{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD055267/PXD055267_community_annotated.sdrf.tsv"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD055267/DM_Levitz_prep2_mGlur8_arrestin_uphos_5h_B_C_000545.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD055267/DM_Levitz_prep1_mGlur8_arrestin_uphos_3h_A_C_000438.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD055267/DM_Levitz_prep1_mGlur8_arrestin_uphos_5h_B_C_000411.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD055267/DM_Levitz_prep2_mGlur8_arrestin_uphos_5h_A_C_000544.raw"],"Mzid":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD055267/3371_DM_Levitz_prep2_mGlur8_arrestin_uphos_5h_B_C_000545_psc.mzid.gz","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD055267/3365_DM_Levitz_prep1_mGlur8_arrestin_uphos_3h_A_C_000438_psc.mzid.gz","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD055267/3369_DM_Levitz_prep2_mGlur8_arrestin_uphos_5h_A_C_000544_psc.mzid.gz","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD055267/3367_DM_Levitz_prep1_mGlur8_arrestin_uphos_5h_B_C_000411_psc.mzid.gz"],"Mzxml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD055267/DM_Levitz_prep1_mGlur8_arrestin_uphos_5h_B_C_000411_psc.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD055267/DM_Levitz_prep2_mGlur8_arrestin_uphos_5h_A_C_000544_psc.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD055267/DM_Levitz_prep1_mGlur8_arrestin_uphos_3h_A_C_000438_psc.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD055267/DM_Levitz_prep2_mGlur8_arrestin_uphos_5h_B_C_000545_psc.mzXML"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["jtl2003@med.cornell.edu"],"submitter":["Marian Kalocsay"],"technology_type":["Data-dependent acquisition","Mass Spectrometry"],"software":["Not available"],"submitter_keywords":["Neuronal receptor","Phosphorylation","Gpcr","Metabotropic glutamate receptor 8"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD055267"],"sample_protocol":["Protein preparations were dissolved in SDS lysis buffer (10 mM (tris(2-carboxyethyl)phosphine) (TCEP), 2% SDS, 150 mM NaCl, 50 mM Tris, pH 8.5) and reduced cysteine residues were alkylated with iodoacetamide at a final concentration of 20 mM and incubation at room temperature in the dark for 25 minutes. Alkylation was quenched with 50 mM freshly prepared DTT. SDS was removed by SP3 protein cleanup 1 and proteins were digested with Lys-C protease (Wako, Catalog Number 129–02541) and trypsin (Promega Catalog Number V5113). Peptides were subjected to micro-phospho enrichment as described recently in Susa et al. 2024 2 and analyzed on an Orbitrap Ascend Mass spectrometer (Thermo Fisher Scientific) using 180 or 300 minute FAIMS runs (CVs -40V, -55V, -70V, -85V, cycle time 6s) at an MS1 resolution of 120,000 in the orbitrap. After HCD fragmentation (25% collision energy), MS2 scans were collected at 45,000 resolution in the orbitrap with a 1.6 m/z quadrupole isolation window.  References: 1. Hughes CS, Moggridge S, Müller T, Sorensen PH, Morin GB, Krijgsveld J. Single-pot, solid-phase-enhanced sample preparation for proteomics experiments. Nat Protoc. 2019 Jan;14(1):68-85. doi: 10.1038/s41596-018-0082-x. PMID: 30464214. 2. Susa KJ, Bradshaw GA, Eisert RJ, Schilling CM, Kalocsay M, Blacklow SC, Kruse AC. A spatiotemporal map of co-receptor signaling networks underlying B cell activation. Cell Rep. 2024 Jun 25;43(6):114332. doi: 10.1016/j.celrep.2024.114332. Epub 2024 Jun 7. PMID: 38850533; PMCID: PMC11256977."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Data were searched with COMET 3 using additional masses of +15.994914 Da for oxidized methionine modification and + 79.966330 Da for phospho-modification on S, T and Y residues, dynamically. Peptides were identified using MS2 spectra and a false discovery rate (FDR) < 1% and was achieved by applying a target-decoy database search strategy. Details of phospho-proteomic analysis are provided in 2. References: 2. Susa KJ, Bradshaw GA, Eisert RJ, Schilling CM, Kalocsay M, Blacklow SC, Kruse AC. A spatiotemporal map of co-receptor signaling networks underlying B cell activation. Cell Rep. 2024 Jun 25;43(6):114332. doi: 10.1016/j.celrep.2024.114332. Epub 2024 Jun 7. PMID: 38850533; PMCID: PMC11256977. 3. Eng JK, Hoopmann MR, Jahan TA, Egertson JD, Noble WS, MacCoss MJ. A deeper look into Comet--implementation and features. J Am Soc Mass Spectrom. 2015 Nov;26(11):1865-74. doi: 10.1007/s13361-015-1179-x. Epub 2015 Jun 27. PMID: 26115965; PMCID: PMC4607604."],"omics_type":["Proteomics"],"labhead":["Joshua Levitz"],"instrument_platform":[""],"labhead_affiliation":["Weill Cornell Medicine, Department of Biochemistry 1300 York Avenue, Box #63 Room A-108 New York, NY 10065"],"submission_type":["COMPLETE"],"species":["Homo Sapiens (human)"],"publication":["42722688 Marx DC, Gonzalez-Hernandez AJ, Lee J, Siepe D, Weber WF, Huynh K, Gallo PN, Sharghi Moshtaghin S, Arefin A, Broichhagen J, Kalocsay M, Eliezer D, Levitz J. Configurational diversity of metabotropic glutamate receptor complexes with beta-arrestins. Nat Commun. 2026 17(1):9651 10.1038/s41467-026-77555-4"],"submitter_mail":["mkalocsay@mdanderson.org"],"submitter_affiliation":["The University of Texas MD Anderson Cancer Center\nDepartment of Experimental Radiation Oncology"],"submitter_country":["United States"],"doi":["10.6019/PXD055267"],"pubmed_abstract":["Beta-arrestins (β-arrs) are cytosolic proteins which mediate G protein-coupled receptor (GPCR) desensitization, endocytosis, and signaling. Despite the widespread physiological roles of β-arr coupling, the molecular basis of GPCR/β-arr interaction has been studied primarily in monomeric family A GPCRs. Here we develop a single molecule pulldown (SiMPull) assay that reports on both relative GPCR:β-arr interaction strength and stoichiometry to uncover molecular diversity in β-arr coupling to the neuromodulatory metabotropic glutamate receptors (mGluRs), prototypical, dimeric family C GPCRs. We find that mGluRs couple to β-arrs with variable apparent strength and a 2:1 or 2:2 stoichiometry. Focusing on the mGluR8/β-arr1 interaction, we map the contributions of \"tail\" and \"core\" interactions with residues in the receptor C-terminal domain and intracellular loops, respectively. Combinatorial mutagenesis enables the identification of a landscape of β-arr complexes with homo- and hetero-dimeric mGluR8, including both \"cis\" and \"trans\" interactions. Finally, we use our SiMPull assay in conjunction with live cell imaging and transcriptomic analysis to reveal that mGluRs can form megacomplexes either by simultaneously binding β-arr1 and β-arr2 or β-arr and G proteins. Together, this study provides a comprehensive framework for mGluR/β-arr complex diversity, expanding the known range of GPCR/transducer coupling modes."],"pubmed_title":["Configurational diversity of metabotropic glutamate receptor complexes with beta-arrestins."],"pubmed_authors":["Marx Dagan C DC, Gonzalez-Hernandez Alberto J AJ, Lee Joon J, Siepe Dirk D, Weber Willem F WF, Huynh Kevin K, Gallo Pamela N PN, Sharghi Moshtaghin Sheida S, Arefin Anisul A, Broichhagen Johannes J, Kalocsay Marian M, Eliezer David D, Levitz Joshua J"],"additional_accession":[]},"is_claimable":false,"name":"Phosphorylation site mapping on purified mGluR8/arrestin complexes","description":"phosphorylation sites of purified mGluR8 with arrestin are mapped by mass 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