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First published online January 16, 2004
doi: 10.1242/10.1242/jcs.00910

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Mevalonate kinase is a cytosolic enzyme in humans

¹ Laboratory Genetic Metabolic Diseases, Department of Pediatrics, Emma Children's Hospital, Academic Medical Center, Amsterdam
² Department of Anatomy, Embryology, Histology & Medical Physics, University of Gent, Belgium

^* Author for correspondence (e-mail: h.r.waterham{at}amc.uva.nl)

Accepted 2 October 2003

In the past decade several reports have appeared which suggest that peroxisomes play a central role in isoprenoid/cholesterol biosynthesis. These suggestions were based primarily on the reported finding of several of the enzymes of the presqualene segment of the biosynthetic pathway in peroxisomes. More recently, however, conflicting results have been reported raising doubt about the postulated role of peroxisomes in isoprenoid biosynthesis, at least in humans. In this study we have studied the subcellular localisation of human mevalonate kinase (MK) using a variety of biochemical and microscopical techniques. These include conventional subcellular fractionation studies, digitonin permeabilisation studies, immunofluorescence microscopy and immunocytochemistry. We exclusively found a cytosolic localisation of both endogenous human MK (human fibroblasts, liver and HEK293 cells) and overexpressed human MK (human fibroblasts, HEK293 cells and CV1 cells). No indication of a peroxisomal localisation was obtained. Our results do not support a central role for peroxisomes in isoprenoid biosynthesis.

Key words: Cholesterol biosynthesis, Isoprenoid, Peroxisomes, Mevalonate kinase

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