{"doi":"10.1083/jcb.200308012","title":"Mmm2p, a mitochondrial outer membrane protein required for yeast mitochondrial shape and maintenance of mtDNA nucleoids","abstract":"<jats:p>The mitochondrial outer membrane protein, Mmm1p, is required for normal mitochondrial shape in yeast. To identify new morphology proteins, we isolated mutations incompatible with the mmm1-1 mutant. One of these mutants, mmm2-1, is defective in a novel outer membrane protein. Lack of Mmm2p causes a defect in mitochondrial shape and loss of mitochondrial DNA (mtDNA) nucleoids. Like the Mmm1 protein (Aiken Hobbs, A.E., M. Srinivasan, J.M. McCaffery, and R.E. Jensen. 2001. J. Cell Biol. 152:401–410.), Mmm2p is located in dot-like particles on the mitochondrial surface, many of which are adjacent to mtDNA nucleoids. While some of the Mmm2p-containing spots colocalize with those containing Mmm1p, at least some of Mmm2p is separate from Mmm1p. Moreover, while Mmm2p and Mmm1p both appear to be part of large complexes, we find that Mmm2p and Mmm1p do not stably interact and appear to be members of two different structures. We speculate that Mmm2p and Mmm1p are components of independent machinery, whose dynamic interactions are required to maintain mitochondrial shape and mtDNA structure.</jats:p>","journal":"The Journal of Cell Biology","year":2004,"id":647426,"datarank":0.7515952941144385,"base_score":5.0106352940962555,"endowment":5.0106352940962555,"self_citation_contribution":0.7515952941144385,"citation_network_contribution":0.0,"self_endowment_contribution":0.7515952941144385,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":149,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":14,"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":1686798,"name":"Alyson E. 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Lack of Mmm2p causes a defect in mitochondrial shape and loss of mitochondrial DNA (mtDNA) nucleoids. Like the Mmm1 protein (Aiken Hobbs, A.E., M. Srinivasan, J.M. McCaffery, and R.E. Jensen. 2001. J. Cell Biol. 152:401–410.), Mmm2p is located in dot-like particles on the mitochondrial surface, many of which are adjacent to mtDNA nucleoids. While some of the Mmm2p-containing spots colocalize with those containing Mmm1p, at least some of Mmm2p is separate from Mmm1p. Moreover, while Mmm2p and Mmm1p both appear to be part of large complexes, we find that Mmm2p and Mmm1p do not stably interact and appear to be members of two different structures. We speculate that Mmm2p and Mmm1p are components of independent machinery, whose dynamic interactions are required to maintain mitochondrial shape and mtDNA structure.</jats:p>","is_dataset_classified":null,"base_score":5.0106352940962555,"endowment":5.0106352940962555,"datacite_reuse_total":14,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"14981098","pmcid":"PMC2172170","openalex_id":"https://openalex.org/W1964155535","authors":[],"funders":[{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM054021","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"2T32-GM07445","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R01-GM54021","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"T32 GM007445","title":null},{"funder_name":"National Institutes of Health","grant_id":"1R01GM054021-01","title":"MITOCHONDRIAL DYNAMICS--MORPHOLOGY/DIVISION/SEGREGATION"},{"funder_name":"National Institutes of Health","grant_id":"5T32GM007445-33","title":"Biochemistry, Cellular and Molecular Biology Program"}],"total_grants":6,"fwci":2.8383,"citation_percentile":0.90641081,"influential_citations":0,"citation_trend":[{"year":2012,"count":5},{"year":2013,"count":7},{"year":2014,"count":15},{"year":2015,"count":4},{"year":2016,"count":12},{"year":2017,"count":8},{"year":2018,"count":7},{"year":2019,"count":3},{"year":2020,"count":7},{"year":2021,"count":4},{"year":2022,"count":3},{"year":2023,"count":5},{"year":2024,"count":6},{"year":2025,"count":3},{"year":2026,"count":1}],"oa_status":"bronze","license":null,"oa_locations":[{"url":"https://rupress.org/jcb/article-pdf/164/5/677/1064935/jcb1645677.pdf","host_type":"journal"},{"url":"https://rupress.org/jcb/article-pdf/164/5/677/1064935/jcb1645677.pdf","host_type":"publisher"},{"url":"https://rupress.org/jcb/article-pdf/164/5/677/1529232/jcb1645677.pdf","host_type":"publisher"},{"url":"https://doi.org/10.1083/jcb.200308012","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/14981098","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/2172170","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC2172170","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC2172170?pdf=render","host_type":"Europe_PMC"},{"url":"http://dx.doi.org/10.1083/jcb.200308012","host_type":""},{"url":"https://dx.doi.org/10.1083/jcb.200308012","host_type":""}],"fields_of_study":["Mitochondrial Function and Pathology","RNA and protein synthesis mechanisms","RNA Research and Splicing","0301 basic medicine","0303 health sciences","03 medical and health sciences","Cell Division","Cell Membrane","DNA, Mitochondrial","Macromolecular Substances","Membrane Proteins","Mitochondria","Mitochondrial Proteins","Nucleic Acid Conformation","Recombinant Fusion Proteins","Saccharomyces cerevisiae","Saccharomyces cerevisiae Proteins","Subcellular Fractions"],"mesh_terms":["Cell Division","Cell Membrane","DNA, Mitochondrial","Membrane Proteins","Mitochondria","Nucleic Acid Conformation","Recombinant Fusion Proteins","Saccharomyces cerevisiae","Subcellular Fractions","Mitochondrial Proteins","Saccharomyces cerevisiae Proteins","Macromolecular Substances"],"keywords":["Biology","Mitochondrial DNA","Nucleoid","Mitochondrial carrier","Translocase of the inner membrane","ATP–ADP translocase","Bacterial outer membrane","Mitochondrion","Inner mitochondrial membrane","Mutant","DNAJA3","Translocase of the outer membrane","Cell biology","HSPA9","Inner membrane","mitochondrial fusion","Genetics","Mitochondrial membrane transport protein","Gene","Peptide sequence","Saccharomyces cerevisiae Proteins","Macromolecular Substances","Recombinant Fusion Proteins","Cell Membrane","Membrane Proteins","Saccharomyces cerevisiae","DNA, Mitochondrial","Article","Mitochondria","Mitochondrial Proteins","Nucleic Acid Conformation","Cell Division","Subcellular Fractions"],"sdg_mappings":[{"sdg_number":3,"sdg_label":"3. 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