Homology of SMP Domains to the TULIP Superfamily of Lipid-Binding Proteins Provides a Structural Basis for Lipid Exchange between ER and Mitochondria
Open accessAbstract
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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Mdm12, Mdm34, and Mmm1 have synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domains, and the ERMES complex mediates lipid transport.
“Mdm12, Mdm34, and Mmm1 have synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domains [24], and the ERMES complex mediates lipid transport [25,26].”
From In Candida glabrata, ERMES Component GEM1 Controls Mitochondrial Morphology, mtROS, and Drug Efflux Pump Expression, Resulting in Azole Susceptibility (2023) · cites this paper as [24]
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Cites
Basic local alignment search tool
Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669 · see citing works
Murzin, A. G., Brenner, S. E., Hubbard, T., & Chothia, C. (1995) · Journal of Molecular Biology · doi:10.1016/s0022-2836(05)80134-2 · Cited by 6,412 · see citing works
I-TASSER: a unified platform for automated protein structure and function prediction
Roy, A., Küçükural, A., & Zhang, Y. (2010) · Nature Protocols · doi:10.1038/nprot.2010.5 · Cited by 6,093 · see citing works
Protein structure prediction on the Web: a case study using the Phyre server
Kelley, L. A., & Sternberg, M. J. E. (2009) · Nature Protocols · doi:10.1038/nprot.2009.2 · Cited by 4,154 · see citing works
The HHpred interactive server for protein homology detection and structure prediction
Söding, J., Biegert, A., & Lupas, A. N. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki408 · Cited by 3,703 · see citing works
Self-citationMitochondria: More Than Just a Powerhouse
McBride, H. M., Neuspiel, M., & Wasiak, S. (2006) · Current Biology · doi:10.1016/j.cub.2006.06.054 · Cited by 1,985 · see citing works
An ER-Mitochondria Tethering Complex Revealed by a Synthetic Biology Screen
Kornmann, B., Currie, E., Collins, S. R., Schuldiner, M., Nunnari, J., Weissman, J. S., & Walter, P. (2009) · Science · doi:10.1126/science.1175088 · Cited by 1,275 · see citing works
Mitochondrial Morphology and Dynamics in Yeast and Multicellular Eukaryotes
Okamoto, K., & Shaw, J. M. (2005) · Annual Review of Genetics · doi:10.1146/annurev.genet.38.072902.093019 · Cited by 737 · see citing works
CLANS: a Java application for visualizing protein families based on pairwise similarity
Frickey, T., & Lupas, A. N. (2004) · Bioinformatics · doi:10.1093/bioinformatics/bth444 · Cited by 721 · see citing works
Self-citationTemplate-based modeling and free modeling by I-TASSER in CASP7
Zhang, Y. (2007) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21702 · Cited by 467 · see citing works
I‐TASSER: Fully automated protein structure prediction in CASP8
Zhang, Y. (2009) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22588 · Cited by 420 · see citing works
Wu, S., & Zhang, Y. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21945 · Cited by 375 · see citing works
Maturation of cellular Fe–S proteins: an essential function of mitochondria
Lill, R., & Kispal, G. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01589-9 · Cited by 358 · see citing works
Crystal Structure of Human BPI and Two Bound Phospholipids at 2.4 Angstrom Resolution
Beamer, L. J., Carroll, S. F., & Eisenberg, D. S. (1997) · Science · doi:10.1126/science.276.5320.1861 · Cited by 357 · see citing works
Maturation of cellular Fe-S proteins: an essential function of mitochondria
Gray, H. B. (2000) · Cited by 307 · see citing works
Achleitner, G., Gaigg, B., Krasser, A., Kainersdorfer, E., Kohlwein, S. D., Perktold, A., Zellnig, G., & Daum, G. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00658.x · Cited by 300 · see citing works
Qiu, X., Mistry, A., Ammirati, M. J., Chrunyk, B. A., Clark, R. W., Cong, Y., Culp, J. S., Danley, D. E., Freeman, T. B., Geoghegan, K. F., et al. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1197 · Cited by 275 · see citing works
The MPI Bioinformatics Toolkit for protein sequence analysis
Biegert, A., Mayer, C., Remmert, M., et al. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl217 · Cited by 274 · see citing works
Meisinger, C., Rissler, M., Chacińska, A., Szklarz, L. K. S., Milenkovic, D., Kozjak‐Pavlovic, V., Schönfisch, B., Lohaus, C., Meyer, H. E., Yaffe, M. P., et al. (2004) · Developmental Cell · doi:10.1016/j.devcel.2004.06.003 · Cited by 268 · see citing works
Youngman, M. J., Hobbs, A. E. A., Burgess, S. M., Srinivasan, M., & Jensen, R. E. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200308012 · Cited by 148 · see citing works
A new progressive-iterative algorithm for multiple structure alignment
Lupyan, D., Leo‐Macías, A., & Ortíz, Á. R. (2005) · Bioinformatics · doi:10.1093/bioinformatics/bti527 · Cited by 145 · see citing works
The Structure of the Dust Mite Allergen Der p 7 Reveals Similarities to Innate Immune Proteins
Mueller, G., Edwards, L. L., Aloor, J., Fessler, M., Glesner, J., Pomés, A., Chapman, M., London, R., & Pedersen, L. (2010) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2009.12.016 · Cited by 112 · see citing works
Wang, Z., Eickholt, J., & Cheng, J. J. (2010) · Bioinformatics · doi:10.1093/bioinformatics/btq058 · Cited by 97 · see citing works
New perspectives on the regulation of intermembrane glycerophospholipid traffic
Voelker, D. R. (2003) · Journal of Lipid Research · doi:10.1194/jlr.r200020-jlr200 · Cited by 96 · see citing works
Diverse membrane‐associated proteins contain a novel SMP domain
Lee, I., & Hong, W. (2006) · The FASEB Journal · doi:10.1096/fj.05-4581hyp · Cited by 89 · see citing works
HHsenser: exhaustive transitive profile search using HMM-HMM comparison
Söding, J., Remmert, M., Biegert, A., & Lupas, A. N. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl195 · Cited by 88 · see citing works
Self-citationCorrelation of observed fold frequency with the occurrence of local structural motifs
Salem, G. M., Hutchinson, E. G., Orengo, C. A., & Thornton, J. M. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2642 · Cited by 81 · see citing works
Insect Juvenile Hormone Binding Protein Shows Ancestral Fold Present in Human Lipid-Binding Proteins
Kolodziejczyk, R., Bujacz, G., Jakób, M., Ożyhar, A., Jaskólski, M., & Kochman, M. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.01.026 · Cited by 62 · see citing works
Hamiaux, C., Stanley, D., Greenwood, D. R., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807467200 · Cited by 54 · see citing works
Kleiger, G., Beamer, L. J., Grothe, R., et al. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3805 · Cited by 48 · see citing works
MALISAM: a database of structurally analogous motifs in proteins
Cheng, H., Kim, B., & Grishin, N. V. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm698 · Cited by 47 · see citing works
Structurally Analogous Proteins Do Exist!
Krishna, S., & Grishin, N. V. (2004) · Structure · doi:10.1016/j.str.2004.06.004 · Cited by 42 · see citing works
Protein structure prediction center in CASP8
Kryshtafovych, A., Krysko, O., Daniluk, P., et al. (2009) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22517 · Cited by 38 · see citing works
Bioinformatic insights to the ESAG5 and GRESAG5 gene families in kinetoplastid parasites
Barker, A., Wickstead, B., Gluenz, E., & Keith Gull, B. (2008) · Molecular and Biochemical Parasitology · doi:10.1016/j.molbiopara.2008.08.003 · Cited by 14 · see citing works
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Rowland, A. A., & Voeltz, G. K. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3440 · Cited by 1,018 · see citing works
Endoplasmic reticulum-mitochondrial contactology: structure and signaling functions
Csordás, G., Weaver, D., & Hajnóczky, G. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.02.009 · Cited by 625 · see citing works
Organization and Function of Membrane Contact Sites
Helle, S. C. J., Kanfer, G., Kolar, K., Lang, A., Michel, A. H., & Kornmann, B. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.01.028 · Cited by 453 · see citing works
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Kornmann, B., Osman, C., & Walter, P. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1111314108 · Cited by 335 · see citing works
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Elbaz, Y., & Schuldiner, M. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.08.004 · Cited by 226 · see citing works
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Kawano, S., Tamura, Y., Kojima, R., Bala, S., Asai, E., Michel, A. H., Kornmann, B., Riezman, I., Riezman, H., Sakae, Y., et al. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201704119 · Cited by 148 · see citing works
Dagley, M. J., Gentle, I. E., Beilharz, T. H., Pettolino, F. A., Djordjevic, J. T., Lo, T. L., Uwamahoro, N., Rupasinghe, T., Tull, D. L., McConville, M., et al. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07503.x · Cited by 128 · see citing works
Okamoto, M., Nakano, K., Takahashi-Nakaguchi, A., Sasamoto, K., Yamaguchi, M., Teixeira, M. C., & Chibana, H. (2023) · Journal of Fungi · doi:10.3390/jof9020240 · Cited by 11 · see citing works
“Mdm12, Mdm34, and Mmm1 have synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domains [24], and the ERMES complex mediates lipid transport [25,26].”
Background
- Authors
- Kopec, K. O., Alva, V., & Lupas, A. N.
- Affiliations
- Max Planck Institute for Developmental Biology (DE)
- Corresponding author
- Lupas, Andrei N.
- Venue
- Bioinformatics
- Publisher
- Oxford University Press (OUP)
- Published
- 2010-06-16
- Volume
- 26
- Issue
- 16
- Pages
- 1927-1931
- ISSN
- 1367-4803 (ISSN-L)
- 1367-4811
- PMC
- PMC2916718
- 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
- hybrid
- doi.org
- Licence
- 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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