{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,28]],"date-time":"2026-10-28T02:45:43Z","timestamp":1793155543419,"version":"4.5.0"},"reference-count":51,"publisher":"National Academy of Sciences","issue":"13","license":[{"start":{"date-parts":[[2026,3,27]],"date-time":"2026-03-27T00:00:00Z","timestamp":1774569600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100003725","name":"National Research Foundation of Korea","doi-asserted-by":"publisher","award":["RS-2023-00207997"],"award-info":[{"award-number":["RS-2023-00207997"]}],"id":[{"id":"10.13039\/501100003725","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003645","name":"National Cancer Center","doi-asserted-by":"publisher","award":["NCC-2411910"],"award-info":[{"award-number":["NCC-2411910"]}],"id":[{"id":"10.13039\/501100003645","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2026,3,31]]},"abstract":"<jats:p>\n                    The bacterial pathogen\n                    <jats:italic toggle=\"yes\">Legionella pneumophila<\/jats:italic>\n                    secretes effector proteins that remodel host endomembranes to establish a replication-permissive niche known as the\n                    <jats:italic toggle=\"yes\">Legionella<\/jats:italic>\n                    -containing vacuole (LCV). Among these, SetA disrupts vesicle trafficking by glucosylating the small GTPase Rab1, essential for ER-to-Golgi transport. Here, we report comprehensive structural and mechanistic insights into SetA-mediated Rab1 glucosylation and its PI3P-dependent membrane targeting. Crystal structures of its N-terminal glycosyltransferase and C-terminal lipid-binding domains, captured in multiple ligand-bound states, reveal how SetA specifically recognizes GDP-bound Rab1 and the head group of phosphatidylinositol 3-phosphate (PI3P), which is enriched on early LCV membranes. SAXS-based full-length modeling, biochemical assays, and cellular imaging analyses demonstrate that SetA integrates Rab1 modification with membrane localization, thereby perturbing Golgi integrity and ER morphology. Together, these findings define the dual structural mechanisms underlying SetA\u2019s coordination of substrate glucosylation and membrane association, providing a spatiotemporal framework for understanding\n                    <jats:italic toggle=\"yes\">Legionella<\/jats:italic>\n                    \u2019s early infection strategy.\n                  <\/jats:p>","DOI":"10.1073\/pnas.2535016123","type":"journal-article","created":{"date-parts":[[2026,3,27]],"date-time":"2026-03-27T17:19:52Z","timestamp":1774631992000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":1,"title":["Structural insights into SetA-mediated Rab1 glucosylation and PI3P-guided localization during early\n                    <i>Legionella<\/i>\n                    infection"],"prefix":"10.1073","volume":"123","author":[{"given":"Ha Na","family":"Im","sequence":"first","affiliation":[{"name":"Research Institute, National Cancer Center","place":["Goyang, Republic of Korea"]},{"name":"Department of Chemistry, College of Natural Sciences, Seoul National University","place":["Seoul, Republic of Korea"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3017-4664","authenticated-orcid":false,"given":"Yeon","family":"Lee","sequence":"additional","affiliation":[{"name":"Research Institute, National Cancer Center","place":["Goyang, Republic of Korea"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yunju","family":"Song","sequence":"additional","affiliation":[{"name":"Research Institute, National Cancer Center","place":["Goyang, Republic of Korea"]},{"name":"Department of Biomedical Sciences, Seoul National University","place":["Seoul, Republic of Korea"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hyunggu","family":"Hahn","sequence":"additional","affiliation":[{"name":"Research Institute, National Cancer Center","place":["Goyang, Republic of Korea"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hyerry","family":"Jeon","sequence":"additional","affiliation":[{"name":"Research Institute, National Cancer Center","place":["Goyang, Republic of Korea"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Donghyuk","family":"Shin","sequence":"additional","affiliation":[{"name":"Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University","place":["Seoul, Republic of Korea"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3886-4579","authenticated-orcid":false,"given":"Sangho","family":"Lee","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Sungkyunkwan University","place":["Suwon, Republic of Korea"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7623-3949","authenticated-orcid":false,"given":"Kyung-Hee","family":"Kim","sequence":"additional","affiliation":[{"name":"Research Institute, National Cancer Center","place":["Goyang, Republic of Korea"]},{"name":"Department of Applied Chemistry, School of Science and Technology, Kookmin University","place":["Seoul, Republic of Korea"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kyung-Tae","family":"Kim","sequence":"additional","affiliation":[{"name":"Research Institute, National Cancer Center","place":["Goyang, Republic of Korea"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Se Won","family":"Suh","sequence":"additional","affiliation":[{"name":"Department of Chemistry, College of Natural Sciences, Seoul National University","place":["Seoul, Republic of Korea"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0701-0503","authenticated-orcid":false,"given":"Dong Man","family":"Jang","sequence":"additional","affiliation":[{"name":"Research Institute, National Cancer Center","place":["Goyang, Republic of Korea"]},{"name":"Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School","place":["Boston"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1095-6463","authenticated-orcid":false,"given":"Hyoun Sook","family":"Kim","sequence":"additional","affiliation":[{"name":"Research Institute, National Cancer Center","place":["Goyang, Republic of Korea"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2026,3,27]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"publisher","DOI":"10.1128\/CMR.00029-14"},{"key":"e_1_3_4_2_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev-pathmechdis-012419-032742"},{"key":"e_1_3_4_3_2","doi-asserted-by":"publisher","DOI":"10.1101\/cshperspect.a009993"},{"key":"e_1_3_4_4_2","doi-asserted-by":"publisher","DOI":"10.1038\/srep33442"},{"key":"e_1_3_4_5_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrmicro.2017.67"},{"key":"e_1_3_4_6_2","doi-asserted-by":"publisher","DOI":"10.3389\/fmicb.2015.00087"},{"key":"e_1_3_4_7_2","doi-asserted-by":"publisher","DOI":"10.3389\/fimmu.2015.00447"},{"key":"e_1_3_4_8_2","doi-asserted-by":"publisher","DOI":"10.1111\/cmi.12450"},{"key":"e_1_3_4_9_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.mib.2008.12.004"},{"key":"e_1_3_4_10_2","doi-asserted-by":"publisher","DOI":"10.3389\/fmicb.2011.00208"},{"key":"e_1_3_4_11_2","doi-asserted-by":"publisher","DOI":"10.4161\/sgtp.28651"},{"key":"e_1_3_4_12_2","doi-asserted-by":"publisher","DOI":"10.1111\/cmi.12533"},{"key":"e_1_3_4_13_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.tim.2015.07.003"},{"key":"e_1_3_4_14_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.01798-07"},{"key":"e_1_3_4_15_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbagen.2009.07.022"},{"key":"e_1_3_4_16_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.71.1.181-186.2003"},{"key":"e_1_3_4_17_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0601562103"},{"key":"e_1_3_4_18_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.celrep.2017.10.088"},{"key":"e_1_3_4_19_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1462-5822.2008.01249.x"},{"key":"e_1_3_4_20_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1462-5822.2012.01761.x"},{"key":"e_1_3_4_21_2","doi-asserted-by":"publisher","DOI":"10.1038\/s41421-018-0055-9"},{"key":"e_1_3_4_22_2","doi-asserted-by":"publisher","DOI":"10.1105\/tpc.12.11.2201"},{"key":"e_1_3_4_23_2","doi-asserted-by":"publisher","DOI":"10.1038\/s41589-018-0189-y"},{"key":"e_1_3_4_24_2","doi-asserted-by":"publisher","DOI":"10.1007\/s00210-018-1562-9"},{"key":"e_1_3_4_25_2","first-page":"49","article-title":"Formation 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N. Im Y. Lee D. M. Jang H. Hahn H. S. Kim Crystal structure of the glycosyltransferase domain of Legionella SetA (unbound). Protein Data Bank. https:\/\/doi.org\/10.2210\/pdb8X4J\/pdb. Deposited 15 November 2023.","DOI":"10.2210\/pdb8x4j\/pdb"},{"key":"e_1_3_4_49_2","doi-asserted-by":"crossref","unstructured":"H. N. Im Y. Lee D. M. Jang H. Hahn H. S. Kim Crystal structure of the glycosyltransferase domain of Legionella SetA in complex with UDPGlc. Protein Data Bank. https:\/\/doi.org\/10.2210\/pdb8X4K\/pdb. Deposited 15 November 2023.","DOI":"10.2210\/pdb8x4k\/pdb"},{"key":"e_1_3_4_50_2","doi-asserted-by":"crossref","unstructured":"H. N. Im Y. Lee D. M. Jang H. Hahn H. S. Kim Crystal structure of the glycosyltransferase domain of Legionella SetA in complex with UDP. Protein Data Bank. https:\/\/doi.org\/10.2210\/pdb8X4M\/pdb. Deposited 15 November 2023.","DOI":"10.2210\/pdb8x4m\/pdb"},{"key":"e_1_3_4_51_2","doi-asserted-by":"crossref","unstructured":"H. N. Im Y. Lee D. M. Jang H. 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