{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065058/mqpar_P000669.xml","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065058/mqpar_P000586.xml"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065058/S11015.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065058/S11016.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065058/S11018.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065058/S11628.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065058/S11629.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065058/S11017.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065058/S11630.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065058/S11631.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065058/S11633.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065058/S11632.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["junge@umn.edu"],"submitter":["Harald Junge"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Hela","Bioid","Hek293t","Fzd4","Lc-ms/ms"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD065058"],"sample_protocol":["The samples were digested with trypsin and acidified with TFA and desalted using Bravo AssayMap and loaded on to the MS"],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["MaxQuant 1.5.5.1 was for performing search and data was serached against the human database with Trypsin digestion and oxidation(M) and Acetyl (Protein N-term) as variable modifications"],"omics_type":["Proteomics"],"labhead":["Harald Junge"],"instrument_platform":[""],"labhead_affiliation":["Harald Junge, Ph.D. Mary and Marian Robinson Chair in Macular Degeneration Associate Professor and Research Director Department of Ophthalmology and Visual Neuroscience University of Minnesota Room 310A LRB, 2001 6th St SE Minneapolis, MN 55455 office: (612) 624-6017 web: https://med.umn.edu/ophthalmology/research/junge-lab"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["junge@umn.edu"],"publication":["40777252 Jo HN, Kiffmeyer E, Zhang C, Zhang L, Odame E, Dinh QC, Levey J, Howe M, Roux KJ, Fischer KD, Chen Z, Junge HJ. The Calcium Pump ATP2B1/PMCA1 Regulates CNS Vascular Development by Facilitating Norrin- and WNT7A/B-induced Frizzled4 signaling. bioRxiv. 2025:2025.07.17.664964 10.1101/2025.07.17.664964"],"submitter_affiliation":["University of Minnesota"],"submitter_country":["United States"],"pubmed_abstract":["Frizzled4 (FZD4) is a receptor for Norrin and WNT7A/B ligands, is expressed in endothelial cells (ECs), is required for blood-CNS-barrier function as well as CNS angiogenesis, and transduces β-catenin-dependent signaling. Despite its fundamental importance in neurovascular biology, including as drug target, the molecular mechanisms governing FZD4 regulation remain poorly understood. Here, we employed proximity biotinylation to identify proteins that regulate FZD4. We identified ATPase Plasma Membrane Ca<sup>2+</sup> Transporting 1 (ATP2B1, also known as PMCA1) as a FZD4 proximity interactor. Functional analyses revealed that ATP2B1 depletion increased EC Ca<sup>2+</sup> and significantly attenuated Norrin/Frizzled4 signaling. These effects of <i>Atp2b1</i> deficiency were recapitulated by ionomycin-mediated elevation of intracellular Ca<sup>2+</sup> and suppressed by inhibition of calcineurin/NFAT signaling. Endothelial-specific <i>Atp2b1</i> deletion caused retinal vascular defects consistent with compromised Norrin/Frizzled4 signaling. In the developing brain, WNT7A/B pathway LOF phenotypes in <i>Gpr124</i> KO mice were exacerbated by additional deletion of <i>Atp2b1</i> in ECs. This study identifies ATP2B1 as a novel regulator of Norrin- and WNT7A/B-induced FZD4 signaling and suggests that in pathological contexts with elevated EC Ca<sup>2+</sup>-levels, EC function may be modulated by suppression of β-catenin-dependent signaling. In addition, this mechanism may be relevant in the context of pharmacological approaches that transiently open the barrier for drug delivery."],"pubmed_title":["The Calcium Pump ATP2B1/PMCA1 Regulates CNS Vascular Development by Facilitating Norrin- and WNT7A/B-induced Frizzled4 signaling."],"pubmed_authors":["Jo Ha-Neul HN, Kiffmeyer Elizabeth E, Zhang Chi C, Zhang Lingling L, Odame Emmanuel E, Dinh Quynh Chau QC, Levey Jacklyn J, Howe Miranda M, Roux Kyle J KJ, Fischer Klaus-Dieter KD, Chen Zhe Z, Junge Harald J HJ"],"additional_accession":[]},"is_claimable":false,"name":"Frizzled4 proximity interactors","description":"Frizzled4 (FZD4) is a pivotal receptor for Norrin and Wnt7a/b that mediates CNS angiogenesis, blood-brain barrier function and blood-retina barrier function. FZD4 is a target for pharmacological interventions in retinal and neurological disease. In order to understand mechanisms of regulation of Frizzled4 activity, two proximity biotinylation screens were performed, one in HEK293T cells and one in HeLa cells. For the screen in HEK293T cells, cells were transiently transfected. 24 hours later, cells were stimulated with 50 µM biotin for an additional 24 hours. Samples were processed and subjected to LC-MS/MSas described (PMID: 29516480). Samples S480 and S483 were biological replicates of cells co-transfected with V5-FZD4-BioID, HA-LRP5, and HA-TSPAN12 to reconstitute the norrin receptor complex. Samples S481 and S484 were biological replicates of cells co-transfected with V5-FZD4-BioID, HA-LRP5, and HA-TSPAN12 that were stimulated with flag-AP-Norrin conditioned media during the 24 hour biotin incubation period to induce norrin/frizzled4 signaling. Sample S479 and S482 were biological replicates of cells co-transfected with GFP-BioID, HA-LRP5, and HA-TSPAN12 as negative control. For the screen in HeLa cells, cells were transfected and biotinylated as described above. Sample S454 was transfected with V5-FZD4 (without BioID fusion, as a negative control). Sample S455 was transfected with GFP-BioID as another negative control. Sample S456 and S457 were transfected with V5-FZD4-BioID, of which only S457 was stimulated with flag-AP-Norrin conditioned medium during the biotin incubation period in order to induce FZD4 endocytosis. Multiple known and novel proximity interactors were identified in HEK293T and HeLa cells with high specificity. Comparisons of cells stimulated with norrin vs. vehicle indicate that proximity interactors of FZD4 were largely similar in cells with and without norrin stimulation in an overexpression 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