{"doi":"10.1083/jcb.200410030","title":"Mdm31 and Mdm32 are inner membrane proteins required for maintenance of mitochondrial shape and stability of mitochondrial DNA nucleoids in yeast","abstract":"<jats:p>The MDM31 and MDM32 genes are required for normal distribution and morphology of mitochondria in the yeast Saccharomyces cerevisiae. They encode two related proteins located in distinct protein complexes in the mitochondrial inner membrane. Cells lacking Mdm31 and Mdm32 harbor giant spherical mitochondria with highly aberrant internal structure. Mitochondrial DNA (mtDNA) is instable in the mutants, mtDNA nucleoids are disorganized, and their association with Mmm1-containing complexes in the outer membrane is abolished. Mutant mitochondria are largely immotile, resulting in a mitochondrial inheritance defect. Deletion of either one of the MDM31 and MDM32 genes is synthetically lethal with deletion of either one of the MMM1, MMM2, MDM10, and MDM12 genes, which encode outer membrane proteins involved in mitochondrial morphogenesis and mtDNA inheritance. We propose that Mdm31 and Mdm32 cooperate with Mmm1, Mmm2, Mdm10, and Mdm12 in maintenance of mitochondrial morphology and mtDNA.</jats:p>","journal":"The Journal of Cell Biology","year":2005,"id":645080,"datarank":0.6937459219926407,"base_score":4.624972813284271,"endowment":4.624972813284271,"self_citation_contribution":0.6937459219926407,"citation_network_contribution":0.0,"self_endowment_contribution":0.6937459219926407,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":101,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":813369,"name":"Stefan Jakobs","orcid":"0000-0002-8028-3121","position":1,"is_corresponding":false},{"id":1679498,"name":"Frank Vogel","orcid":null,"position":2,"is_corresponding":false},{"id":1679499,"name":"Katrin Altmann","orcid":null,"position":3,"is_corresponding":false},{"id":1679500,"name":"Benedikt Westermann","orcid":null,"position":4,"is_corresponding":false},{"id":1679497,"name":"Kai Stefan Dimmer","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Mdm31 and Mdm32 are inner membrane proteins required for maintenance of mitochondrial shape and stability of mitochondrial DNA nucleoids in yeast","abstract":"<jats:p>The MDM31 and MDM32 genes are required for normal distribution and morphology of mitochondria in the yeast Saccharomyces cerevisiae. They encode two related proteins located in distinct protein complexes in the mitochondrial inner membrane. Cells lacking Mdm31 and Mdm32 harbor giant spherical mitochondria with highly aberrant internal structure. Mitochondrial DNA (mtDNA) is instable in the mutants, mtDNA nucleoids are disorganized, and their association with Mmm1-containing complexes in the outer membrane is abolished. Mutant mitochondria are largely immotile, resulting in a mitochondrial inheritance defect. Deletion of either one of the MDM31 and MDM32 genes is synthetically lethal with deletion of either one of the MMM1, MMM2, MDM10, and MDM12 genes, which encode outer membrane proteins involved in mitochondrial morphogenesis and mtDNA inheritance. We propose that Mdm31 and Mdm32 cooperate with Mmm1, Mmm2, Mdm10, and Mdm12 in maintenance of mitochondrial morphology and mtDNA.</jats:p>","is_dataset_classified":null,"base_score":4.624972813284271,"endowment":4.624972813284271,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"15631992","pmcid":"PMC2171677","openalex_id":"https://openalex.org/W2131236935","authors":[],"funders":[],"total_grants":0,"fwci":3.4442,"citation_percentile":0.93190423,"influential_citations":0,"citation_trend":[{"year":2012,"count":9},{"year":2013,"count":4},{"year":2014,"count":11},{"year":2015,"count":3},{"year":2016,"count":7},{"year":2017,"count":3},{"year":2018,"count":2},{"year":2019,"count":3},{"year":2020,"count":2},{"year":2021,"count":1},{"year":2022,"count":2},{"year":2023,"count":1},{"year":2024,"count":1},{"year":2025,"count":1}],"oa_status":"bronze","license":"other-oa","oa_locations":[{"url":"http://jcb.rupress.org/content/168/1/103.full.pdf","host_type":"journal"},{"url":"http://jcb.rupress.org/content/168/1/103.full.pdf","host_type":"publisher"},{"url":"https://rupress.org/jcb/article-pdf/168/1/103/1541944/jcb1681103.pdf","host_type":"publisher"},{"url":"https://doi.org/10.1083/jcb.200410030","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/15631992","host_type":"repository"},{"url":"http://edoc.mpg.de/256011","host_type":"repository"},{"url":"https://eref.uni-bayreuth.de/58261/","host_type":"repository"},{"url":"https://resolver.sub.uni-goettingen.de/purl?gro-2/1471","host_type":"repository"},{"url":"https://resolver.sub.uni-goettingen.de/purl?gro-2/13527","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/2171677","host_type":"repository"},{"url":"http://hdl.handle.net/11858/00-001M-0000-0012-EA57-2","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC2171677","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC2171677?pdf=render","host_type":"Europe_PMC"}],"fields_of_study":["Mitochondrial Function and Pathology","RNA and protein synthesis mechanisms","Photosynthetic Processes and Mechanisms"],"mesh_terms":["Actins","DNA, Mitochondrial","Epistasis, Genetic","Humans","Intracellular Membranes","Membrane Proteins","Mitochondria","Phenotype","Phylogeny","Saccharomyces cerevisiae","Mitochondrial Proteins","Saccharomyces cerevisiae Proteins","Genomic Instability","Multiprotein Complexes","Green Fluorescent Proteins"],"keywords":["Mitochondrial DNA","Biology","Mitochondrion","Mitochondrial fission","Nucleoid","Inner mitochondrial membrane","Inner membrane","Translocase of the inner membrane","Mitochondrial carrier","Cell biology","Bacterial outer membrane","mitochondrial fusion","MT-RNR1","Mutant","Saccharomyces cerevisiae","DNAJA3","ATP–ADP translocase","Gene","HSPA9","Genetics","Mitochondrial membrane transport protein","Peptide sequence"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Life in Land"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-09T02:49:31.281942Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}