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J. Lipid Res.
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A more recent version of this article appeared on April 1, 2004

Papers In Press, published online ahead of print January 16, 2004
J. Lipid Res., doi:10.1194/jlr.M300373-JLR200
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Submitted on September 4, 2003
Revised on January 8, 2004
Accepted on January 9, 2004

Phosphomevalonate kinase is a cytosolic protein in humans

Sietske Hogenboom, John J.M. Tuyp, Marc Espeel, Janet Koster, Ronald J.A. Wanders, and Hans R. Waterham

Departments of Clinical Chemistry, University of Amsterdam, Amsterdam, Amsterdam 1100 DE

Corresponding Author: H.R.Waterham{at}amc.uva.nl

In the past decade a predominant peroxisomal localization has been reported for several enzymes functioning in the pre-squalene segment of the cholesterol/isoprenoid biosynthetis pathway. 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 determined the subcellular localization of human phosphomevalonate kinase using a variety of biochemical and microscopical techniques, including conventional subcellular fractionation studies, digitonin permeabilization studies, immunofluorescence, and immunoelectron microscopy. We found an exclusive cytosolic localization of both endogenously expressed human phosphomevalonate kinase (in human fibroblasts, human liver and HEK293 cells) and overexpressed human phosphomevalonate kinase (in human fibroblasts, HEK293 cells and CV1 cells). No indication of a peroxisomal localization was obtained. Our results do not support a central role of peroxisomes in isoprenoid biosynthesis.


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