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Caveolin-2 has a lower tendency to associate with high molecular weight oligomers than caveolin-1, facilitating the study of its structural modulation upon association with other proteins or lipids. In this paper, we have successfully expressed and purified recombinant human caveolin-2 using E. coli. The structural changes of caveolin-2 upon interaction with a lipid bilayer of liposomes were characterized using bioinformatic prediction models, circular dichroism, differential scanning calorimetry, and fluorescence techniques. Our data support that caveolin-2 binds and alters cholesterol-rich domains in the membranes through a CARC domain, a type of cholesterol-interacting domain in its sequence. The far UV-CD spectra support that the purified protein keeps its folding properties but undergoes a change in its secondary structure in the presence of lipids that correlates with the acquisition of a more stable conformation, as shown by differential scanning calorimetry experiments. Fluorescence experiments using egg yolk lecithin large unilamellar vesicles loaded with 1,6-diphenylhexatriene confirmed that caveolin-2 adsorbs to the membrane but only penetrates the core of the phospholipid bilayer if vesicles are supplemented with 30% of cholesterol. Our study sheds light on the caveolin-2 interaction with lipids. In addition, we propose that purified recombinant caveolin-2 can provide a new tool to study protein\u2013lipid interactions within caveolae.<\/jats:p>","DOI":"10.3390\/ijms232315203","type":"journal-article","created":{"date-parts":[[2022,12,5]],"date-time":"2022-12-05T01:42:21Z","timestamp":1670204541000},"page":"15203","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Biochemical and Biophysical Characterization of the Caveolin-2 Interaction with Membranes and Analysis of the Protein Structural Alteration by the Presence of Cholesterol"],"prefix":"10.3390","volume":"23","author":[{"given":"Berta","family":"Gorospe","sequence":"first","affiliation":[{"name":"LAQV-REQUIMTE, Departamento de Qu\u00edmica, Faculdade de Ci\u00eancias e Tecnologia, Universidade Nova de Lisboa, 2829-516 Lisbon, Portugal"}]},{"given":"Jos\u00e9 J. G.","family":"Moura","sequence":"additional","affiliation":[{"name":"LAQV-REQUIMTE, Departamento de Qu\u00edmica, Faculdade de Ci\u00eancias e Tecnologia, Universidade Nova de Lisboa, 2829-516 Lisbon, Portugal"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3673-7007","authenticated-orcid":false,"given":"Carlos","family":"Gutierrez-Merino","sequence":"additional","affiliation":[{"name":"Research Institute of Molecular Pathology Biomarkers, University of Extremadura, 06006 Badajoz, Spain"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9602-4848","authenticated-orcid":false,"given":"Alejandro K.","family":"Samhan-Arias","sequence":"additional","affiliation":[{"name":"LAQV-REQUIMTE, Departamento de Qu\u00edmica, Faculdade de Ci\u00eancias e Tecnologia, Universidade Nova de Lisboa, 2829-516 Lisbon, Portugal"},{"name":"Departamento de Bioqu\u00edmica, Universidad Aut\u00f3noma de Madrid (UAM), C\/Arturo Duperier 4, 28029 Madrid, Spain"},{"name":"Instituto de Investigaciones Biom\u00e9dicas \u2018Alberto Sols\u2019 (CSIC-UAM), C\/Arturo Duperier 4, 28029 Madrid, Spain"}]}],"member":"1968","published-online":{"date-parts":[[2022,12,2]]},"reference":[{"key":"ref_1","first-page":"1424","article-title":"Fine Structure of Blood Capillaries","volume":"24","author":"Palade","year":"1953","journal-title":"J. Appl. Phys."},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Stillwell, W. (2013). Chapter 11-Long-Range Membrane Properties. An Introduction to Biological Membranes, Elsevier.","DOI":"10.1016\/B978-0-444-52153-8.00011-8"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1242\/jcs.02853","article-title":"Biogenesis of Caveolae: A Structural Model for Caveolin-Induced Domain Formation","volume":"119","author":"Parton","year":"2006","journal-title":"J. Cell Sci."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"jcs241562","DOI":"10.1242\/jcs.241562","article-title":"Non-Caveolar Caveolins-Duties Outside the Caves","volume":"133","author":"Pol","year":"2020","journal-title":"J. Cell Sci."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1016\/j.ceb.2020.02.001","article-title":"Caveolae: Formation, Dynamics, and Function","volume":"65","author":"Parton","year":"2020","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_6","first-page":"15160","article-title":"Expression of Caveolin-3 in Skeletal, Cardiac, and Smooth Muscle Cells","volume":"271","author":"Song","year":"1996","journal-title":"Caveolin-3 Is a Component of the Sarcolemma and Co-Fractionates with Dystrophin and Dystrophin-Associated Glycoproteins. J. Biol. Chem."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"809259","DOI":"10.1155\/2011\/809259","article-title":"Novel Insights into the Role of Caveolin-2 in Cell- and Tissue-Specific Signaling and Function","volume":"2011","author":"Sowa","year":"2011","journal-title":"Biochem. Res. Int."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1186\/gb-2004-5-3-214","article-title":"The Caveolin Proteins","volume":"5","author":"Williams","year":"2004","journal-title":"Genome Biol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1073\/pnas.93.1.131","article-title":"Identification, Sequence, and Expression of Caveolin-2 Defines a Caveolin Gene Family","volume":"93","author":"Scherer","year":"1996","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.devcel.2012.06.012","article-title":"Structure-Based Reassessment of the Caveolin Signaling Model: Do Caveolae Regulate Signaling through Caveolin-Protein Interactions?","volume":"23","author":"Collins","year":"2012","journal-title":"Dev. Cell"},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Byrne, D.P., Dart, C., and Rigden, D.J. (2012). Evaluating Caveolin Interactions: Do Proteins Interact with the Caveolin Scaffolding Domain through a Widespread Aromatic Residue-Rich Motif?. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0044879"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"29182","DOI":"10.1074\/jbc.271.46.29182","article-title":"Src Tyrosine Kinases, Galpha Subunits, and H-Ras Share a Common Membrane-Anchored Scaffolding Protein, Caveolin. Caveolin Binding Negatively Regulates the Auto-Activation of Src Tyrosine Kinases","volume":"271","author":"Li","year":"1996","journal-title":"J. Biol. Chem."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1146\/annurev.pharmtox.48.121506.124841","article-title":"Caveolae as Organizers of Pharmacologically Relevant Signal Transduction Molecules","volume":"48","author":"Patel","year":"2008","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1124\/pr.54.3.431","article-title":"Caveolae: From Cell Biology to Animal Physiology","volume":"54","author":"Razani","year":"2002","journal-title":"Pharmacol. Rev."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"2588","DOI":"10.1016\/j.bbamem.2014.06.018","article-title":"Interactions of Caveolin-1 Scaffolding and Intramembrane Regions Containing a CRAC Motif with Cholesterol in Lipid Bilayers","volume":"1838","author":"Yang","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"31","DOI":"10.3389\/fphys.2013.00031","article-title":"How Cholesterol Interacts with Membrane Proteins: An Exploration of Cholesterol-Binding Sites Including CRAC, CARC, and Tilted Domains","volume":"4","author":"Fantini","year":"2013","journal-title":"Front. Physiol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1038\/srep00069","article-title":"Disclosure of Cholesterol Recognition Motifs in Transmembrane Domains of the Human Nicotinic Acetylcholine Receptor","volume":"1","author":"Baier","year":"2011","journal-title":"Sci. Rep."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"888","DOI":"10.1111\/j.1582-4934.2010.01079.x","article-title":"A Novel Domain of Caveolin-2 That Controls Nuclear Targeting: Regulation of Insulin-Specific ERK Activation and Nuclear Translocation by Caveolin-2","volume":"15","author":"Kwon","year":"2011","journal-title":"J. Cell. Mol. Med."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"4457","DOI":"10.1242\/jcs.00130","article-title":"The Scaffolding Domain of Caveolin 2 Is Responsible for Its Golgi Localization in Caco-2 Cells","volume":"115","author":"Breuza","year":"2002","journal-title":"J. Cell Sci."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1079","DOI":"10.1083\/jcb.152.5.1079","article-title":"Caveolin-2 Is Targeted to Lipid Droplets, a New \u201cMembrane Domain\u201d in the Cell","volume":"152","author":"Fujimoto","year":"2001","journal-title":"J. Cell Biol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"1537","DOI":"10.1016\/j.bbamcr.2017.06.016","article-title":"Functional Interaction of the Two-Pore Domain Potassium Channel TASK-1 and Caveolin-3","volume":"1864","author":"Kang","year":"2017","journal-title":"Biochim. Biophys. Acta Mol. Cell Res."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"38048","DOI":"10.1074\/jbc.M005321200","article-title":"Caveolin-3 Directly Interacts with the C-Terminal Tail of Beta -Dystroglycan. Identification of a Central WW-like Domain within Caveolin Family Members","volume":"275","author":"Sotgia","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"28187","DOI":"10.1074\/jbc.272.45.28187","article-title":"Interaction of Neuronal Nitric-Oxide Synthase with Caveolin-3 in Skeletal Muscle. Identification of a Novel Caveolin Scaffolding\/Inhibitory Domain","volume":"272","author":"Venema","year":"1997","journal-title":"J. Biol. Chem."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"H392","DOI":"10.1152\/ajpheart.01039.2007","article-title":"Caveolin-1 and Caveolin-3 Form Heterooligomeric Complexes in Atrial Cardiac Myocytes That Are Required for Doxorubicin-Induced Apoptosis","volume":"294","author":"Volonte","year":"2008","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1530","DOI":"10.3389\/fimmu.2017.01530","article-title":"Caveolin-1 and Caveolin-2 Can Be Antagonistic Partners in Inflammation and Beyond","volume":"8","year":"2017","journal-title":"Front. Immunol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"15693","DOI":"10.1074\/jbc.270.26.15693","article-title":"Evidence for a Regulated Interaction between Heterotrimeric G Proteins and Caveolin","volume":"270","author":"Li","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/j.redox.2017.11.021","article-title":"Cytochrome B5 Reductase Is the Component from Neuronal Synaptic Plasma Membrane Vesicles That Generates Superoxide Anion upon Stimulation by Cytochrome c","volume":"15","author":"Fortalezas","year":"2018","journal-title":"Redox Biol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1016\/j.freeradbiomed.2014.04.033","article-title":"Purified NADH-Cytochrome B5 Reductase Is a Novel Superoxide Anion Source Inhibited by Apocynin: Sensitivity to Nitric Oxide and Peroxynitrite","volume":"73","year":"2014","journal-title":"Free Radic. Biol. Med."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"2934","DOI":"10.1016\/j.jprot.2011.12.007","article-title":"Stimulation and Clustering of Cytochrome B5 Reductase in Caveolin-Rich Lipid Microdomains Is an Early Event in Oxidative Stress-Mediated Apoptosis of Cerebellar Granule Neurons","volume":"75","author":"Yanamala","year":"2012","journal-title":"J. Proteom."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1016\/j.mcn.2008.08.013","article-title":"Clustering of Plasma Membrane-Bound Cytochrome B5 Reductase within \u201clipid Raft\u201d Microdomains of the Neuronal Plasma Membrane","volume":"40","year":"2009","journal-title":"Mol. Cell. Neurosci."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"148134","DOI":"10.1016\/j.bbabio.2019.148134","article-title":"Human Erythrocytes Exposure to Juglone Leads to an Increase of Superoxide Anion Production Associated with Cytochrome B5 Reductase Uncoupling","volume":"1861","author":"Nogueira","year":"2020","journal-title":"Biochim. Biophys. Acta (BBA)-Bioenerg."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"25708","DOI":"10.1074\/jbc.274.36.25708","article-title":"Caveolin-2 Localizes to the Golgi Complex but Redistributes to Plasma Membrane, Caveolae, and Rafts When Co-Expressed with Caveolin-1","volume":"274","author":"Mora","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1071","DOI":"10.1083\/jcb.152.5.1071","article-title":"Accumulation of Caveolin in the Endoplasmic Reticulum Redirects the Protein to Lipid Storage Droplets","volume":"152","author":"Ostermeyer","year":"2001","journal-title":"J. Cell Biol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"3888","DOI":"10.1038\/sj.onc.1206625","article-title":"Peroxisome Proliferator-Activated Receptor-Gamma Upregulates Caveolin-1 and Caveolin-2 Expression in Human Carcinoma Cells","volume":"22","author":"Burgermeister","year":"2003","journal-title":"Oncogene"},{"key":"ref_35","first-page":"1549","article-title":"Identification of PY19-Caveolin-2 as a Positive Regulator of Insulin-Stimulated Actin Cytoskeleton-Dependent Mitogenesis","volume":"13","author":"Kwon","year":"2009","journal-title":"J. Cell. Mol. Med."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1016\/S0014-5793(98)00945-4","article-title":"Mutational Analysis of Caveolin-Induced Vesicle Formation. Expression of Caveolin-1 Recruits Caveolin-2 to Caveolae Membranes","volume":"434","author":"Li","year":"1998","journal-title":"FEBS Lett."},{"key":"ref_37","first-page":"29337","article-title":"Cell-Type and Tissue-Specific Expression of Caveolin-2","volume":"272","author":"Scherer","year":"1997","journal-title":"Caveolins 1 and 2 Co-Localize and Form a Stable Hetero-Oligomeric Complex in Vivo. J. Biol. Chem."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"4398","DOI":"10.1074\/jbc.272.7.4398","article-title":"Mutational Analysis of the Properties of Caveolin-1. A Novel Role for the C-Terminal Domain in Mediating Homo-Typic Caveolin-Caveolin Interactions","volume":"272","author":"Song","year":"1997","journal-title":"J. Biol. Chem."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"9407","DOI":"10.1073\/pnas.92.20.9407","article-title":"Oligomeric Structure of Caveolin: Implications for Caveolae Membrane Organization","volume":"92","author":"Sargiacomo","year":"1995","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1007\/s00249-009-0548-4","article-title":"Structural and Dynamic Properties of Juxta-Membrane Segments of Caveolin-1 and Caveolin-2 at the Membrane Interface","volume":"39","author":"Gallay","year":"2010","journal-title":"Eur. Biophys. J."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"W329","DOI":"10.1093\/nar\/gky384","article-title":"IUPred2A: Context-Dependent Prediction of Protein Disorder as a Function of Redox State and Protein Binding","volume":"46","author":"Erdos","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"2745","DOI":"10.1093\/bioinformatics\/btp518","article-title":"ANCHOR: Web Server for Predicting Protein Binding Regions in Disordered Proteins","volume":"25","author":"Simon","year":"2009","journal-title":"Bioinformatics"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"4859","DOI":"10.1039\/C5CS00084J","article-title":"Circular Dichroism Spectroscopy of Membrane Proteins","volume":"45","author":"Miles","year":"2016","journal-title":"Chem. Soc. Rev."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1111\/j.1747-0285.2009.00847.x","article-title":"Circular Dichroism Techniques: Biomolecular and Nanostructural Analyses- a Review","volume":"74","author":"Ranjbar","year":"2009","journal-title":"Chem. Biol. Drug Des."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/S0014-5793(96)01279-3","article-title":"Efforts toward Deriving the CD Spectrum of a 3(10) Helix in Aqueous Medium","volume":"399","author":"Andersen","year":"1996","journal-title":"FEBS Lett."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1016\/j.bpj.2011.06.048","article-title":"Aggregation of Model Membrane Proteins, Modulated by Hydrophobic Mismatch, Membrane Curvature, and Protein Class","volume":"101","author":"Parton","year":"2011","journal-title":"Biophys. J."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"819","DOI":"10.1146\/annurev.bi.47.070178.004131","article-title":"Fluorescence Energy Transfer as a Spectroscopic Ruler","volume":"47","author":"Stryer","year":"1978","journal-title":"Annu. Rev. Biochem."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"33371","DOI":"10.1074\/jbc.M110.153569","article-title":"The Role of Proline in the Membrane Re-Entrant Helix of Caveolin-1","volume":"285","author":"Aoki","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1158","DOI":"10.1016\/j.bbamem.2011.12.033","article-title":"The Transmembrane Domain of Caveolin-1 Exhibits a Helix-Break-Helix Structure","volume":"1818","author":"Lee","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"1383","DOI":"10.1016\/j.bbrc.2005.10.099","article-title":"Structural Insights into the Function of Human Caveolin 1","volume":"338","author":"Spisni","year":"2005","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1021\/bi201356v","article-title":"Structural Characterization of the Caveolin Scaffolding Domain in Association with Cholesterol-Rich Membranes","volume":"51","author":"Hoop","year":"2012","journal-title":"Biochemistry"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"21605","DOI":"10.1074\/jbc.M002558200","article-title":"A Molecular Dissection of Caveolin-1 Membrane Attachment and Oligomerization. Two Separate Regions of the Caveolin-1 C-Terminal Domain Mediate Membrane Binding and Oligomer\/Oligomer Interactions in Vivo","volume":"275","author":"Schlegel","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_53","unstructured":"Lakowicz, J.R. (2010). Principles of Fluorescence Spectroscopy, Springer."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"3654","DOI":"10.1073\/pnas.0809959106","article-title":"Effect of Cholesterol on the Structure of a Phospholipid Bilayer","volume":"106","author":"Smit","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_55","doi-asserted-by":"crossref","unstructured":"Aguilar, L.F., Pino, J.A., Soto-Arriaza, M.A., Cuevas, F.J., S\u00e1nchez, S., and Sotomayor, C.P. (2012). Differential Dynamic and Structural Behavior of Lipid-Cholesterol Domains in Model Membranes. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0040254"},{"key":"ref_56","first-page":"91","article-title":"Lipid Antioxidants: Free Radical Scavenging versus Regulation of Enzymatic Lipid Peroxidation","volume":"48","author":"Tyurina","year":"2011","journal-title":"J. Clin. Biochem. Nutr."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"1189","DOI":"10.1093\/bioinformatics\/btp033","article-title":"Jalview Version 2\u2014A Multiple Sequence Alignment Editor and Analysis Workbench","volume":"25","author":"Waterhouse","year":"2009","journal-title":"Bioinformatics"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"10881","DOI":"10.1093\/nar\/16.22.10881","article-title":"Multiple Sequence Alignment with Hierarchical Clustering","volume":"16","author":"Corpet","year":"1988","journal-title":"Nucleic Acids Res."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"2624","DOI":"10.1002\/pro.256","article-title":"MPEx: A Tool for Exploring Membrane Proteins","volume":"18","author":"Snider","year":"2009","journal-title":"Protein Sci."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/23\/23\/15203\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T01:33:00Z","timestamp":1760146380000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/23\/23\/15203"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,12,2]]},"references-count":59,"journal-issue":{"issue":"23","published-online":{"date-parts":[[2022,12]]}},"alternative-id":["ijms232315203"],"URL":"https:\/\/doi.org\/10.3390\/ijms232315203","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,12,2]]}}}