MIC10 subcomplex

cellstructuremech:mic10_subcomplex · Other · Multiprotein complex · Proposed

A mitochondrial inner-membrane MICOS subcomplex containing Mic10, Mic12, Mic26 and Mic27, organized around Mic10 oligomers and involved in crista architecture. [DOI:10.1016/j.jmb.2018.04.037]

Conditional MICOS subassembly in W303-derived Saccharomyces cerevisiae, not an image of an isolated intact four-protein MIC10 complex. Full Figure 3: confocal fluorescence of tagged MICOS proteins and mitochondrial markers in deletion and reconstitution strains (A-C, E), Mic27 foci counts (D, F), and Mic27-EGFP immunopurification mass-spectrometry comparison (G). Mic10 and Mic12 support focal Mic27 assemblies without Mic60. Original multipanel figure retained. FLUORESCENCE · *Saccharomyces cerevisiae* (`NCBITaxon:4932`) · Jonathan R Friedman, Arnaud Mourier, Justin Yamada, J Michael McCaffery, Jodi Nunnari; CC BY, via PubMed Central · CC_BY_4_0 · source: PMC PMC4434539.1 fig3 · `DOI:10.7554/eLife.07739`

Part of: MICOS complex (GO:0061617)

UniProt location names: UniProt Consortium, CC BY 4.0. Reference label and route sources.

Components

Component	Type	Part of / acts on	Grounding	Genes	Role
MICOS complex subunit Mic10	Protein	part of	`InterPro:IPR007512`	MIC10	Oligomeric scaffold of the inner-membrane subcomplex. `DOI:10.1016/j.jmb.2018.04.037` Mic10 oligomer ladders and cross-linking products are altered by Mic26 and Mic27 deletion.
MICOS complex subunit Mic12	Protein	part of	`InterPro:IPR031463`	MIC12	Subunit that promotes focal assembly of the Mic10-Mic27 organizing center. `DOI:10.7554/elife.07739` In W303 derivatives lacking other MICOS proteins, Mic10 plus Mic12 restores prominent Mic27 foci; mic12 deletion reduces foci in the mic60-deletion background. `DOI:10.1016/j.jmb.2018.04.037` The paper explicitly defines the four-protein MIC10 subcomplex.
MICOS subunit Mic26, fungi	Protein	part of	`InterPro:IPR033181`	MIC26	Fungal subunit that counteracts stabilization of higher-order Mic10 oligomers. `DOI:10.1016/j.jmb.2018.04.037` Mic26 co-cross-links with Mic10; mic26 deletion favors higher-order Mic10 assemblies. `InterPro:IPR033181` Current InterPro fungal Mic26 family; the broader MIC26/MIC27 family also includes animal paralogs.
MICOS complex subunit MIC27	Protein	part of	`InterPro:IPR061953`	MIC27	Yeast subunit that stabilizes higher-order Mic10 assemblies. `DOI:10.1016/j.jmb.2018.04.037` Mic27 co-cross-links with Mic10; mic27 deletion reduces higher-order assemblies. `InterPro:IPR061953` Current family represents MIC27 from Saccharomycetaceae, not mammalian MIC27 or the broader ApoO family.

Taxonomic distribution

NCBITaxon:4932 Saccharomyces cerevisiae — COMMON: Demonstrated in budding-yeast mitochondrial MICOS using YPH499 derivatives; no universal fungal or eukaryotic distribution is asserted. [DOI:10.1016/j.jmb.2018.04.037]

Canonical examples

NCBITaxon:4932 Saccharomyces cerevisiae — YPH499 derivatives supply mitochondrial purification and cross-linking evidence. The separate 2015 fluorescence experiments use W303 derivatives, not the S288c proteins consulted for family lookup. [DOI:10.1016/j.jmb.2018.04.037]

Functions

inner mitochondrial membrane organization GO:0007007 — Contributes a Mic10-based organizing module to the MICOS machinery that maintains mitochondrial crista architecture.
- DOI:10.7554/elife.07739 Genetics, microscopy and Mic27 immunopurification distinguish an independent organizing center from the Mic60-containing module. Junction localization of Mic27 foci is inferred from proximity to crista markers, not resolved by direct immuno-electron microscopy.
- DOI:10.1016/j.jmb.2018.04.037 Antagonistic Mic26-Mic27 effects regulate the Mic10 oligomeric scaffold.

Mechanism graphs

Mic10 oligomer regulation and conditional Mic27 focal assembly (ASSEMBLY)

Protein-specific perturbations distinguish regulation of Mic10 oligomers from focal assembly of a Mic27-containing organizing center.

Subject	Predicate	Object	Evidence
MICOS complex subunit Mic10	oligomerizes into	Higher-order Mic10 assemblies	`DOI:10.1016/j.jmb.2018.04.037` Native-gel ladders and in-organello cross-linking provide complementary assembly evidence.
MICOS subunit Mic26, fungi	destabilizes	Higher-order Mic10 assemblies	`DOI:10.1016/j.jmb.2018.04.037` Deletion shifts Mic10 toward larger assemblies and increases cross-linking adducts.
MICOS complex subunit MIC27	stabilizes	Higher-order Mic10 assemblies	`DOI:10.1016/j.jmb.2018.04.037` Deletion favors smaller assemblies and reduces Mic10 cross-linking adducts.
MICOS complex subunit Mic10	is required for	Focal Mic27-containing assemblies without Mic60	`DOI:10.7554/elife.07739` Figure 3E-F: mic60 mic10 double-deletion cells lack detectable Mic27 foci; reconstitution with Mic10 supports some focal assembly.
MICOS complex subunit Mic12	promotes	Focal Mic27-containing assemblies without Mic60	`DOI:10.7554/elife.07739` Figure 3C-F: Mic10 plus Mic12 restores prominent Mic27 foci in cells lacking the other MICOS proteins; Mic12 loss reduces, rather than abolishes, foci in mic60-deletion cells.

Discussions

INTERPRETATION (RESOLVED): Reconcile the four-subunit MIC10 module with the three-protein organizing center seen in deletion strains. The 2015 Mic27/Mic12/Mic10 assembly does not establish that Mic26 is absent from the normal module; the experiments ask which proteins sustain focal assembly without other MICOS subunits.
INTERPRETATION (RESOLVED): Distinguish environmental assembly dependencies from constituent identity. Genetic cardiolipin dependence and proximity to ER contact sites do not identify additional stoichiometric components of this protein module.
CURATION_TODO (OPEN): Resolve intact native subcomplex architecture, stoichiometry and direct cardiolipin-binding interfaces. Native-gel migration, cross-linking and fluorescent foci do not establish one atomic structure or copy number. Direct cardiolipin binding to Mic10 is proposed from the perturbation data rather than independently measured in the cited 2018 study.

Evidence

DOI:10.1016/j.jmb.2018.04.037 Rampelt et al. (2018), Assembly of the Mitochondrial Cristae Organizer Mic10 Is Regulated by Mic26-Mic27 Antagonism and Cardiolipin. Main text, captions and Figures 1-4 inspected in the institutional publisher-version PDF.
DOI:10.7554/elife.07739 Friedman et al. (2015), MICOS coordinates with respiratory complexes and lipids to establish mitochondrial inner membrane architecture. Relevant Results, Discussion, strain methods and Figure 3 inspected in checksum-verified PMC4434539 version 1.
DOI:10.1083/jcb.202003024 Tirrell et al. (2020), MICOS subcomplexes assemble independently on the mitochondrial inner membrane in proximity to ER contact sites. Subcomplex-localization and ERMES-perturbation Results plus strain methods inspected in checksum-verified PMC7545361 version 1.
GO:0098800 Broader is-a parent: inner mitochondrial membrane protein complex.
GO:0061617 Containing MICOS complex; not an exact synonym or is-a parent of this subassembly.

Curation history

2026-10-04T22:30:30Z codex · CREATED_RECORD — Scaffolded by scripts/new_record.py
2026-10-04T22:31:41Z codex · EXPANDED_RECORD — Added four verified protein families, bounded yeast examples, inner-membrane organization, five experimental assembly edges and explicit conditional-core, lipid and native-architecture limits.
2026-10-04T22:32:05Z pmc_oa · ADD_IMAGE — Added PMC4434539.1 fig3; version, CC licence, JATS figure identity and media md5 verified through the PMC OA S3 dataset.

Source: data/structures/other/mic10_subcomplex.yaml