{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,17]],"date-time":"2026-05-17T12:45:51Z","timestamp":1779021951181,"version":"3.51.4"},"reference-count":76,"publisher":"The Company of Biologists","issue":"20","license":[{"start":{"date-parts":[[2023,10,18]],"date-time":"2023-10-18T00:00:00Z","timestamp":1697587200000},"content-version":"vor","delay-in-days":3,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["R01AI130139"],"award-info":[{"award-number":["R01AI130139"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["R56AI173133"],"award-info":[{"award-number":["R56AI173133"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["T32AI060546"],"award-info":[{"award-number":["T32AI060546"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100007699","name":"University of Georgia","doi-asserted-by":"crossref","id":[{"id":"10.13039\/100007699","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2023,10,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>The malaria-causing parasite, Plasmodium falciparum completely remodels its host red blood cell (RBC) through the export of several hundred parasite proteins, including transmembrane proteins, across multiple membranes to the RBC. However, the process by which these exported membrane proteins are extracted from the parasite plasma membrane for export remains unknown. To address this question, we fused the exported membrane protein, skeleton binding protein 1 (SBP1), with TurboID, a rapid, efficient and promiscuous biotin ligase (SBP1TbID). Using time-resolved proximity biotinylation and label-free quantitative proteomics, we identified two groups of SBP1TbID interactors \u2013 early interactors (pre-export) and late interactors (post-export). Notably, two promising membrane-associated proteins were identified as pre-export interactors, one of which possesses a predicted translocon domain, that could facilitate the export of membrane proteins. Further investigation using conditional mutants of these candidate proteins showed that these proteins were essential for asexual growth and localize to the host\u2013parasite interface during early stages of the intraerythrocytic cycle. These data suggest that they might play a role in ushering membrane proteins from the parasite plasma membrane for export to the host RBC.<\/jats:p>","DOI":"10.1242\/jcs.260506","type":"journal-article","created":{"date-parts":[[2023,9,29]],"date-time":"2023-09-29T05:20:21Z","timestamp":1695964821000},"source":"Crossref","is-referenced-by-count":13,"title":["Time-resolved proximity biotinylation implicates a porin protein in export of transmembrane malaria parasite effectors"],"prefix":"10.1242","volume":"136","author":[{"given":"David","family":"Anaguano","sequence":"first","affiliation":[{"name":"University of Georgia 1 Department of Cellular Biology , , Athens, GA , USA"},{"name":"Center for Tropical and Emerging Global Diseases, University of Georgia 2 , Athens, GA 30602 , USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3850-0142","authenticated-orcid":false,"given":"Watcharatip","family":"Dedkhad","sequence":"additional","affiliation":[{"name":"University of Georgia 1 Department of Cellular Biology , , Athens, GA , USA"},{"name":"Center for Tropical and Emerging Global Diseases, University of Georgia 2 , Athens, GA 30602 , USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Carrie F.","family":"Brooks","sequence":"additional","affiliation":[{"name":"Center for Tropical and Emerging Global Diseases, University of Georgia 2 , Athens, GA 30602 , USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"David W.","family":"Cobb","sequence":"additional","affiliation":[{"name":"University of Georgia 1 Department of Cellular Biology , , Athens, GA , USA"},{"name":"Center for Tropical and Emerging Global Diseases, University of Georgia 2 , Athens, GA 30602 , USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6367-6284","authenticated-orcid":false,"given":"Vasant","family":"Muralidharan","sequence":"additional","affiliation":[{"name":"University of Georgia 1 Department of Cellular Biology , , Athens, GA , USA"},{"name":"Center for Tropical and Emerging Global Diseases, University of Georgia 2 , Athens, GA 30602 , USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"237","published-online":{"date-parts":[[2023,10,18]]},"reference":[{"key":"2023101810413142600_JCS260506C1","doi-asserted-by":"publisher","first-page":"D898","DOI":"10.1093\/nar\/gkab929","article-title":"VEuPathDB: the eukaryotic pathogen, vector and host bioinformatics resource center","volume":"50","author":"Amos","year":"2022","journal-title":"Nucleic Acids Res."},{"key":"2023101810413142600_JCS260506C76","doi-asserted-by":"publisher","first-page":"679","DOI":"10.1146\/annurev-biochem-032620-104527","article-title":"Role of the TOM complex in protein import into mitochondria: atructural views","volume":"91","author":"Araiso","year":"2022","journal-title":"Annu. 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