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...
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| Veröffentlicht in: | The Journal of cell biology 2008-02, Vol.180 (3), p.473-482 |
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| creator | Fei, Weihua Shui, Guanghou Gaeta, Bruno Du, Ximing Kuerschner, Lars Li, Peng Brown, Andrew J Wenk, Markus R Parton, Robert G Yang, Hongyuan |
| 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. |
| doi_str_mv | 10.1083/jcb.200711136 |
| format | Article |
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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.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.200711136</identifier><identifier>PMID: 18250201</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: The Rockefeller University Press</publisher><subject>Amino Acid Sequence ; Amino acids ; Animals ; Cell growth ; Cells ; Cellular biology ; Centrifugation ; Conserved Sequence ; Cytoplasm - metabolism ; Cytoplasm - ultrastructure ; Fluorescence ; Green Fluorescent Proteins ; GTP-Binding Protein gamma Subunits - genetics ; GTP-Binding Protein gamma Subunits - isolation & purification ; GTP-Binding Protein gamma Subunits - metabolism ; Humans ; Lipid Metabolism - physiology ; Lipids ; Lipodystrophy ; Membrane Proteins - genetics ; Membrane Proteins - isolation & purification ; Membrane Proteins - metabolism ; Metabolism ; Mice ; Microscopy ; Microscopy, Electron, Transmission ; Molecular Sequence Data ; Mutation ; Organelles - metabolism ; Organelles - ultrastructure ; Phospholipids ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae - ultrastructure ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - isolation & purification ; Saccharomyces cerevisiae Proteins - metabolism ; Sequence Homology, Amino Acid ; Steepest descent method ; Yeast ; Yeasts</subject><ispartof>The Journal of cell biology, 2008-02, Vol.180 (3), p.473-482</ispartof><rights>Copyright 2008 The Rockefeller University Press</rights><rights>Copyright Rockefeller University Press Feb 11, 2008</rights><rights>Copyright © 2008, The Rockefeller University Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c555t-10c6d6fd0f90daabcaff2395759fd8ff9851290e880284cf0d9c228ad37488313</citedby><cites>FETCH-LOGICAL-c555t-10c6d6fd0f90daabcaff2395759fd8ff9851290e880284cf0d9c228ad37488313</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18250201$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fei, Weihua</creatorcontrib><creatorcontrib>Shui, Guanghou</creatorcontrib><creatorcontrib>Gaeta, Bruno</creatorcontrib><creatorcontrib>Du, Ximing</creatorcontrib><creatorcontrib>Kuerschner, Lars</creatorcontrib><creatorcontrib>Li, Peng</creatorcontrib><creatorcontrib>Brown, Andrew J</creatorcontrib><creatorcontrib>Wenk, Markus R</creatorcontrib><creatorcontrib>Parton, Robert G</creatorcontrib><creatorcontrib>Yang, Hongyuan</creatorcontrib><title>Fld1p, a functional homologue of human seipin, regulates the size of lipid droplets in yeast</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><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.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Cell growth</subject><subject>Cells</subject><subject>Cellular biology</subject><subject>Centrifugation</subject><subject>Conserved Sequence</subject><subject>Cytoplasm - metabolism</subject><subject>Cytoplasm - ultrastructure</subject><subject>Fluorescence</subject><subject>Green Fluorescent Proteins</subject><subject>GTP-Binding Protein gamma Subunits - genetics</subject><subject>GTP-Binding Protein gamma Subunits - isolation & purification</subject><subject>GTP-Binding Protein gamma Subunits - metabolism</subject><subject>Humans</subject><subject>Lipid Metabolism - physiology</subject><subject>Lipids</subject><subject>Lipodystrophy</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - isolation & purification</subject><subject>Membrane Proteins - metabolism</subject><subject>Metabolism</subject><subject>Mice</subject><subject>Microscopy</subject><subject>Microscopy, Electron, Transmission</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Organelles - metabolism</subject><subject>Organelles - ultrastructure</subject><subject>Phospholipids</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae - ultrastructure</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - isolation & purification</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Steepest descent method</subject><subject>Yeast</subject><subject>Yeasts</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUuPFCEURitG47SjS5cqceFqarxAUcDGxEwcNZnEhc7OhNA8uulQRQlVJuOvl7Y77WPjisU5fHDv1zRPMVxiEPT1zqwvCQDHGNP-XrPCrINW4A7uNysAglvJCDtrHpWyA4COd_Rhc4YFYUAAr5qv19Hi6QJp5JfRzCGNOqJtGlJMm8Wh5NF2GfSIigtTGC9Qdpsl6tkVNG8dKuHHLydWaJHNaYpuLiiM6M7pMj9uHngdi3tyPM-b2-t3X64-tDef3n-8envTGsbY3GIwve29BS_Bar022ntCJeNMeiu8l4JhIsEJAUR0xoOVhhChLeWdEBTT8-bNIXda1oOzxo1z1lFNOQw636mkg_qbjGGrNum7IoR2hPQ14NUxIKdviyuzGkIxLkY9urQUxevDVAL_r0hAdJyzvfjyH3GXllyXWx3MMXDZd1VqD5LJqZTs_OnLGNS-XVXbVad2q__8zzl_28c6q_DsIOzKnPKJk9o744JU_uLAvU5Kb3Io6vbz_iKAYLKul_4E7ZSy6Q</recordid><startdate>20080211</startdate><enddate>20080211</enddate><creator>Fei, Weihua</creator><creator>Shui, Guanghou</creator><creator>Gaeta, Bruno</creator><creator>Du, Ximing</creator><creator>Kuerschner, Lars</creator><creator>Li, Peng</creator><creator>Brown, Andrew J</creator><creator>Wenk, Markus R</creator><creator>Parton, Robert G</creator><creator>Yang, Hongyuan</creator><general>The Rockefeller University Press</general><general>Rockefeller University Press</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20080211</creationdate><title>Fld1p, a functional homologue of human seipin, regulates the size of lipid droplets in yeast</title><author>Fei, Weihua ; 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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.</abstract><cop>United States</cop><pub>The Rockefeller University Press</pub><pmid>18250201</pmid><doi>10.1083/jcb.200711136</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Amino acids Animals Cell growth Cells Cellular biology Centrifugation Conserved Sequence Cytoplasm - metabolism Cytoplasm - ultrastructure Fluorescence Green Fluorescent Proteins GTP-Binding Protein gamma Subunits - genetics GTP-Binding Protein gamma Subunits - isolation & purification GTP-Binding Protein gamma Subunits - metabolism Humans Lipid Metabolism - physiology Lipids Lipodystrophy Membrane Proteins - genetics Membrane Proteins - isolation & purification Membrane Proteins - metabolism Metabolism Mice Microscopy Microscopy, Electron, Transmission Molecular Sequence Data Mutation Organelles - metabolism Organelles - ultrastructure Phospholipids Saccharomyces cerevisiae Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae - ultrastructure Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - isolation & purification Saccharomyces cerevisiae Proteins - metabolism Sequence Homology, Amino Acid Steepest descent method Yeast Yeasts |
| title | Fld1p, a functional homologue of human seipin, regulates the size of lipid droplets in yeast |
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