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A piggybacking mechanism enables peroxisomal localization of the glyoxylate cycle enzyme Mdh2 in yeast.

ABSTRACT: Eukaryotic cells have evolved organelles that allow the compartmentalization and regulation of metabolic processes. Knowledge of molecular mechanisms that allow temporal and spatial organization of enzymes within organelles is therefore crucial for understanding eukaryotic metabolism. Here, we show that the yeast malate dehydrogenase 2 (Mdh2) is dually localized to the cytosol and to peroxisomes and is targeted to peroxisomes via association with Mdh3 and a Pex5-dependent piggybacking mechanism. This dual localization of Mdh2 contributes to our understanding of the glyoxylate cycle and provides a new perspective on compartmentalization of cellular metabolism, which is critical for the perception of metabolic disorders and aging.

SUBMITTER: Gabay-Maskit S

PROVIDER: S-EPMC7758625 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature

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A piggybacking mechanism enables peroxisomal localization of the glyoxylate cycle enzyme Mdh2 in yeast.

Gabay-Maskit Shiran S Cruz-Zaragoza Luis Daniel LD Shai Nadav N Eisenstein Miriam M Bibi Chen C Cohen Nir N Hansen Tobias T Yifrach Eden E Harpaz Nofar N Belostotsky Ruth R Schliebs Wolfgang W Schuldiner Maya M Erdmann Ralf R Zalckvar Einat E

Journal of cell science 20201217 24

Eukaryotic cells have evolved organelles that allow the compartmentalization and regulation of metabolic processes. Knowledge of molecular mechanisms that allow temporal and spatial organization of enzymes within organelles is therefore crucial for understanding eukaryotic metabolism. Here, we show that the yeast malate dehydrogenase 2 (Mdh2) is dually localized to the cytosol and to peroxisomes and is targeted to peroxisomes via association with Mdh3 and a Pex5-dependent piggybacking mechanism. ...[more]

PMID: 33177075

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