Ask about this productRelated genes to: MDM1 antibody
- Gene:
- MDM1 NIH gene
- Name:
- Mdm1 nuclear protein
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 12q15
- Locus Type:
- gene with protein product
- Date approved:
- 2004-12-20
- Date modifiied:
- 2015-06-19
Related products to: MDM1 antibody
Related articles to: MDM1 antibody
- Membrane contact sites are organized by protein assemblies that physically couple organelles and coordinate lipid metabolism, yet the structural principles that enable lipid exchange across these junctions remain poorly defined. At the nuclear-vacuolar junction (NVJ) in budding yeast, the tethering protein Mdm1 and its binding partner Nvj3 form a complex that regulates lipid metabolic pathways, but the structural features underlying their interaction have not been resolved. Here, we use AlphaFold-based complex prediction and comparative structural analysis to define the organization of Nvj3-Mdm1 complex assembly. We identify a high-confidence heterodimer in which conserved PXA and PXC domains generate an extended tunnel spanning both proteins. Tunnel analysis predicts a core hydrophobic conduit traversing the Nvj3-Mdm1 interface, consistent with a lipid-compatible architecture. Evolutionary conservation is enriched at the Nvj3-Mdm1 interface. The predicted conduit shares geometric and physicochemical properties with bridge-like lipid transfer proteins, including Atg2, Fmp27, and Hob2, suggesting that heteromeric tether assemblies may contribute directly to inter-organelle lipid transfer. Notably, this conduit is predicted to arise from a heteromeric α-helical assembly rather than the β-sheet-rich architecture characteristic of canonical bridge-like lipid transfer proteins. Comparative phylogenetic analyses showed that Nvj3 and Mdm1 share broadly congruent evolutionary patterns across Saccharomycetes, consistent with their conserved functional association. Together, these findings define Nvj3 as a structural partner of Mdm1 and support a conduit-based model of lipid transfer at the NVJ. - Source: PubMed
Publication date: 2026/07/24
Aboumourad MarwaHariri Hanaa - Membrane contact sites are organized by protein assemblies that physically couple organelles and coordinate lipid metabolism, yet the structural principles that enable lipid exchange across these junctions remain poorly defined. At the nuclear-vacuolar junction (NVJ) in budding yeast, the tethering protein Mdm1 and its binding partner Nvj3 form a complex that regulates lipid metabolic pathways, but the structural features underlying their interaction have not been resolved. Here, we use AlphaFold-based complex prediction and comparative structural analysis to define the organization of Nvj3-Mdm1 complex assembly. We identify a high-confidence heterodimer in which conserved PXA and PXC domains generate an extended tunnel spanning both proteins. Tunnel analysis predicts a core hydrophobic conduit traversing the Nvj3-Mdm1 interface, consistent with a lipid-compatible architecture. Evolutionary conservation is enriched at the Nvj3-Mdm1 interface. The predicted conduit shares geometric and physicochemical properties with bridge-like lipid transfer proteins, including Atg2, Fmp27, and Hob2, suggesting that heteromeric tether assemblies may contribute directly to inter-organelle lipid transfer. Notably, this conduit is predicted to arise from a heteromeric α-helical assembly rather than the β-sheet-rich architecture characteristic of canonical bridge-like lipid transfer proteins. Comparative phylogenetic analyses showed that Nvj3 and Mdm1 share broadly congruent evolutionary patterns across Saccharomycetes, consistent with their conserved functional association. Together, these findings define Nvj3 as a structural partner of Mdm1 and support a conduit-based model of lipid transfer at the NVJ. - Source: PubMed
Publication date: 2026/07/03
Aboumourad MarwaHariri Hanaa - Membrane lipid composition influences endocytic remodeling of nutrient transporters, yet how lipid metabolism is spatially coordinated to support sustained adaptation to nutrient limitations remains unclear. Here, we investigated whether the endoplasmic reticulum (ER)-vacuole tether Mdm1 links sphingolipid (SL) homeostasis to regulation of the high-affinity methionine permease Mup1 in budding yeast. To test this, we examined Mup1 trafficking, amino acid homeostasis, and SL composition in Δ cells during starvation. We found that loss of Mdm1 causes persistent retention of Mup1 at the plasma membrane (PM), accompanied by reduced intracellular methionine and broad amino acid depletion. Lipidomic analyses revealed decreased sphingoid bases and altered ceramide composition in Δ cells. Importantly, supplementation with the SL precursor phytosphingosine restored SL pools, rescued Mup1 endocytosis, and improved amino acid homeostasis. Consistent with a chronic amino acid restriction-like state, Δ cells exhibited extended chronological lifespan. Together, these findings support a model in which Mdm1 functions as a spatial organizer of SL metabolism, contributing to adaptive endocytic remodeling of Mup1, thereby linking ER-vacuole contact site function to PM proteostasis and metabolic adaptation. - Source: PubMed
Publication date: 2026/06/16
Adebayo DanielObaseki EseiwiVasudeva KashviAboumourad MarwaMiller ScottOstermeyer-Fay AnneCanals DanielBao XunLi JingHariri Hanaa - Membrane lipid composition influences endocytic remodeling of nutrient transporters, yet how lipid metabolism is spatially coordinated to support sustained adaptation to nutrient limitations remains unclear. Here, we investigated whether the ER-vacuole tether Mdm1 links sphingolipid homeostasis to regulation of the high-affinity methionine permease Mup1 in budding yeast. To test this, we examined Mup1 trafficking, amino acid homeostasis, and sphingolipid composition in Δ cells during starvation. We found that loss of Mdm1 causes persistent retention of Mup1 at the plasma membrane, accompanied by reduced intracellular methionine and broad amino acid depletion. Lipidomic analyses revealed decreased sphingoid bases and altered ceramide composition in Δ cells. Importantly, supplementation with the sphingolipid precursor phytosphingosine restored sphingolipid pools, rescued Mup1 endocytosis, and improved amino acid homeostasis. Consistent with a chronic amino acid restriction-like state, Δ cells exhibited extended chronological lifespan. Together, these findings identify Mdm1 as a spatial organizer of sphingolipid metabolism required for adaptive endocytic remodeling of Mup1, thereby linking ER-vacuole contact site function to plasma membrane proteostasis and metabolic adaptation. - Source: PubMed
Publication date: 2026/02/26
Adebayo DanielObaseki EseiwiVasudeva KashviAboumourad MarwaMiller ScottOstermeyer-Fay AnneCanals DanielBao XunLi JingHariri Hanaa - Over 500 genes have been linked to various forms of inherited retinal diseases (IRDs), a class of Mendelian conditions that affect the survival and function of rod and cone photoreceptors and, in most instances, lead to progressive visual loss. Yet some affected individuals still lack a clear genetic diagnosis, suggesting that more disease-associated genes remain to be discovered. Following the genetic analysis of extended cohorts of individuals diagnosed with late-onset recessive retinal dystrophy, we identified bi-allelic combinations of six predicted null variants in MDM1 (now renamed SAXO6, stabilizer of axonemal microtubules 6) in six subjects from five families. Iterative ultrastructure expansion microscopy coupled with immuno-gold transmission electron microscopy revealed co-localization of SAXO6 with distinct ciliary microtubules from the immotile cilium present in rod and cone photoreceptors in human retina, as well as from the motile cilia present in lung epithelial cells. Cross-linking mass spectrometry uncovered an interaction between SAXO6 and α-tubulin, supporting its classification as a microtubule inner protein (MIP). These results link SAXO proteins to Mendelian conditions, highlighting the fundamental role for MIPs in the preservation of long-term retinal function. - Source: PubMed
Publication date: 2026/02/24
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