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dc.contributor.authorCarmichael, RE
dc.contributor.authorIslinger, M
dc.contributor.authorSchrader, M
dc.date.accessioned2022-06-13T07:23:45Z
dc.date.issued2022-06-14
dc.date.updated2022-06-10T16:49:40Z
dc.description.abstractPeroxisomes are highly dynamic and responsive organelles, which can adjust their morphology, number, intracellular position, and metabolic functions according to cellular needs. Peroxisome multiplication in mammalian cells involves the concerted action of the membrane shaping protein PEX11β and division proteins such as the membrane adaptors FIS1 and MFF, which recruit the fission GTPase DRP1 to the peroxisomal membrane. The latter proteins are also involved in mitochondrial division. Patients with loss of DRP1, MFF or PEX11β function have been identified, showing abnormalities in peroxisomal (and, for the shared proteins, mitochondrial) dynamics as well as developmental and neurological defects, whereas metabolic functions of the organelles are often unaffected. Here, we provide a timely update on peroxisomal membrane dynamics with particular focus on peroxisome formation by membrane growth and division. We address the function of PEX11β in these processes, as well as the role of peroxisome-ER contacts in lipid transfer for peroxisomal membrane expansion. Furthermore, we summarize the clinical phenotypes and pathophysiology of patients with defects in the key division proteins DRP1, MFF, and PEX11β as well as in the peroxisome-ER tether ACBD5. Potential therapeutic strategies for these rare disorders with limited treatment options are discusseden_GB
dc.description.sponsorshipBiotechnology & Biological Sciences Research Council (BBSRC)en_GB
dc.identifier.citationVol. 11 (12), article 1922en_GB
dc.identifier.doi10.3390/cells11121922
dc.identifier.grantnumberBB/T002255/1en_GB
dc.identifier.grantnumberBB/R016844/1en_GB
dc.identifier.urihttp://hdl.handle.net/10871/129917
dc.identifierORCID: 0000-0003-2146-0535 (Schrader, Michael)
dc.language.isoenen_GB
dc.publisherMDPIen_GB
dc.rights© 2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).en_GB
dc.subjectperoxisomesen_GB
dc.subjectmitochondriaen_GB
dc.subjectorganelle dynamicsen_GB
dc.subjectdivision defectsen_GB
dc.subjectdynamin-related protein 1en_GB
dc.subjectmitochondrial fission factoren_GB
dc.subjectPEX11βen_GB
dc.subjectFIS1en_GB
dc.subjectACBD5en_GB
dc.subjectmembrane fissionen_GB
dc.titleFission Impossible (?) – New Insights into Disorders of Peroxisome Dynamicsen_GB
dc.typeArticleen_GB
dc.date.available2022-06-13T07:23:45Z
dc.identifier.issn2073-4409
dc.descriptionThis is the final version. Available on open access from MDPI via the DOI in this recorden_GB
dc.descriptionData Availability Statement: All datasets generated for this study are included in the article.en_GB
dc.identifier.journalCellsen_GB
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/  en_GB
dcterms.dateAccepted2022-06-10
rioxxterms.versionVoRen_GB
rioxxterms.licenseref.startdate2022-06-10
rioxxterms.typeJournal Article/Reviewen_GB
refterms.dateFCD2022-06-10T16:49:43Z
refterms.versionFCDAM
refterms.dateFOA2022-06-28T14:15:56Z
refterms.panelAen_GB


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© 2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
Except where otherwise noted, this item's licence is described as © 2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).