{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,8]],"date-time":"2026-01-08T23:00:57Z","timestamp":1767913257557,"version":"3.49.0"},"reference-count":33,"publisher":"Oxford University Press (OUP)","issue":"16","license":[{"start":{"date-parts":[[2016,10,2]],"date-time":"2016-10-02T00:00:00Z","timestamp":1475366400000},"content-version":"vor","delay-in-days":2300,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/2.5"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2010,8,15]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Mitochondria must uptake some phospholipids from the endoplasmic reticulum (ER) for the biogenesis of their membranes. They convert one of these lipids, phosphatidylserine, to phosphatidylethanolamine, which can be re-exported via the ER to all other cellular membranes. The mechanisms underlying these exchanges between ER and mitochondria are poorly understood. Recently, a complex termed ER\u2013mitochondria encounter structure (ERMES) was shown to be necessary for phospholipid exchange in budding yeast. However, it is unclear whether this complex is merely an inter-organelle tether or also the transporter. ERMES consists of four proteins: Mdm10, Mdm34 (Mmm2), Mdm12 and Mmm1, three of which contain the uncharacterized SMP domain common to a number of eukaryotic membrane-associated proteins. Here, we show that the SMP domain belongs to the TULIP superfamily of lipid\/hydrophobic ligand-binding domains comprising members of known structure. This relationship suggests that the SMP domains of the ERMES complex mediate lipid exchange between ER and mitochondria.<\/jats:p>\n               <jats:p>Contact: \u00a0andrei.lupas@tuebingen.mpg.de<\/jats:p>\n               <jats:p>Supplementary information: \u00a0Supplementary data are available at Bioinformatics online.<\/jats:p>","DOI":"10.1093\/bioinformatics\/btq326","type":"journal-article","created":{"date-parts":[[2010,6,17]],"date-time":"2010-06-17T01:00:02Z","timestamp":1276736402000},"page":"1927-1931","source":"Crossref","is-referenced-by-count":193,"title":["Homology of SMP domains to the TULIP superfamily of lipid-binding proteins provides a structural basis for lipid exchange between ER and mitochondria"],"prefix":"10.1093","volume":"26","author":[{"given":"Klaus O.","family":"Kopec","sequence":"first","affiliation":[{"name":"Department of Protein Evolution, Max-Planck-Institute for Developmental Biology, Spemannstr. 35, 72076 T\u00fcbingen, Germany"}]},{"given":"Vikram","family":"Alva","sequence":"additional","affiliation":[{"name":"Department of Protein Evolution, Max-Planck-Institute for Developmental Biology, Spemannstr. 35, 72076 T\u00fcbingen, Germany"}]},{"given":"Andrei N.","family":"Lupas","sequence":"additional","affiliation":[{"name":"Department of Protein Evolution, Max-Planck-Institute for Developmental Biology, Spemannstr. 35, 72076 T\u00fcbingen, Germany"}]}],"member":"286","published-online":{"date-parts":[[2010,6,16]]},"reference":[{"key":"2023012508020904000_B1","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1046\/j.1432-1327.1999.00658.x","article-title":"Association between the endoplasmic reticulum and mitochondria of yeast facilitates interorganelle transport of phospholipids through membrane contact","volume":"264","author":"Achleitner","year":"1999","journal-title":"Eur. 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