{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T07:07:36Z","timestamp":1790665656808,"version":"4.1.0"},"reference-count":175,"publisher":"MDPI AG","issue":"11","license":[{"start":{"date-parts":[[2021,6,5]],"date-time":"2021-06-05T00:00:00Z","timestamp":1622851200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>ATP-binding cassette (ABC) transporters constitute one of the largest superfamilies of conserved proteins from bacteria to mammals. In humans, three members of this family are expressed in the peroxisomal membrane and belong to the subfamily D: ABCD1 (ALDP), ABCD2 (ALDRP), and ABCD3 (PMP70). These half-transporters must dimerize to form a functional transporter, but they are thought to exist primarily as tetramers. They possess overlapping but specific substrate specificity, allowing the transport of various lipids into the peroxisomal matrix. The defects of ABCD1 and ABCD3 are responsible for two genetic disorders called X-linked adrenoleukodystrophy and congenital bile acid synthesis defect 5, respectively. In addition to their role in peroxisome metabolism, it has recently been proposed that peroxisomal ABC transporters participate in cell signaling and cell control, particularly in cancer. This review presents an overview of the knowledge on the structure, function, and mechanisms involving these proteins and their link to pathologies. We summarize the different in vitro and in vivo models existing across the species to study peroxisomal ABC transporters and the consequences of their defects. Finally, an overview of the known and possible interactome involving these proteins, which reveal putative and unexpected new functions, is shown and discussed.<\/jats:p>","DOI":"10.3390\/ijms22116093","type":"journal-article","created":{"date-parts":[[2021,6,6]],"date-time":"2021-06-06T23:59:55Z","timestamp":1623023995000},"page":"6093","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":71,"title":["Peroxisomal ABC Transporters: An Update"],"prefix":"10.3390","volume":"22","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5077-5267","authenticated-orcid":false,"given":"Ali","family":"Tawbeh","sequence":"first","affiliation":[{"name":"Laboratoire Bio-PeroxIL EA7270, University of Bourgogne Franche-Comt\u00e9, 6 Boulevard Gabriel, 21000 Dijon, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Catherine","family":"Gondcaille","sequence":"additional","affiliation":[{"name":"Laboratoire Bio-PeroxIL EA7270, University of Bourgogne Franche-Comt\u00e9, 6 Boulevard Gabriel, 21000 Dijon, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Doriane","family":"Trompier","sequence":"additional","affiliation":[{"name":"Laboratoire Bio-PeroxIL EA7270, University of Bourgogne Franche-Comt\u00e9, 6 Boulevard Gabriel, 21000 Dijon, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9237-1727","authenticated-orcid":false,"given":"St\u00e9phane","family":"Savary","sequence":"additional","affiliation":[{"name":"Laboratoire Bio-PeroxIL EA7270, University of Bourgogne Franche-Comt\u00e9, 6 Boulevard Gabriel, 21000 Dijon, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,6,5]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1146\/annurev-biochem-011520-105201","article-title":"Structural and Mechanistic Principles of ABC Transporters","volume":"89","author":"Thomas","year":"2020","journal-title":"Annu. 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