دورية أكاديمية
Homology of SMP domains to the TULIP superfamily of lipid-binding proteins provides a structural basis for lipid exchange between ER and mitochondria.
| العنوان: | Homology of SMP domains to the TULIP superfamily of lipid-binding proteins provides a structural basis for lipid exchange between ER and mitochondria. |
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| المؤلفون: | Kopec KO; Department of Protein Evolution, Max-Planck-Institute for Developmental Biology, Tübingen, Germany., Alva V, Lupas AN |
| المصدر: | Bioinformatics (Oxford, England) [Bioinformatics] 2010 Aug 15; Vol. 26 (16), pp. 1927-31. Date of Electronic Publication: 2010 Jun 16. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Oxford University Press Country of Publication: England NLM ID: 9808944 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1367-4811 (Electronic) Linking ISSN: 13674803 NLM ISO Abbreviation: Bioinformatics Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Oxford : Oxford University Press, c1998- |
| مواضيع طبية MeSH: | Carrier Proteins/*chemistry , Endoplasmic Reticulum/*metabolism , Mitochondria/*metabolism , Mitochondrial Proteins/*chemistry , Phospholipids/*metabolism, Amino Acid Sequence ; Animals ; Biological Transport ; Carrier Proteins/classification ; Carrier Proteins/metabolism ; Membrane Proteins/chemistry ; Membrane Proteins/classification ; Membrane Proteins/metabolism ; Mitochondrial Proteins/classification ; Mitochondrial Proteins/metabolism ; Molecular Sequence Data |
| مستخلص: | 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-mitochondria 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. |
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| المشرفين على المادة: | 0 (Carrier Proteins) 0 (Membrane Proteins) 0 (Mitochondrial Proteins) 0 (Phospholipids) |
| تواريخ الأحداث: | Date Created: 20100618 Date Completed: 20101007 Latest Revision: 20211020 |
| رمز التحديث: | 20240628 |
| مُعرف محوري في PubMed: | PMC2916718 |
| DOI: | 10.1093/bioinformatics/btq326 |
| PMID: | 20554689 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 1367-4811 |
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| DOI: | 10.1093/bioinformatics/btq326 |