{"id":365809,"date":"2026-03-26T07:32:10","date_gmt":"2026-03-26T07:32:10","guid":{"rendered":"https:\/\/www.newsbeep.com\/ie\/365809\/"},"modified":"2026-03-26T07:32:10","modified_gmt":"2026-03-26T07:32:10","slug":"parallel-crispr-screens-reveal-pathways-controlling-the-cell-surface-levels-of-the-attractant-receptor-fpr1","status":"publish","type":"post","link":"https:\/\/www.newsbeep.com\/ie\/365809\/","title":{"rendered":"Parallel CRISPR screens reveal pathways controlling the cell surface levels of the attractant receptor FPR1"},"content":{"rendered":"

Peiseler, M. & Kubes, P. More friend than foe: the emerging role of neutrophils in tissue repair. J. Clin. Invest. 129, 2629\u20132639 (2019).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Herrero-Cervera, A., Soehnlein, O. & Kenne, E. Neutrophils in chronic inflammatory diseases. Cell. Mol. Immunol. 19, 177\u2013191 (2022).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Metzemaekers, M., Gouwy, M. & Proost, P. Neutrophil chemoattractant receptors in health and disease: double-edged swords. Cell. Mol. Immunol. 17, 433\u2013450 (2020).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Dahlgren, C. et al. Neutrophil signaling that challenges dogmata of G protein-coupled receptor regulated functions. ACS Pharmacol. Transl. Sci. 3, 203\u2013220 (2020).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Dahlgren, C. et al. G protein coupled pattern receptors expressed in neutrophils: recognition, activation\/modulation, signaling and receptor regulated functions. Immunol. Rev. 314, 69\u201392 (2023).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Dorward, D. A. et al. The role of formylated peptides and formyl peptide receptor 1 in governing neutrophil function during acute inflammation. Am. J. Pathol. 185, 1172\u20131184 (2015).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

He, H.-Q. & Ye, R. D. The formyl peptide receptors: diversity of ligands and mechanism for recognition. Mol. J. Synth. Chem. Nat. Prod. Chem. 22, 455 (2017).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Honda, M. et al. Intravital imaging of neutrophil recruitment reveals the efficacy of FPR1 blockade in hepatic ischemia-reperfusion injury. J. Immunol. 198, 1718\u20131728 (2017).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Lind, S., Dahlgren, C., Holmdahl, R., Olofsson, P. & Forsman, H. Functional selective FPR1 signaling in favor of an activation of the neutrophil superoxide generating NOX2 complex. J. Leukoc. Biol. 109, 1105\u20131120 (2021).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Li, Y. et al. Targeting formyl peptide receptor 1 reduces brain inflammation and neurodegeneration. Science 390, eadq1177 (2025).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Wang, J., Chen, M., Li, S. & Ye, R. D. Targeted delivery of a ligand\u2013drug conjugate via formyl peptide receptor 1 through cholesterol-dependent endocytosis. Mol. Pharm. 16, 2636\u20132647 (2019).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Pierce, K. L., Premont, R. T. & Lefkowitz, R. J. Seven-transmembrane receptors. Nat. Rev. Mol. Cell Biol. 3, 639\u2013650 (2002).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Maaty, W. S. et al. Identification of C-terminal phosphorylation sites of N-formyl peptide receptor-1 (FPR1) in human blood neutrophils. J. Biol. Chem. 288, 27042\u201327058 (2013).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Prossnitz, E. R., Kim, C. M., Benovic, J. L. & Ye, R. D. Phosphorylation of the N-formyl peptide receptor carboxyl terminus by the G protein-coupled receptor kinase, GRK2. J. Biol. Chem. 270, 1130\u20131137 (1995).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Liu, X. et al. Bidirectional regulation of neutrophil migration by mitogen-activated protein kinases. Nat. Immunol. 13, 457\u2013464 (2012).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Subramanian, B. C., Moissoglu, K. & Parent, C. A. The LTB4\u2013BLT1 axis regulates the polarized trafficking of chemoattractant GPCRs during neutrophil chemotaxis. J. Cell Sci. 131, jcs217422 (2018).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Potter, R. M., Maestas, D. C., Cimino, D. F. & Prossnitz, E. R. Regulation of N-formyl peptide receptor signaling and trafficking by individual carboxyl-terminal serine and threonine residues. J. Immunol. 176, 5418\u20135425 (2006).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Gilbert, T. L., Bennett, T. A., Maestas, D. C., Cimino, D. F. & Prossnitz, E. R. Internalization of the human N -formyl peptide and C5a chemoattractant receptors occurs via clathrin-independent mechanisms. Biochemistry 40, 3467\u20133475 (2001).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Nakai, A. et al. The COMMD3\/8 complex determines GRK6 specificity for chemoattractant receptors. J. Exp. Med. 216, 1630\u20131647 (2019).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Vines, C. M. et al. N-formyl peptide receptors internalize but do not recycle in the absence of arrestins. J. Biol. Chem. 278, 41581\u201341584 (2003).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Wang, J. & Ye, R. D. Agonist concentration\u2013dependent changes in FPR1 conformation lead to biased signaling for selective activation of phagocyte functions. Proc. Natl. Acad. Sci. 119, e2201249119 (2022).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Winther, M., Dahlgren, C. & Forsman, H. Formyl peptide receptors in mice and men: similarities and differences in recognition of conventional ligands and modulating lipopeptides. Basic Clin. Pharmacol. Toxicol. 122, 191\u2013198 (2018).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Mayer, D. et al. Distinct G protein-coupled receptor phosphorylation motifs modulate arrestin affinity and activation and global conformation. Nat. Commun. 10, 1261 (2019).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Rinc\u00f3n, E., Rocha-Gregg, B. L. & Collins, S. R. A map of gene expression in neutrophil-like cell lines. BMC Genomics 19, 573 (2018).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Sengel\u00f8v, H., Boulay, F., Kjeldsen, L. & Borregaard, N. Subcellular localization and translocation of the receptor for N -formylmethionyl-leucyl-phenylalanine in human neutrophils. Biochem. J. 299, 473\u2013479 (1994).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Bock, C. et al. High-content CRISPR screening. Nat. Rev. Methods Prim. 2, 8 (2022).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Evers, B. et al. CRISPR knockout screening outperforms shRNA and CRISPRi in identifying essential genes. Nat. Biotechnol. 34, 631\u2013633 (2016).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Morgens, D. W. et al. Genome-scale measurement of off-target activity using Cas9 toxicity in high-throughput screens. Nat. Commun. 8, 15178 (2017).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Novy, B. et al. An engineered trafficking biosensor reveals a role for DNAJC13 in DOR downregulation. BMC Genomics 19, 573 (2024).<\/p>\n

Haney, M. S. et al. Identification of phagocytosis regulators using magnetic genome-wide CRISPR screens. Nat. Genet. 50, 1716\u20131727 (2018).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Belliveau, N. M. et al. Whole-genome screens reveal regulators of differentiation state and context-dependent migration in human neutrophils. Nat. Commun. 14, 5770 (2023).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Tiedemann, R. E. et al. Kinome-wide RNAi studies in human multiple myeloma identify vulnerable kinase targets, including a lymphoid-restricted kinase, GRK6. Blood 115, 1594\u20131604 (2010).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Willets, J. M., Challiss, R. A. J. & Nahorski, S. R. Non-visual GRKs: are we seeing the whole picture? Trends Pharmacol. Sci. 24, 626\u2013633 (2003).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Okawa, T. et al. Design, synthesis, and evaluation of the highly selective and potent G-protein-coupled receptor kinase 2 (GRK2) inhibitor for the potential treatment of heart failure. J. Med. Chem. 60, 6942\u20136990 (2017).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Dahlgren, C., Gabl, M., Holdfeldt, A., Winther, M. & Forsman, H. Basic characteristics of the neutrophil receptors that recognize formylated peptides, a danger-associated molecular pattern generated by bacteria and mitochondria. Biochem. Pharmacol. 114, 22\u201339 (2016).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Bennett, T. A., Maestas, D. C. & Prossnitz, E. R. Arrestin binding to the g protein-coupled N-formyl peptide receptor is regulated by the conserved \u201cDRY\u201d sequence. J. Biol. Chem. 275, 24590\u201324594 (2000).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Morgens, D. W., Deans, R. M., Li, A. & Bassik, M. C. Systematic comparison of CRISPR\/Cas9 and RNAi screens for essential genes. Nat. Biotechnol. 34, 634\u2013636 (2016).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Guna, A., Volkmar, N., Christianson, J. C. & Hegde, R. S. The ER membrane protein complex is a transmembrane domain insertase. Science 359, 470\u2013473 (2018).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Shurtleff, M. J. et al. The ER membrane protein complex interacts cotranslationally to enable biogenesis of multipass membrane proteins. eLife 7, e37018 (2018).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Subramanian, A. et al. Gene set enrichment analysis: a knowledge-based approach for interpreting genome-wide expression profiles. Proc. Natl. Acad. Sci. 102, 15545\u201315550 (2005).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Aliyu, M. et al. Interleukin-6 cytokine: an overview of the immune regulation, immune dysregulation, and therapeutic approach. Int. Immunopharmacol. 111, 109130 (2022).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Park, S.-J. et al. IL-6 regulates in vivo dendritic cell differentiation through STAT3 activation. J. Immunol. 173, 3844\u20133854 (2004).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Yang, J. et al. Sequential genome-wide CRISPR-Cas9 screens identify genes regulating cell-surface expression of tetraspanins. Cell Rep. 42, 112065 (2023).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Lachance, V. et al. Ubiquitination and activation of a Rab GTPase promoted by a \u03b22-adrenergic receptor\/HACE1 complex. J. Cell Sci. 126, 5669\u20135682 (2013).<\/p>\n

Bai, S. et al. Exocyst controls exosome biogenesis via Rab11a. Mol. Ther. Nucleic Acids 27, 535\u2013546 (2022).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Shirakawa, R. & Horiuchi, H. Ral GTPases: crucial mediators of exocytosis and tumourigenesis. J. Biochem. 157, 285\u2013299 (2015).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Kawato, M. et al. Regulation of platelet dense granule secretion by the Ral GTPase-exocyst pathway. J. Biol. Chem. 283, 166\u2013174 (2008).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Laulumaa, S. & Varjosalo, M. Commander complex\u2014a multifaceted operator in intracellular signaling and cargo. Cells 10, 3447 (2021).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Gershlick, D. C. & Lucas, M. Endosomal trafficking: retromer and retriever are relatives in recycling. Curr. Biol. 27, R1233\u2013R1236 (2017).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Liu, D., Tsarouhas, V. & Samakovlis, C. WASH activation controls endosomal recycling and EGFR and Hippo signaling during tumor-suppressive cell competition. Nat. Commun. 13, 6243 (2022).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Xu, J. et al. Divergent signals and cytoskeletal assemblies regulate self-organizing polarity in neutrophils. Cell 114, 201\u2013214 (2003).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Hind, L. E., Vincent, W. J. B. & Huttenlocher, A. Leading from the back: the role of the uropod in neutrophil polarization and migration. Dev. Cell 38, 161\u2013169 (2016).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Kumar, A., Kremer, K. N., Dominguez, D., Tadi, M. & Hedin, K. E. G\u03b113 and Rho mediate endosomal trafficking of CXCR4 into Rab11+ vesicles upon stromal cell-derived factor-1 stimulation. J. Immunol. 186, 951\u2013958 (2011).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Abouelezz, A. & Almeida-Souza, L. The mammalian endocytic cytoskeleton. Eur. J. Cell Biol. 101, 151222 (2022).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Chakrabarti, R., Lee, M. & Higgs, H. N. Multiple roles for actin in secretory and endocytic pathways. Curr. Biol. 31, R603\u2013R618 (2021).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Soykan, T. et al. Synaptic vesicle endocytosis occurs on multiple timescales and is mediated by formin-dependent actin assembly. Neuron 93, 854\u2013866.e4 (2017).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Nishimura, Y. et al. The formin inhibitor SMIFH2 inhibits members of the myosin superfamily. J. Cell Sci. 134, jcs253708 (2021).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Chen, P.-W., Gasilina, A., Yadav, M. P. & Randazzo, P. A. Control of cell signaling by Arf GTPases and their regulators: focus on links to cancer and other GTPase families. Biochim. Biophys. Acta – Mol. Cell Res. 1869, 119171 (2022).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Donaldson, J. G. & Jackson, C. L. ARF family G proteins and their regulators: roles in membrane transport, development and disease. Nat. Rev. Mol. Cell Biol. 12, 362\u2013375 (2011).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Dong, C. et al. ADP-ribosylation factors modulate the cell surface transport of G protein-coupled receptors. J. Pharmacol. Exp. Ther. 333, 174\u2013183 (2010).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Cavenagh, M. M. et al. Intracellular distribution of arf proteins in mammalian cells. J. Biol. Chem. 271, 21767\u201321774 (1996).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Paleotti, O. et al. The small G-protein ARF6GTP recruits the AP-2 adaptor complex to membranes. J. Biol. Chem. 280, 21661\u201321666 (2005).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Poupart, M.-E., Fessart, D., Cotton, M., Laporte, S. A. & Claing, A. ARF6 regulates angiotensin II type 1 receptor endocytosis by controlling the recruitment of AP-2 and clathrin. Cell. Signal. 19, 2370\u20132378 (2007).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Delaney, K. A., Murph, M. M., Brown, L. M. & Radhakrishna, H. Transfer of M2 muscarinic acetylcholine receptors to clathrin-derived early endosomes following clathrin-independent endocytosis. J. Biol. Chem. 277, 33439\u201333446 (2002).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Claing, A. et al. \u03b2-arrestin-mediated ADP-ribosylation factor 6 activation and \u03b22-adrenergic receptor endocytosis. J. Biol. Chem. 276, 42509\u201342513 (2001).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Rosenberg, E. M. et al. The small molecule inhibitor NAV-2729 has a complex target profile including multiple ADP-ribosylation factor regulatory proteins. J. Biol. Chem. 299, 102992 (2023).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Montagnac, G. et al. Decoupling of activation and effector binding underlies ARF6 priming of fast endocytic recycling. Curr. Biol. 21, 574\u2013579 (2011).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Dana, R. R., Eigsti, C., Holmes, K. L. & Leto, T. L. A regulatory role for ADP-ribosylation factor 6 (ARF6) in activation of the phagocyte NADPH oxidase. J. Biol. Chem. 275, 32566\u201332571 (2000).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Matthees, E. S. F., Haider, R. S., Hoffmann, C. & Drube, J. Differential regulation of GPCRs\u2014are GRK expression levels the key? Front. Cell Dev. Biol. 9, 687489 (2021).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Nobles, K. N. et al. Distinct phosphorylation sites on the \u03b22 -adrenergic receptor establish a barcode that encodes differential functions of \u03b2-arrestin. Sci. Signal. 4, ra51 (2011).<\/p>\n

Liggett, S. B. Phosphorylation barcoding as a mechanism of directing GPCR signaling. Sci. Signal. 4, re3 (2011).<\/p>\n

Kee, T. R. et al. The multifaceted functions of \u03b2-arrestins and their therapeutic potential in neurodegenerative diseases. Exp. Mol. Med. 56, 129\u2013141 (2024).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Xiao, K. et al. Functional specialization of beta-arrestin interactions revealed by proteomic analysis. Proc. Natl. Acad. Sci. USA 104, 12011\u201312016 (2007).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Takahashi, Y. et al. VPS37A directs ESCRT recruitment for phagophore closure. J. Cell Biol. 218, 3336\u20133354 (2019).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Ram\u00edrez-Garc\u00eda, P. D. et al. A pH-responsive nanoparticle targets the neurokinin 1 receptor in endosomes to prevent chronic pain. Nat. Nanotechnol. 14, 1150\u20131159 (2019).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Chew, H. Y. et al. Endocytosis inhibition in humans to improve responses to ADCC-mediating antibodies. Cell 180, 895\u2013914.e27 (2020).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Lundgren, S. M. et al. Signaling dynamics distinguish high- and low-priority neutrophil chemoattractant receptors. Sci. Signal. 16, eadd1845 (2023).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Gera, N., Swanson, K. D. & Jin, T. \u03b2-Arrestin 1-dependent regulation of Rap2 is required for fMLP-stimulated chemotaxis in neutrophil-like HL-60 cells. J. Leukoc. Biol. 101, 239\u2013251 (2017).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Li, W. et al. MAGeCK enables robust identification of essential genes from genome-scale CRISPR\/Cas9 knockout screens. Genome Biol. 15, 554 (2014).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Bailey, T. L. & Gribskov, M. Combining evidence using p-values: application to sequence homology searches. Bioinformatics 14, 48\u201354 (1998).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Storey, J. D. A direct approach to false discovery rates. J. R. Stat. Soc. Ser. B Stat. Methodol. 64, 479\u2013498 (2002).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Reimand, J. et al. Pathway enrichment analysis and visualization of omics data using g:Profiler, GSEA, Cytoscape and EnrichmentMap. Nat. Protoc. 14, 482\u2013517 (2019).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Conway, J. R., Lex, A. & Gehlenborg, N. UpSetR: an R package for the visualization of intersecting sets and their properties. Bioinformatics 33, 2938\u20132940 (2017).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n","protected":false},"excerpt":{"rendered":"Peiseler, M. & Kubes, P. More friend than foe: the emerging role of neutrophils in tissue repair. J.…\n","protected":false},"author":2,"featured_media":365810,"comment_status":"","ping_status":"","sticky":false,"template":"","format":"standard","meta":{"footnotes":""},"categories":[7],"tags":[164890,164891,1437,61,60,2137,82,164892],"class_list":["post-365809","post","type-post","status-publish","format-standard","has-post-thumbnail","category-science","tag-chemotaxis","tag-endocytosis","tag-general","tag-ie","tag-ireland","tag-life-sciences","tag-science","tag-systems-analysis"],"_links":{"self":[{"href":"https:\/\/www.newsbeep.com\/ie\/wp-json\/wp\/v2\/posts\/365809","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/www.newsbeep.com\/ie\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/www.newsbeep.com\/ie\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/www.newsbeep.com\/ie\/wp-json\/wp\/v2\/users\/2"}],"replies":[{"embeddable":true,"href":"https:\/\/www.newsbeep.com\/ie\/wp-json\/wp\/v2\/comments?post=365809"}],"version-history":[{"count":0,"href":"https:\/\/www.newsbeep.com\/ie\/wp-json\/wp\/v2\/posts\/365809\/revisions"}],"wp:featuredmedia":[{"embeddable":true,"href":"https:\/\/www.newsbeep.com\/ie\/wp-json\/wp\/v2\/media\/365810"}],"wp:attachment":[{"href":"https:\/\/www.newsbeep.com\/ie\/wp-json\/wp\/v2\/media?parent=365809"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/www.newsbeep.com\/ie\/wp-json\/wp\/v2\/categories?post=365809"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/www.newsbeep.com\/ie\/wp-json\/wp\/v2\/tags?post=365809"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}