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

Shiran Gabay-Maskit, Luis Daniel Cruz-Zaragoza, Nadav Shai, Miriam Eisenstein, Chen Bibi, Nir Cohen, Tobias Hansen, Eden Yifrach, Nofar Harpaz, Ruth Belostotsky, Wolfgang Schliebs, Maya Schuldiner, Ralf Erdmann, Einat Zalckvar

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Article numberjcs244376
Number of pages10
JournalJournal of Cell Science
Volume133
Issue number24
DOIs
StatePublished - 17 Dec 2020

Keywords

  • Glyoxylate cycle
  • Malate dehydrogenase
  • Peroxisomes
  • Pex5
  • Piggybacking
  • Protein targeting

All Science Journal Classification (ASJC) codes

  • Cell Biology

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