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Updated: May 27, 2026

Peroxisome Staining in Mammalian Cells Using Peroxisome-Specific Probes
Published on: December 19, 2025
Subcellular evidence for the involvement of peroxisomes in plant isoprenoid biosynthesis
Marc Clastre1, Nicolas Papon, Vincent Courdavault
1Université François-Rabelais de Tours, EA2106, Biomolécules et Biotechnologies Végétales, Tours, France.
Abstract:
The role of peroxisomes in isoprenoid metabolism, especially in plants, has been questioned in several reports. A recent study of Sapir-Mir et al. revealed that the two isoforms of isopentenyl diphosphate (IPP) isomerase, catalyzing the isomerisation of IPP to dimethylallyl diphosphate (DMAPP) are found in the peroxisome. In this addendum, we provide additional data describing the peroxisomal localization of 5-phosphomevalonate kinase and mevalonate 5-diphosphate decarboxylase, the last two enzymes of the mevalonic acid pathway leading to IPP. This finding was reinforced in our latest report showing that a short isoform of farnesyl diphosphate, using IPP and DMAPP as substrates, is also targeted to the organelle. Therefore, the classical sequestration of isoprenoid biosynthesis between plastids and cytosol/ER can be revisited by including the peroxisome as an additional isoprenoid biosynthetic compartment within plant cells.
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