CG32803 is the fly homolog of LDAF1 and influences lipid storage in vivo
The Seipin protein is a conserved key component in the biogenesis of lipid droplets (LDs). Recently, a cooperation between human Seipin and the Lipid droplet assembly factor 1 (LDAF1) was described. LDAF1 physically interacts with Seipin and the holocomplex safeguards regular LD biogenesis. The func...
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Veröffentlicht in: | Insect biochemistry and molecular biology 2021-06, Vol.133, p.103512-103512, Article 103512 |
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creator | Chartschenko, Eugenia Hugenroth, Marie Akhtar, Irfan Droste, Andrea Kolkhof, Petra Bohnert, Maria Beller, Mathias |
description | The Seipin protein is a conserved key component in the biogenesis of lipid droplets (LDs). Recently, a cooperation between human Seipin and the Lipid droplet assembly factor 1 (LDAF1) was described. LDAF1 physically interacts with Seipin and the holocomplex safeguards regular LD biogenesis. The function of LDAF1 proteins outside mammals is less clear. In yeast, the lipid droplet organization (LDO) proteins, which also cooperate with Seipin, are the putative homologs of LDAF1. While certain functional aspects are shared between the LDO and mammalian LDAF1 proteins, the relationship between the proteins is under debate. Here, we identify the Drosophila melanogaster protein CG32803, which we re-named to dmLDAF1, as an insect member of this protein family. dmLDAF1 decorates LDs in cultured cells and in vivo and the protein is linked to the fly and mouse Seipin proteins. Altering the dmLDAF1 abundance affects LD size, number and overall lipid storage amounts. Our results suggest that the LDAF1 proteins thus fulfill an evolutionarily conserved function in the biogenesis and biology of LDs.
[Display omitted]
•CG32803 is the fly LDAF1 homolog.•LDAF1 proteins are evolutionarily conserved regulators of lipid droplet biogenesis.•Drosophila LDAF1 interacts with Seipin.•Overexpression and knock-down of Drosophila LDAF1 influence lipid storage in vivo. |
doi_str_mv | 10.1016/j.ibmb.2020.103512 |
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[Display omitted]
•CG32803 is the fly LDAF1 homolog.•LDAF1 proteins are evolutionarily conserved regulators of lipid droplet biogenesis.•Drosophila LDAF1 interacts with Seipin.•Overexpression and knock-down of Drosophila LDAF1 influence lipid storage in vivo.</description><identifier>ISSN: 0965-1748</identifier><identifier>EISSN: 1879-0240</identifier><identifier>DOI: 10.1016/j.ibmb.2020.103512</identifier><identifier>PMID: 33307187</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Drosophila ; LDAF1 ; Ldo16 ; Ldo45 ; lipid droplet biogenesis ; Lipid droplets ; Lipid metabolism ; lipid storage ; Promethin ; Seipin ; TMEM159</subject><ispartof>Insect biochemistry and molecular biology, 2021-06, Vol.133, p.103512-103512, Article 103512</ispartof><rights>2020 Elsevier Ltd</rights><rights>Copyright © 2020 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c356t-105e60964fd253e191aac7f3b283856c2a26cce6be5b080eab9472f18f4a82653</citedby><cites>FETCH-LOGICAL-c356t-105e60964fd253e191aac7f3b283856c2a26cce6be5b080eab9472f18f4a82653</cites><orcidid>0000-0002-8154-555X ; 0000-0002-4678-4280 ; 0000-0003-2499-7274 ; 0000-0003-0987-0080</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.ibmb.2020.103512$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33307187$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chartschenko, Eugenia</creatorcontrib><creatorcontrib>Hugenroth, Marie</creatorcontrib><creatorcontrib>Akhtar, Irfan</creatorcontrib><creatorcontrib>Droste, Andrea</creatorcontrib><creatorcontrib>Kolkhof, Petra</creatorcontrib><creatorcontrib>Bohnert, Maria</creatorcontrib><creatorcontrib>Beller, Mathias</creatorcontrib><title>CG32803 is the fly homolog of LDAF1 and influences lipid storage in vivo</title><title>Insect biochemistry and molecular biology</title><addtitle>Insect Biochem Mol Biol</addtitle><description>The Seipin protein is a conserved key component in the biogenesis of lipid droplets (LDs). Recently, a cooperation between human Seipin and the Lipid droplet assembly factor 1 (LDAF1) was described. LDAF1 physically interacts with Seipin and the holocomplex safeguards regular LD biogenesis. The function of LDAF1 proteins outside mammals is less clear. In yeast, the lipid droplet organization (LDO) proteins, which also cooperate with Seipin, are the putative homologs of LDAF1. While certain functional aspects are shared between the LDO and mammalian LDAF1 proteins, the relationship between the proteins is under debate. Here, we identify the Drosophila melanogaster protein CG32803, which we re-named to dmLDAF1, as an insect member of this protein family. dmLDAF1 decorates LDs in cultured cells and in vivo and the protein is linked to the fly and mouse Seipin proteins. Altering the dmLDAF1 abundance affects LD size, number and overall lipid storage amounts. Our results suggest that the LDAF1 proteins thus fulfill an evolutionarily conserved function in the biogenesis and biology of LDs.
[Display omitted]
•CG32803 is the fly LDAF1 homolog.•LDAF1 proteins are evolutionarily conserved regulators of lipid droplet biogenesis.•Drosophila LDAF1 interacts with Seipin.•Overexpression and knock-down of Drosophila LDAF1 influence lipid storage in vivo.</description><subject>Drosophila</subject><subject>LDAF1</subject><subject>Ldo16</subject><subject>Ldo45</subject><subject>lipid droplet biogenesis</subject><subject>Lipid droplets</subject><subject>Lipid metabolism</subject><subject>lipid storage</subject><subject>Promethin</subject><subject>Seipin</subject><subject>TMEM159</subject><issn>0965-1748</issn><issn>1879-0240</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><recordid>eNp9kE1Lw0AQhhdRbK3-AQ-yRy-p-50UvEi1rVDwoudls5lttyTZmk0L_fcmpHr0NDDzzMvMg9A9JVNKqHraTX1e5VNGWN_gkrILNKZZOksIE-QSjclMyYSmIhuhmxh3hBAhZHqNRpxzknbkGK3mS84ywrGPuN0CduUJb0MVyrDBweH168uCYlMX2NeuPEBtIeLS732BYxsas4FugI_-GG7RlTNlhLtznaCvxdvnfJWsP5bv85d1YrlUbUKJBNXdJVzBJAc6o8bY1PGcZTyTyjLDlLWgcpA5yQiYfCZS5mjmhMmYknyCHofcfRO-DxBbXflooSxNDeEQNRMpF4wpJTqUDahtQowNOL1vfGWak6ZE9wb1TvcGdW9QDwa7pYdz_iGvoPhb-VXWAc8DAN2XRw-Njtb3YgrfgG11Efx_-T_hSX5r</recordid><startdate>20210601</startdate><enddate>20210601</enddate><creator>Chartschenko, Eugenia</creator><creator>Hugenroth, Marie</creator><creator>Akhtar, Irfan</creator><creator>Droste, Andrea</creator><creator>Kolkhof, Petra</creator><creator>Bohnert, Maria</creator><creator>Beller, Mathias</creator><general>Elsevier Ltd</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-8154-555X</orcidid><orcidid>https://orcid.org/0000-0002-4678-4280</orcidid><orcidid>https://orcid.org/0000-0003-2499-7274</orcidid><orcidid>https://orcid.org/0000-0003-0987-0080</orcidid></search><sort><creationdate>20210601</creationdate><title>CG32803 is the fly homolog of LDAF1 and influences lipid storage in vivo</title><author>Chartschenko, Eugenia ; Hugenroth, Marie ; Akhtar, Irfan ; Droste, Andrea ; Kolkhof, Petra ; Bohnert, Maria ; Beller, Mathias</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c356t-105e60964fd253e191aac7f3b283856c2a26cce6be5b080eab9472f18f4a82653</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Drosophila</topic><topic>LDAF1</topic><topic>Ldo16</topic><topic>Ldo45</topic><topic>lipid droplet biogenesis</topic><topic>Lipid droplets</topic><topic>Lipid metabolism</topic><topic>lipid storage</topic><topic>Promethin</topic><topic>Seipin</topic><topic>TMEM159</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chartschenko, Eugenia</creatorcontrib><creatorcontrib>Hugenroth, Marie</creatorcontrib><creatorcontrib>Akhtar, Irfan</creatorcontrib><creatorcontrib>Droste, Andrea</creatorcontrib><creatorcontrib>Kolkhof, Petra</creatorcontrib><creatorcontrib>Bohnert, Maria</creatorcontrib><creatorcontrib>Beller, Mathias</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Insect biochemistry and molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chartschenko, Eugenia</au><au>Hugenroth, Marie</au><au>Akhtar, Irfan</au><au>Droste, Andrea</au><au>Kolkhof, Petra</au><au>Bohnert, Maria</au><au>Beller, Mathias</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>CG32803 is the fly homolog of LDAF1 and influences lipid storage in vivo</atitle><jtitle>Insect biochemistry and molecular biology</jtitle><addtitle>Insect Biochem Mol Biol</addtitle><date>2021-06-01</date><risdate>2021</risdate><volume>133</volume><spage>103512</spage><epage>103512</epage><pages>103512-103512</pages><artnum>103512</artnum><issn>0965-1748</issn><eissn>1879-0240</eissn><abstract>The Seipin protein is a conserved key component in the biogenesis of lipid droplets (LDs). Recently, a cooperation between human Seipin and the Lipid droplet assembly factor 1 (LDAF1) was described. LDAF1 physically interacts with Seipin and the holocomplex safeguards regular LD biogenesis. The function of LDAF1 proteins outside mammals is less clear. In yeast, the lipid droplet organization (LDO) proteins, which also cooperate with Seipin, are the putative homologs of LDAF1. While certain functional aspects are shared between the LDO and mammalian LDAF1 proteins, the relationship between the proteins is under debate. Here, we identify the Drosophila melanogaster protein CG32803, which we re-named to dmLDAF1, as an insect member of this protein family. dmLDAF1 decorates LDs in cultured cells and in vivo and the protein is linked to the fly and mouse Seipin proteins. Altering the dmLDAF1 abundance affects LD size, number and overall lipid storage amounts. Our results suggest that the LDAF1 proteins thus fulfill an evolutionarily conserved function in the biogenesis and biology of LDs.
[Display omitted]
•CG32803 is the fly LDAF1 homolog.•LDAF1 proteins are evolutionarily conserved regulators of lipid droplet biogenesis.•Drosophila LDAF1 interacts with Seipin.•Overexpression and knock-down of Drosophila LDAF1 influence lipid storage in vivo.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>33307187</pmid><doi>10.1016/j.ibmb.2020.103512</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0002-8154-555X</orcidid><orcidid>https://orcid.org/0000-0002-4678-4280</orcidid><orcidid>https://orcid.org/0000-0003-2499-7274</orcidid><orcidid>https://orcid.org/0000-0003-0987-0080</orcidid></addata></record> |
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subjects | Drosophila LDAF1 Ldo16 Ldo45 lipid droplet biogenesis Lipid droplets Lipid metabolism lipid storage Promethin Seipin TMEM159 |
title | CG32803 is the fly homolog of LDAF1 and influences lipid storage in vivo |
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