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

J Cell Sci. 2020 Dec 17;133(24):jcs244376. doi: 10.1242/jcs.244376.

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.

Keywords: Glyoxylate cycle; Malate dehydrogenase; Peroxisomes; Pex5; Piggybacking; Protein targeting.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cytosol / metabolism
  • Glyoxylates
  • Malate Dehydrogenase / genetics
  • Malate Dehydrogenase / metabolism
  • Peroxisomes / metabolism
  • Saccharomyces cerevisiae Proteins* / genetics
  • Saccharomyces cerevisiae Proteins* / metabolism
  • Saccharomyces cerevisiae* / genetics
  • Saccharomyces cerevisiae* / metabolism

Substances

  • Glyoxylates
  • Saccharomyces cerevisiae Proteins
  • MDH2 protein, S cerevisiae
  • Malate Dehydrogenase