{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMICOS10, also known as MINOS1/MIO10 in yeast and mammals, is an evolutionarily conserved mitochondrial inner membrane protein that plays a critical role in organizing mitochondrial architecture. As a constituent of the Mitofilin/Fcj1 and broader MICOS complexes, MICOS10 contributes to the formation and maintenance of crista junctions and the inner membrane’s subcompartmentalization. Disruption of MICOS10 or mutations affecting its function alter inner membrane organization and compromise mitochondrial performance, particularly under conditions requiring oxidative metabolism."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nRecent advances in nanoscopy have provided deeper insights into the molecular arrangement of MICOS subunits. High-resolution MINFLUX imaging has revealed that while core components such as Mic60 adopt defined ring‐like structures around crista junctions, the spatial distribution of MICOS10 (Mic10) is more variable. This suggests that Mic10 may be subject to unique regulatory mechanisms within the MICOS complex, contributing in a specialized manner to the overall architecture of the mitochondrial inner membrane."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMoreover, MICOS10 has been implicated in dynamic mitochondrial remodeling during cellular stress. In particular, studies investigating Listeria monocytogenes infection have shown that an increase in MICOS10 levels is essential for the pathogen-induced mitochondrial fragmentation—an effect distinct from canonical fission pathways. Disruption of the MIC10 subcomplex, for example by mutations in bridging factors such as MIC13, further underscores the pivotal role of MICOS10 in maintaining cristae morphology and proper bioenergetic function during physiological challenges."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Alwaleed K Alkhaja, Daniel C Jans, Miroslav Nikolov, et al. "}, {"type": "b", "children": [{"type": "t", "text": "MINOS1 is a conserved component of mitofilin complexes and required for mitochondrial function and cristae organization."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Biol Cell (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1091/mbc.E11-09-0774"}], "href": "https://doi.org/10.1091/mbc.E11-09-0774"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22114354"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22114354"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Tobias A Weber, Sebastian Koob, Heinrich Heide, et al. "}, {"type": "b", "children": [{"type": "t", "text": "APOOL is a cardiolipin-binding constituent of the Mitofilin/MINOS protein complex determining cristae morphology in mammalian mitochondria."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS One (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.pone.0063683"}], "href": "https://doi.org/10.1371/journal.pone.0063683"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23704930"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23704930"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Jasmin K Pape, Till Stephan, Francisco Balzarotti, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Multicolor 3D MINFLUX nanoscopy of mitochondrial MICOS proteins."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.2009364117"}], "href": "https://doi.org/10.1073/pnas.2009364117"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32788360"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32788360"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Filipe Carvalho, Anna Spier, Thibault Chaze, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Listeria monocytogenes Exploits Mitochondrial Contact Site and Cristae Organizing System Complex Subunit Mic10 To Promote Mitochondrial Fragmentation and Cellular Infection."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "mBio (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/mBio.03171-19"}], "href": "https://doi.org/10.1128/mBio.03171-19"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32019800"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32019800"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Jennifer Urbach, Arun Kumar Kondadi, Céline David, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Conserved GxxxG and WN motifs of MIC13 are essential for bridging two MICOS subcomplexes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochim Biophys Acta Biomembr (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbamem.2021.183683"}], "href": "https://doi.org/10.1016/j.bbamem.2021.183683"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34271005"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34271005"}]}]}]}