Sec14 family of lipid transfer proteins in yeasts

Holic̆, Roman; Šťastný, Dominik; Griač, Peter

doi:10.1016/j.bbalip.2021.158990

Cited by 6 publications

(11 citation statements)

References 181 publications

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“…Sec14-family proteins are also conserved in other yeasts (Holič et al 2021 ). Eight genes encoding Sec14-family proteins are present in the genome of Y. lipolytica (Fig.…”

Section: Introductionmentioning

confidence: 99%

Utilization of n-alkane and roles of lipid transfer proteins in Yarrowia lipolytica

Fukuda

2023

World J Microbiol Biotechnol

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Yarrowia lipolytica, a dimorphic yeast belonging to the Ascomycota, has potent abilities to utilize hydrophobic compounds, such as n-alkanes and fatty acids, as carbon and energy sources. Yarrowia lipolytica can synthesize and accumulate large amounts of lipids, making it a promising host to produce various lipids and convert n-alkanes to useful compounds. For advanced use of Y. lipolytica in these applications, it is necessary to understand the metabolism of these hydrophobic compounds in this yeast and the underlying molecular mechanisms. In this review, current knowledge on the n-alkane metabolism and how this is regulated in Y. lipolytica is summarized. Furthermore, recent studies revealed that lipid transfer proteins are involved in the utilization of n-alkanes and the regulation of cell morphology in response to n-alkanes. This review discusses the roles of membrane lipids in these processes in Y. lipolytica.

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“…Sec14-family proteins are also conserved in other yeasts (Holič et al 2021 ). Eight genes encoding Sec14-family proteins are present in the genome of Y. lipolytica (Fig.…”

Section: Introductionmentioning

confidence: 99%

Utilization of n-alkane and roles of lipid transfer proteins in Yarrowia lipolytica

Fukuda

2023

World J Microbiol Biotechnol

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“…The Sec14 family is identified in all eukaryotes and characterized by a conserved Sec14 domain that can bind and transfer a wide range of lipids and hydrophobic vitamins in vitro ( 14 ). The Saccharomyces cerevisiae genome encodes prototype Sec14p and five Sec14 homologues (designated Sfh1p-Sfh5p) that exhibit various physiological functions in lipid metabolism and membrane trafficking ( 15 ). There are ~30 Sec14-containing proteins in Homo sapiens, and dysfunctions of them would cause a number of diseases such as vitamin E deficiency, autosomal-dominant cancers, and ataxia ( 14 ).…”

mentioning

confidence: 99%

Arabidopsis Sec14 proteins (SFH5 and SFH7) mediate interorganelle transport of phosphatidic acid and regulate chloroplast development

Yao

Yang

et al. 2023

Proc. Natl. Acad. Sci. U.S.A.

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Lipids establish the specialized thylakoid membrane of chloroplast in eukaryotic photosynthetic organisms, while the molecular basis of lipid transfer from other organelles to chloroplast remains further elucidation. Here we revealed the structural basis of Arabidopsis Sec14 homology proteins AtSFH5 and AtSFH7 in transferring phosphatidic acid (PA) from endoplasmic reticulum (ER) to chloroplast, and whose function in regulating the lipid composition of chloroplast and thylakoid development. AtSFH5 and AtSFH7 localize at both ER and chloroplast, whose deficiency resulted in an abnormal chloroplast structure and a decreased thickness of stacked thylakoid membranes. We demonstrated that AtSFH5, but not yeast and human Sec14 proteins, could specifically recognize and transfer PA in vitro. Crystal structures of the AtSFH5-Sec14 domain in complex with L-α-phosphatidic acid (L-α-PA) and 1,2-dipalmitoyl-sn-glycero-3-phosphate (DPPA) revealed that two PA ligands nestled in the central cavity with different configurations, elucidating the specific binding mode of PA to AtSFH5, different from the reported phosphatidylethanolamine (PE)/phosphatidylcholine (PC)/phosphatidylinositol (PI) binding modes. Quantitative lipidomic analysis of chloroplast lipids showed that PA and monogalactosyldiacylglycerol (MGDG), particularly the C18 fatty acids at sn -2 position in MGDG were significantly decreased, indicating a disrupted ER-to-plastid (chloroplast) lipid transfer, under deficiency of AtSFH5 and AtSFH7. Our studies identified the role and elucidated the structural basis of plant SFH proteins in transferring PA between organelles, and suggested a model for ER-chloroplast interorganelle phospholipid transport from inherent ER to chloroplast derived from endosymbiosis of a cyanobacteriumproviding a mechanism involved in the adaptive evolution of cellular plastids.

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“…In this issue of Plant Physiology , Yang et al reveal a new role for Sec14-like proteins AtPITP7 and OsPITP6 in regulating phosphorous utilization in chloroplasts and present exciting possibilities for manipulating OsPITP6 expression to improve growth and yield in phosphate-limiting conditions ( Yang et al 2023 ). In yeast, Sec14 family proteins are some of the most extensively studied lipid transfer proteins ( Holič et al 2021 ). Specifically, many Sec14 family proteins mediate transport of phosphatidylinositol between membrane bilayers and are also able to bind ligands such as phosphatidylcholine, sterols, squalene, phosphatidylserine, and heme ( Holič et al 2021 ).…”

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confidence: 99%

Sec14-like proteins to the rescue: Improving plant performance in low-phosphate conditions

McMillan

2023

Plant Physiology

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Sec14 family of lipid transfer proteins in yeasts

Cited by 6 publications

References 181 publications

Utilization of n-alkane and roles of lipid transfer proteins in Yarrowia lipolytica

Utilization of n-alkane and roles of lipid transfer proteins in Yarrowia lipolytica

Arabidopsis Sec14 proteins (SFH5 and SFH7) mediate interorganelle transport of phosphatidic acid and regulate chloroplast development

Sec14-like proteins to the rescue: Improving plant performance in low-phosphate conditions

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