ArticleEMBO reports2016
Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex.
Article in EMBO reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers, 1 of them a synthesis that pooled it.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
47 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Inter-organellar Communication in Parkinson's and Alzheimer's Disease: Looking Beyond Endoplasmic Reticulum-Mitochondria Contact Sites.Frontiers in neuroscience · 2022Pooled it
- Mitochondrially tethered Mmm1 can function as a sole lipid transporter at ER-mitochondria contacts.The Journal of cell biology · 2026Article
- Yeast mitochondrial adaptation to freeze thaw stress depends on pre freeze fermentation state.NPJ science of food · 2026Article
- The conformational plasticity of structurally unrelated lipid transport proteins correlates with their mode of action.PLoS biology · 2024Article
- The ER-SURF pathway uses ER-mitochondria contact sites for protein targeting to mitochondria.EMBO reports · 2024Article
- Chemical inhibition of phosphatidylcholine biogenesis reveals its role in mitochondrial division.iScience · 2024Article
- The divergent ER-mitochondria encounter structures (ERMES) are conserved in parabasalids but lost in several anaerobic lineages with hydrogenosomes.BMC biology · 2023Article
- Convergent and divergent mechanisms of peroxisomal and mitochondrial division.The Journal of cell biology · 2023Article
- Article
- In silico modeling human VPS13 proteins associated with donor and target membranes suggests lipid transfer mechanisms.Proteins · 2023Article
- Insights into membrane association of the SMP domain of extended synaptotagmin.Nature communications · 2023Article
- Dissociation of ERMES clusters plays a key role in attenuating the endoplasmic reticulum stress.iScience · 2022Article
- Lipid Transport from Endoplasmic Reticulum to Autophagic Membranes.Cold Spring Harbor perspectives in biology · 2022Review
- Structural basis for mitoguardin-2 mediated lipid transport at ER-mitochondrial membrane contact sites.Nature communications · 2022Article
- Rewiring phospholipid biosynthesis reveals resilience to membrane perturbations and uncovers regulators of lipid homeostasis.The EMBO journal · 2022Article
- Phospholipid transfer function of PTPIP51 at mitochondria-associated ER membranes.EMBO reports · 2021Article
- Emr1 regulates the number of foci of the endoplasmic reticulum-mitochondria encounter structure complex.Nature communications · 2021Article
- Leri: A web-server for identifying protein functional networks from evolutionary couplings.Computational and structural biotechnology journal · 2021Article
- Molecular machineries and physiological relevance of ER-mediated membrane contacts.Theranostics · 2021Article
- Endoplasmic Reticulum-Mitochondria Contact Sites-Emerging Intracellular Signaling Hubs.Frontiers in cell and developmental biology · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The endoplasmic reticulum-mitochondria encounter structure (ERMES) is a protein complex that plays a tethering role in physically connecting ER and mitochondria membranes. The ERMES complex is composed of Mdm12, Mmm1, and Mdm34, which have a SMP domain in common, and Mdm10. Here, we report the crystal structure of S. cerevisiae Mdm12. The Mdm12 forms a dimeric SMP structure through domain swapping of the β1-strand comprising residues 1-7. Biochemical experiments reveal a phospholipid-binding site located along a hydrophobic channel of the Mdm12 structure and that Mdm12 might have a binding preference for glycerophospholipids harboring a positively charged head group. Strikingly, both full-length Mdm12 and Mdm12 truncated to exclude the disordered region (residues 74-114) display the same organization in the asymmetric unit, although they crystallize as a tetramer and hexamer, respectively. Taken together, these studies provide a novel understanding of the overall organization of SMP domains in the ERMES complex, indicating that Mdm12 interacts with Mdm34 through head-to-head contact, and with Mmm1 through tail-to-tail contact of SMP domains.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.