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"name": {
"name": "synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in maintenance of mitochondrial morphology protein 1 (Mmm1) and similar proteins",
"short": "SMP_Mmm1"
},
"description": [
{
"text": "<p>Maintenance of mitochondrial morphology protein 1 (Mmm1), also called mitochondrial outer membrane protein Mmm1, or yeast mitochondrial escape protein 6 (YME6), is a mitochondrial outer membrane protein essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids. It is a component of the ER-mitochondrion encounter structure/ mitochondrial distribution and morphology (ERMES/Mdm) complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. The Mdm12-Mmm1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The Mdm10-Mdm12-Mmm1 subcomplex further acts in the TOM40-specific pathway after the action of the Mdm12-Mmm1 complex. This model corresponds to the SMP domain of Mmm1, which may be implicated in lipid transport. [[cite:PUB00064831], [cite:PUB00148176], [cite:PUB00148175], [cite:PUB00055950], [cite:PUB00064806], [cite:PUB00121183], [cite:PUB00064827], [cite:PUB00016470], [cite:PUB00064833], [cite:PUB00148186], [cite:PUB00148187], [cite:PUB00148188], [cite:PUB00064830], [cite:PUB00075642]]</p>",
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"title": "Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins.",
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"medline_journal": "Mol Biol Cell",
"ISO_journal": "Mol Biol Cell",
"authors": [
"Zahedi RP",
"Sickmann A",
"Boehm AM",
"Winkler C",
"Zufall N",
"Schonfisch B",
"Guiard B",
"Pfanner N",
"Meisinger C."
],
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"title": "A phospholipid transfer function of ER-mitochondria encounter structure revealed in vitro.",
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"authors": [
"Kojima R",
"Endo T",
"Tamura Y."
],
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},
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"issue": "49",
"year": 2003,
"title": "Mmm1p spans both the outer and inner mitochondrial membranes and contains distinct domains for targeting and foci formation.",
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"raw_pages": "48997-9005",
"medline_journal": "J Biol Chem",
"ISO_journal": "J Biol Chem",
"authors": [
"Kondo-Okamoto N",
"Shaw JM",
"Okamoto K."
],
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},
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"title": "The morphology proteins Mdm12/Mmm1 function in the major beta-barrel assembly pathway of mitochondria.",
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"medline_journal": "EMBO J",
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"authors": [
"Meisinger C",
"Pfannschmidt S",
"Rissler M",
"Milenkovic D",
"Becker T",
"Stojanovski D",
"Youngman MJ",
"Jensen RE",
"Chacinska A",
"Guiard B",
"Pfanner N",
"Wiedemann N."
],
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"year": 2003,
"title": "A protein complex containing Mdm10p, Mdm12p, and Mmm1p links mitochondrial membranes and DNA to the cytoskeleton-based segregation machinery.",
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"raw_pages": "4618-27",
"medline_journal": "Mol Biol Cell",
"ISO_journal": "Mol. Biol. Cell",
"authors": [
"Boldogh IR",
"Nowakowski DW",
"Yang HC",
"Chung H",
"Karmon S",
"Royes P",
"Pon LA."
],
"DOI_URL": "http://dx.doi.org/10.1091/mbc.E03-04-0225"
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"title": "Interaction between mitochondria and the actin cytoskeleton in budding yeast requires two integral mitochondrial outer membrane proteins, Mmm1p and Mdm10p.",
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"medline_journal": "J Cell Biol",
"ISO_journal": "J Cell Biol",
"authors": [
"Boldogh I",
"Vojtov N",
"Karmon S",
"Pon LA."
],
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},
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"volume": "114",
"issue": "45",
"year": 2017,
"title": "Crystal structures of Mmm1 and Mdm12-Mmm1 reveal mechanistic insight into phospholipid trafficking at ER-mitochondria contact sites.",
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"raw_pages": "E9502-E9511",
"medline_journal": "Proc Natl Acad Sci U S A",
"ISO_journal": "Proc Natl Acad Sci U S A",
"authors": [
"Jeong H",
"Park J",
"Jun Y",
"Lee C."
],
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"issue": "2",
"year": 2006,
"title": "Diverse membrane-associated proteins contain a novel SMP domain.",
"URL": null,
"raw_pages": "202-6",
"medline_journal": "FASEB J",
"ISO_journal": "FASEB J.",
"authors": [
"Lee I",
"Hong W."
],
"DOI_URL": "http://dx.doi.org/10.1096/fj.05-4581hyp"
},
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"PMID": 14981098,
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"volume": "164",
"issue": "5",
"year": 2004,
"title": "Mmm2p, a mitochondrial outer membrane protein required for yeast mitochondrial shape and maintenance of mtDNA nucleoids.",
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"medline_journal": "J Cell Biol",
"ISO_journal": "J. Cell Biol.",
"authors": [
"Youngman MJ",
"Hobbs AE",
"Burgess SM",
"Srinivasan M",
"Jensen RE."
],
"DOI_URL": "http://dx.doi.org/10.1083/jcb.200308012"
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"title": "Global analysis of protein localization in budding yeast.",
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"authors": [
"Huh WK",
"Falvo JV",
"Gerke LC",
"Carroll AS",
"Howson RW",
"Weissman JS",
"O'Shea EK."
],
"DOI_URL": "http://dx.doi.org/10.1038/nature02026"
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"title": "Maintenance of mitochondrial morphology is linked to maintenance of the mitochondrial genome in Saccharomyces cerevisiae.",
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"medline_journal": "Genetics",
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"authors": [
"Hanekamp T",
"Thorsness MK",
"Rebbapragada I",
"Fisher EM",
"Seebart C",
"Darland MR",
"Coxbill JA",
"Updike DL",
"Thorsness PE."
],
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"volume": "126",
"issue": "6",
"year": 1994,
"title": "MMM1 encodes a mitochondrial outer membrane protein essential for establishing and maintaining the structure of yeast mitochondria.",
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"medline_journal": "J Cell Biol",
"ISO_journal": "J. Cell Biol.",
"authors": [
"Burgess SM",
"Delannoy M",
"Jensen RE."
],
"DOI_URL": "http://dx.doi.org/10.1083/jcb.126.6.1375"
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"title": "An ER-mitochondria tethering complex revealed by a synthetic biology screen.",
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"medline_journal": "Science",
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"authors": [
"Kornmann B",
"Currie E",
"Collins SR",
"Schuldiner M",
"Nunnari J",
"Weissman JS",
"Walter P."
],
"DOI_URL": "http://dx.doi.org/10.1126/science.1175088"
},
"PUB00064831": {
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"volume": "152",
"issue": "2",
"year": 2001,
"title": "Mmm1p, a mitochondrial outer membrane protein, is connected to mitochondrial DNA (mtDNA) nucleoids and required for mtDNA stability.",
"URL": null,
"raw_pages": "401-10",
"medline_journal": "J Cell Biol",
"ISO_journal": "J. Cell Biol.",
"authors": [
"Hobbs AE",
"Srinivasan M",
"McCaffery JM",
"Jensen RE."
],
"DOI_URL": "http://dx.doi.org/10.1083/jcb.152.2.401"
}
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