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Cited 18 time in webofscience Cited 17 time in scopus
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dc.contributor.authorLi-Beisson, Y.-
dc.contributor.authorKong, F.-
dc.contributor.authorWang, P.-
dc.contributor.authorLEE, YOUNGSOOK-
dc.contributor.authorKang, B.-H.-
dc.date.accessioned2021-12-27T02:40:06Z-
dc.date.available2021-12-27T02:40:06Z-
dc.date.created2021-07-06-
dc.date.issued2021-08-
dc.identifier.issn0028-646X-
dc.identifier.urihttps://oasis.postech.ac.kr/handle/2014.oak/108483-
dc.description.abstractLipid droplets (LDs) are ubiquitous and specialized organelles in eukaryotic cells. Consisting of a triacylglycerol core surrounded by a monolayer of membrane lipids, LDs are decorated with proteins and have myriad functions, from carbon/energy storage to membrane lipid remodeling and signal transduction. The biogenesis and turnover of LDs are therefore tightly coordinated with cellular metabolic needs in a fluctuating environment. Lipid droplet turnover requires remodeling of the protein coat, lipolysis, autophagy and fatty acid beta-oxidation. Several key components of these processes have been identified in Chlamydomonas (Chlamydomonas reinhardtii), including the major lipid droplet protein, a CXC-domain containing regulatory protein, the phosphatidylethanolamine-binding DTH1 (DELAYED IN TAG HYDROLYSIS1), two lipases and two enzymes involved in fatty acid beta-oxidation. Here, we review LD turnover and discuss its physiological significance in Chlamydomonas, a major model green microalga in research on algal oil.-
dc.languageEnglish-
dc.publisherBlackwell Publishing Inc.-
dc.relation.isPartOfNew Phytologist-
dc.titleThe disassembly of lipid droplets in Chlamydomonas-
dc.typeArticle-
dc.identifier.doi10.1111/nph.17505-
dc.type.rimsART-
dc.identifier.bibliographicCitationNew Phytologist, v.231, no.4, pp.1359 - 1364-
dc.identifier.wosid000662228700001-
dc.citation.endPage1364-
dc.citation.number4-
dc.citation.startPage1359-
dc.citation.titleNew Phytologist-
dc.citation.volume231-
dc.contributor.affiliatedAuthorLEE, YOUNGSOOK-
dc.identifier.scopusid2-s2.0-85108216339-
dc.description.journalClass1-
dc.description.journalClass1-
dc.description.isOpenAccessY-
dc.type.docTypeReview-
dc.subject.keywordPlusOIL BODIES-
dc.subject.keywordPlusREINHARDTII-
dc.subject.keywordPlusPROTEIN-
dc.subject.keywordPlusTRIACYLGLYCEROL-
dc.subject.keywordPlusACCUMULATION-
dc.subject.keywordPlusDEGRADATION-
dc.subject.keywordPlusMETABOLISM-
dc.subject.keywordPlusPEROXISOME-
dc.subject.keywordPlusAUTOPHAGY-
dc.subject.keywordPlusTURNOVER-
dc.subject.keywordAuthoramphipathic helix-
dc.subject.keywordAuthorautophagy-
dc.subject.keywordAuthorChlamydomonas reinhardtii-
dc.subject.keywordAuthorlipase-
dc.subject.keywordAuthornitrogen recovery-
dc.subject.keywordAuthorperoxisome-
dc.subject.keywordAuthorphosphatidylethanolamine-
dc.subject.keywordAuthorscaffold protein-
dc.relation.journalWebOfScienceCategoryPlant Sciences-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaPlant Sciences-

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