Computational simulations suggest that a flexible part of the human Mic60-Mic19 protein subcomplex may act as a size-dependent gate at the narrow entrances to mitochondrial folds. The result is a model-based proposal—not direct evidence that the full MICOS complex filters proteins inside living mitochondria.
What is the proposed mitochondrial gate?
Mitochondrial cristae are folds or pockets in the inner membrane. The MICOS complex helps stabilize these structures, and the Mic60-Mic19 subcomplex is located at their narrow junctions, according to the Max Delbrück Center’s October 6, 2026 report.
The study proposes that Mic60-Mic19 does more than help shape the junction: it may also influence which proteins can pass through it. Its focus is this subcomplex, not the entire MICOS complex.
How did the researchers model Mic60-Mic19?
A long region of Mic60-Mic19 is disordered, meaning it does not hold one fixed shape. That flexibility makes it difficult to represent with a single static structure. To build a virtual model of the human subcomplex, the researchers combined an X-ray structure of an animal-specific Mic60 section with fungal structural data and AI predictions, then used computational simulations to represent movement.
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The Max Delbrück Center report says the model showed 97% correspondence with structural data from human mitochondria. It does not specify the comparison metric, so the figure should be read as the report’s description of a particular model-to-data comparison—not as a general accuracy score.
What did the simulations suggest could pass?
In a diffusion simulation, spheres stood in for proteins of different sizes. The modeled complex blocked spheres with radii larger than 2 nanometers, and the researchers identified the disordered regions as important to this gatekeeping behavior. This is a result within the simulation; it does not establish a universal size cutoff for proteins passing through mitochondrial cristae in living cells.
The distinction matters: a static structure gives a snapshot, while the simulation explores how a flexible region might move and affect passage. As doctoral student Evangelia Nathanail put it in the institutional report, “With one static structure, we might not have seen exactly how it swats all of those spheres away,”
What does the finding mean for disease?
The report notes that a known mutation associated with optic nerve damage and a developmental brain disorder alters the core of the MICOS complex. The modeled gatekeeping mechanism may offer one possible way to investigate how such a change could affect mitochondrial structure or function, but the study does not demonstrate a causal chain from that mutation to disease through altered protein passage.
What remains unconfirmed?
The work is reported as Evangelia Nathanail et al., “Integrative structural modelling reveals the human Mic60-Mic19 subcomplex as a diffusion barrier in mitochondria,” published in Nature Communications in 2026 (DOI: 10.1038/s41467-026-77869-3). The detailed findings and publication information summarized here are attributed to the Max Delbrück Center report; the journal article is listed at Nature Communications.
The model covers only part of MICOS. Confirming that the full complex performs this filtering function requires observing it at work inside mitochondria. Until then, the proposed gate is a computationally supported mechanism, not a directly observed activity of the complete complex in living cells.
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