Cited by 212Mitochondrial Function and PathologyLipid Membrane Structure and BehaviorCellular transport and secretion

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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Kopec, Klaus O., Alva, Vikram, Lupas, Andrei N.·2010·Bioinformatics

Abstract

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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Authors
Kopec, K. O., Alva, V., & Lupas, A. N.
Affiliations
Max Planck Institute for Developmental Biology (DE)
Corresponding author
Lupas, Andrei N.
Venue
Bioinformatics
Published
2010-06-16
Volume
26
Issue
16
Pages
1927-1931
ISSN
  • 1367-4803 (ISSN-L)
  • 1367-4811
OpenAlex
W2125735360
Cited by
212
References
34
Citations by year
2026: 3 · 2025: 2 · 2024: 11 · 2023: 10 · 2022: 8 · 2021: 12 · 2020: 11 · 2019: 19 · 2018: 12 · 2017: 29 · 2016: 28 · 2015: 13 · 2014: 15 · 2013: 18 · 2012: 9
FWCI
5.04
Type
journal article
Language
en
Open access
Locations
  • Bioinformatics (publishedVersion, cc-by-nc)
  • PubMed Central (publishedVersion, cc-by-nc)
  • PubMed (publishedVersion)
  • Max Planck Institute for Plasma Physics (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords
lipid-binding proteins, ERMES complex, phospholipid exchange, membrane protein structure
MeSH terms
Amino Acid Sequence, Animals, Biological Transport, Carrier Proteins, Endoplasmic Reticulum, Membrane Proteins, Mitochondria, Molecular Sequence Data, Phospholipids, Mitochondrial Proteins

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