Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-9679
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dc.contributor.authorSchiffmann, Andrea-
dc.contributor.authorAhlswede, Lena-
dc.contributor.authorGimpl, Gerald-
dc.date.accessioned2023-11-14T10:25:34Z-
dc.date.available2023-11-14T10:25:34Z-
dc.date.issued2023-
dc.identifier.urihttps://openscience.ub.uni-mainz.de/handle/20.500.12030/9697-
dc.description.abstractThe enzyme acyl-CoA:cholesterol acyltransferase (ACAT) is normally localized in the endoplasmic reticulum (ER) where it can esterify cholesterol for storage in lipid droplets and/or the formation of lipoproteins. Here, we report that ACAT can translocate from the ER into vesicular structures in response to different ACAT inhibitors. The translocation was fast (within minutes), reversible and occurred in different cell types. Interestingly, oleic acid was able to fasten the re-translocation from vesicles back into the reticular ER network. The process of ACAT translocation could also be induced by cyclodextrins, cholesterol, lanosterol (but not 4-cholestene-3 one), 25-hydroxycholesterol, and by certain stress stimuli such as hyperosmolarity (sucrose treatment), temperature change, or high-density cultivation. In vitro esterification showed that ACAT remains fully active after it has been translocated to vesicles in response to hyperosmotic sucrose treatment of the cells. The translocation process was not accompanied by changes in the electrophoretic mobility of ACAT, even after chemical crosslinking. Interestingly, the protein synthesis inhibitor cycloheximide showed a stimulating effect on ACAT activity and prevented the translocation of ACAT from the ER into vesicles.en_GB
dc.language.isoengde
dc.rightsCC BY*
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/*
dc.subject.ddc540 Chemiede_DE
dc.subject.ddc540 Chemistry and allied sciencesen_GB
dc.titleReversible translocation of acyl-CoA:cholesterol acyltransferase (ACAT) between the endoplasmic reticulum and vesicular structuresen_GB
dc.typeZeitschriftenaufsatzde
dc.identifier.doihttp://doi.org/10.25358/openscience-9679-
jgu.type.contenttypeScientific articlede
jgu.type.dinitypearticleen_GB
jgu.type.versionPublished versionde
jgu.type.resourceTextde
jgu.organisation.departmentFB 09 Chemie, Pharmazie u. Geowissensch.de
jgu.organisation.number7950-
jgu.organisation.nameJohannes Gutenberg-Universität Mainz-
jgu.rights.accessrightsopenAccess-
jgu.journal.titleFrontiers in Molecular Biosciencesde
jgu.journal.volume10de
jgu.pages.alternative1258799de
jgu.publisher.year2023-
jgu.publisher.nameFrontiersde
jgu.publisher.placeLausannede
jgu.publisher.issn2296-889Xde
jgu.organisation.placeMainz-
jgu.subject.ddccode540de
jgu.publisher.doi10.3389/fmolb.2023.1258799de
jgu.organisation.rorhttps://ror.org/023b0x485-
jgu.subject.dfgNaturwissenschaftende
Appears in collections:DFG-491381577-G

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