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Fld1p, a functional homologue of human seipin, regulates the size of lipid droplets in yeast
Lipid droplets (LDs) are emerging cellular organelles that are of crucial importance in cell biology and human diseases. In this study, we present our screen of ∼4,700 Saccharomyces cerevisiae mutants for abnormalities in the number and morphology of LDs; we identify 17 fld (few LDs) and 116 mld (ma...
Autores principales: | , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2008
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2234226/ https://www.ncbi.nlm.nih.gov/pubmed/18250201 http://dx.doi.org/10.1083/jcb.200711136 |
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author | Fei, Weihua Shui, Guanghou Gaeta, Bruno Du, Ximing Kuerschner, Lars Li, Peng Brown, Andrew J. Wenk, Markus R. Parton, Robert G. Yang, Hongyuan |
author_facet | Fei, Weihua Shui, Guanghou Gaeta, Bruno Du, Ximing Kuerschner, Lars Li, Peng Brown, Andrew J. Wenk, Markus R. Parton, Robert G. Yang, Hongyuan |
author_sort | Fei, Weihua |
collection | PubMed |
description | Lipid droplets (LDs) are emerging cellular organelles that are of crucial importance in cell biology and human diseases. In this study, we present our screen of ∼4,700 Saccharomyces cerevisiae mutants for abnormalities in the number and morphology of LDs; we identify 17 fld (few LDs) and 116 mld (many LDs) mutants. One of the fld mutants (fld1) is caused by the deletion of YLR404W, a previously uncharacterized open reading frame. Cells lacking FLD1 contain strikingly enlarged (supersized) LDs, and LDs from fld1Δ cells demonstrate significantly enhanced fusion activities both in vivo and in vitro. Interestingly, the expression of human seipin, whose mutant forms are associated with Berardinelli-Seip congenital lipodystrophy and motoneuron disorders, rescues LD-associated defects in fld1Δ cells. Lipid profiling reveals alterations in acyl chain compositions of major phospholipids in fld1Δ cells. These results suggest that an evolutionally conserved function of seipin in phospholipid metabolism and LD formation may be functionally important in human adipogenesis. |
format | Text |
id | pubmed-2234226 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-22342262008-08-11 Fld1p, a functional homologue of human seipin, regulates the size of lipid droplets in yeast Fei, Weihua Shui, Guanghou Gaeta, Bruno Du, Ximing Kuerschner, Lars Li, Peng Brown, Andrew J. Wenk, Markus R. Parton, Robert G. Yang, Hongyuan J Cell Biol Research Articles Lipid droplets (LDs) are emerging cellular organelles that are of crucial importance in cell biology and human diseases. In this study, we present our screen of ∼4,700 Saccharomyces cerevisiae mutants for abnormalities in the number and morphology of LDs; we identify 17 fld (few LDs) and 116 mld (many LDs) mutants. One of the fld mutants (fld1) is caused by the deletion of YLR404W, a previously uncharacterized open reading frame. Cells lacking FLD1 contain strikingly enlarged (supersized) LDs, and LDs from fld1Δ cells demonstrate significantly enhanced fusion activities both in vivo and in vitro. Interestingly, the expression of human seipin, whose mutant forms are associated with Berardinelli-Seip congenital lipodystrophy and motoneuron disorders, rescues LD-associated defects in fld1Δ cells. Lipid profiling reveals alterations in acyl chain compositions of major phospholipids in fld1Δ cells. These results suggest that an evolutionally conserved function of seipin in phospholipid metabolism and LD formation may be functionally important in human adipogenesis. The Rockefeller University Press 2008-02-11 /pmc/articles/PMC2234226/ /pubmed/18250201 http://dx.doi.org/10.1083/jcb.200711136 Text en Copyright © 2008, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Research Articles Fei, Weihua Shui, Guanghou Gaeta, Bruno Du, Ximing Kuerschner, Lars Li, Peng Brown, Andrew J. Wenk, Markus R. Parton, Robert G. Yang, Hongyuan Fld1p, a functional homologue of human seipin, regulates the size of lipid droplets in yeast |
title | Fld1p, a functional homologue of human seipin, regulates the size of lipid droplets in yeast |
title_full | Fld1p, a functional homologue of human seipin, regulates the size of lipid droplets in yeast |
title_fullStr | Fld1p, a functional homologue of human seipin, regulates the size of lipid droplets in yeast |
title_full_unstemmed | Fld1p, a functional homologue of human seipin, regulates the size of lipid droplets in yeast |
title_short | Fld1p, a functional homologue of human seipin, regulates the size of lipid droplets in yeast |
title_sort | fld1p, a functional homologue of human seipin, regulates the size of lipid droplets in yeast |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2234226/ https://www.ncbi.nlm.nih.gov/pubmed/18250201 http://dx.doi.org/10.1083/jcb.200711136 |
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