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Biology subjects

Cho, H. Y.

Publications and source records attributed to Cho, H. Y..

2 recordsLinked to original sources

Humans and marmosets share similar face recognition signatures in shape-based visual face discrimination behavior

Our ability to identify faces is thought to depend on high-level visual processing in the brain. Nonetheless, studies of face recognition have generally relied on 2D face photographs where low-level strategies relying on texture and appearance cues can be employed to adequately support high face identification performance. Here, we designed a fine face discrimination task under 3D pose and lighting variation that was purely based on shape, a task which challenged state-of-the-art artificial vision systems compared to object recognition tasks. In contrast, humans performed this shape based face task at comparable levels to their object recognition performance. We then tested one of the smallest simian primates on this human-level, machine-difficult visual task, the common marmoset - a small, New World monkey. Marmosets successfully discriminated between face identities across 3D viewing conditions based purely on face shape. Their face recognition performance was on par with their object recognition performance and exhibited face-specific behavioral signatures similar to humans, including lower performance for inverted faces, faces lit from below, and contrast reversed faces. These results demonstrate that a high-level visual behavior, invariant face recognition based purely on geometry and not additional texture and appearance cues, is shared across simian primates from among the smallest to the most advanced, consistent with the presence of common underlying high-level visual brain areas across simian primates.

neuroscience↗

Clu1/Clu form mitochondria-associated granules upon metabolic transitions and regulate mitochondrial protein translation via ribosome interactions

Mitochondria perform essential metabolic functions and respond rapidly to changes in metabolic and stress conditions. As the majority of mitochondrial proteins are nuclear-encoded, intricate post-transcriptional regulation is crucial to enable mitochondria to adapt to changing cellular demands. The eukaryotic Clustered mitochondria protein family has emerged as an important regulator of mitochondrial function during metabolic shifts. Here, we show that the Drosophila melanogaster and Saccharomyces cerevisiae Clu/Clu1 proteins form dynamic, membraneless granules adjacent to mitochondria in response to metabolic changes. Yeast Clu1 regulates the translation of a subset of nuclear-encoded mitochondrial protein by interacting with their mRNAs while these are engaged in translation. We further show that Clu1 regulates translation by interacting with polysomes, independently of whether it is in a diffuse or granular state. Our results demonstrate remarkable functional conservation with other members of the Clustered mitochondria protein family and suggests that Clu/Clu1 granules isolate and concentrate ribosomes engaged in translating their mRNA targets, thus, integrating metabolic signals with the regulation of mitochondrial protein synthesis.

molecular biology↗