated PDB4E-probe (5'AACACTTTTTAATACCACTCCTGGCTTACA/3BioTEG/-3, custom-made, IDT) or Scrambled probe (5'GACAATCTTCCAAATATCGCTTTACTCTCA/3BioTEG/-3, custom-made, IDT) was preheated at 95°C for 10 minutes, followed by cooling on ice for 5 minutes. Cell lysates were centrifuged (12000 x g, 10 minutes, 4°C), supernatants were mixed and split across sample replicates, and incubated with probe for 2 hours at room temperature while rotating.      Per AP, 50 μL of PierceTM Streptavidin Magnetic Beads (ThermoFisher, Cat#88816) were prewashed two times with wash buffer (150 mM NaCl, 1 mM EDTA, 0.05% NP40 and 20 mM Tris, pH 7.5), once with buffer A (100 mM NaOH, 50 mM NaCl) and twice with buffer B (100 mM NaCl). After sample incubation with beads for 1 hour at 4°C, rotating, beads were magnetized and washed with 0.5 mL wash buffer for four times. For mass spectrometry, samples were instead washed two times with wash buffer followed by two washes with 50 mM ammoniumbicarbonate. During the last wash, beads were transferred to clean tubes, supernatant was removed, and beads were processed according to their follow-up application.   AP beads were incubated with 1 μg trypsin (Thermo Fisher Scientific, Cat#90058) in 60 μL of 50 mM ammoniumbicarbonate, overnight at 37°C, rotating. Samples were then desalted using C18 Stage tips, dried by SpeedVac and stored at -80°C until further use.   Peptides were dissolved in 15 μL of 0.1% formic acid and loaded onto a reverse-phase trap column (75 μm × 2 cm, Acclaim PepMap100-C18, ThermoScientific). Peptides were separated using an EASY-Spray™ PepMap™ Neo UHPLC column (75 μm i.d. × 50 cm, 2 μm, 100 Å; ES75500PN, ThermoScientific) on a Neo Vanquish UHPLC system (ThermoScientific). Separation was done using a linear acetonitrile gradient (0–3.2% over 6.5 min, then to 31.2% over 103.5 min) at a 0.3 μL/min flow rate. Following electrospray ionization, peptides were analyzed on an Orbitrap Exploris 480 mass spectrometer in data-dependent mode, using one MS (m/z 350-1450) followed by MS/MS with a normalized AGC target of 300% in MS1 and 50% in MS2, an intensity threshold of 5.0e4 and a 45 sec exclusion window."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Each MS/MS spectra file was computationally split into three files based on the FAIMS compensation voltage -50, -57 and -64. The MS/MS data were searched against the Human proteome (UP000000589_10090, 2023_01_25) with MaxQuant software (version 2.1.4.0), with parameters set to unique and razor peptides for protein quantification, variable modifications of methionine oxidation and N-terminal acetylation, carbamidomethylation as a fixed modification and trypsin digestion. Data quality control and differential testing was performed using the Mass Spectrometry Downstream Analysis Pipeline (MS-DAP, version 1.0.3.1)30. Peptides present in ≥60% of samples per condition were used for differential testing by DEqMS after rollup to proteins. The Variance Stabilizing Normalization and mode between protein algorithms were used for normalization. Proteins detected in ≥60% of circ-PDE4B APs and ≤40% of Scrambled-APs showing an abundance difference of ≥30% were also considered true circ-PDE4B interactors and included in follow up analyses."],"omics_type":["Proteomics"],"labhead":["Benjamin Wolozin"],"instrument_platform":[""],"labhead_affiliation":["Department of Anatomy and Neurobiolog; Department of Pharmacology, Physiology and Biophysics; Department of Neurology, Boston University Chobanian and Avedisian School of Medicine, Boston, MA, 02118, USA"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["sophiejf@hotmail.com"],"publication":["42080242 Puri S, van der Spek SJF, Lin M, Wang Z, Porter J, Hu J, Hu L, Rondón-Ortiz AN, Knyshov A, Libera JL, Counts SE, Lahiri DK, Tcw J, Emili A, Zhang X, Wolozin B. circPDE4B downregulation triggers GEMIN5‑dependent translational stress response and autophagy to reduce MAPT pathology. Alzheimers Dement. 2026 22(5):e71436 10.1002/alz.71436"],"submitter_affiliation":["BU, Boston, USA"],"submitter_country":["United States"],"pubmed_abstract":["<h4>Introduction</h4>Circular RNAs (circRNAs) are emerging as key regulators of gene expression, synaptic plasticity, and neuronal function in Alzheimer's disease (AD). Here, we characterize the biological actions of circPDE4B, a highly expressed circRNA markedly reduced in AD.<h4>Methods</h4>circPDE4B knockdown in neuronal progenitor cells was combined with RNA sequencing to identify regulated pathways. circPDE4B affinity purification identified major protein and micro RNA (miRNA) interactors. Assays of translation and autophagy integrated circPDE4B actions.<h4>Results</h4>We found that circPDE4B knockdown inhibited translation through a mechanism mediated by its major interacting protein, gem-associated protein 5. circPDE4B knockdown also decreased mechanistic target of rapamycin and correspondingly enhanced autophagic flux. Consistent with these actions, circPDE4B knockdown strongly attenuated microtubule-associated protein tau pathology in a 3D human assembloid model of tauopathy.<h4>Discussion</h4>Collectively, our findings identify circPDE4B as a regulator of neuronal homeostasis that integrates translation, autophagy, and miRNA pathways, highlighting a potentially important role in the pathophysiology of AD."],"pubmed_title":["circPDE4B downregulation triggers GEMIN5‑dependent translational stress response and autophagy to reduce MAPT pathology."],"pubmed_authors":["Puri Sambhavi S, van der Spek Sophie J F SJF, Lin Mintao M, Wang Zihan Z, Porter Jacob J, Hu Junming J, Hu Liyuan L, Rondón-Ortiz Alejandro N AN, Knyshov Alexander A, Libera Jenna L JL, Counts Scott E SE, Lahiri Debomoy K DK, Tcw Julia J, Emili Andrew A, Zhang Xiaoling X, Wolozin Benjamin B"],"additional_accession":[]},"is_claimable":false,"name":"Alzheimer’s Disease-Associated circPDE4B Triggers Translation Stress Pathways","description":"In the intricate landscape of Alzheimer’s disease (AD) pathology, circular RNAs(circRNA) are emerging as influential players, orchestrating crucial aspects of gene expression, synaptic plasticity, and neuronal function. In this study, we characterize the biological role of circPDE4B, a highly abundant circRNA that is markedly downregulated in AD across brain regions. Unlike most circRNAs, circPDE4B is expressed at substantially higher levels than its linear PDE4B transcript, suggesting a distinctive regulatory significance. Functional analyses in neuronal precursor cells revealed that circPDE4B reduction triggers a translational stress response, indicating its critical role in maintaining protein synthesis homeostasis. Immunoprecipitation identified several RNA-binding proteins associated with circPDE4B, among which the translation factor Gemin5 emerged as a key mediator of its effects on translation. Loss of circPDE4B also reduced mTOR levels and subsequently enhanced autophagic flux. Notably, circPDE4B downregulation was sufficient to mitigate tau pathology in a 3D assembloid model of tauopathy. We also identified a subset of AD-associated miRNAs interacting with circPDE4B, implicating additional layers of post-transcriptional regulation. Collectively, these findings define circPDE4B as a multifunctional regulator of neuronal homeostasis that integrates translational control, autophagic activity, and miRNA-mediated pathways, illuminating its potential involvement in the stress response and pathophysiology of 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