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- W808766328 abstract "Caleosin, a calcium-binding protein associated with plant lipid droplets, stimulates lipid accumulation when heterologously expressed in Saccharomyces cerevisiae. Accumulated lipids are stored in cytoplasmic lipid droplets that are stabilised by incorporated caleosin. We designed a set of mutants affecting putative crucial sites for caleosin function and association with lipid droplets, i.e. the N-terminus, the EF-hand motif and the proline-knot motif. We investigated the effect of introduced mutations on caleosin capacity to initiate lipid accumulation and on caleosin sorting within cell as well as on its association with lipid droplets. Our results strongly suggest that the N-terminal domain is essential for proper protein sorting and targeting to lipid droplets but not for enhancing lipid accumulation." @default.
- W808766328 created "2016-06-24" @default.
- W808766328 creator A5066110110 @default.
- W808766328 creator A5079092089 @default.
- W808766328 creator A5063908583 @default.
- W808766328 date "2015-08-01" @default.
- W808766328 modified "2023-10-12" @default.
- W808766328 title "N-terminus of seed caleosins is essential for lipid droplet sorting but not for lipid accumulation" @default.
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- W808766328 doi "https://doi.org/10.1016/j.abb.2015.05.008" @default.
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