J. Lipid Res.
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A more recent version of this article appeared on July 1, 2006

Papers In Press, published online ahead of print April 20, 2006
J. Lipid Res., doi:10.1194/jlr.R600010-JLR200
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Submitted on April 3, 2006
Revised on April 18, 2006
Accepted on April 20, 2006

Lysosomal metabolism of lipid-modified proteins

Jui-Yun Lu and Sandra L. Hofmann

Internal Medicine, University of Texas Southwestern Medicine Center, Dallas, TX 75390-8593

Corresponding Author: sandra.hofmann{at}utsouthwestern.edu

Much is now understood concerning the synthesis of prenylated and palmitoylated proteins, but what is known of their metabolic fate? This review details metabolic pathways for the lysosomal degradation of S-fatty acylated and prenylated proteins. Central to these pathways are two lysosomal enzymes, palmitoyl-protein thioesterase and prenylcysteine lyase. Palmitoyl-protein thioesterase is a soluble lipase that cleaves fatty acids from cysteine residues in proteins during lysosomal protein degradation. Notably, deficiency in the enzyme causes a neurodegenerative lysosomal storage disorder, infantile neuronal ceroid lipofuscinosis. Prenylcysteine lyase is a membrane-associated flavin-containing lysosomal monooxygenase that metabolizes prenylcysteine to prenyl aldehyde through a completely novel mechanism. The eventual metabolic fates of other lipidated proteins (such as glycosylphosphatidylinositol-anchored and N-myristoylated proteins) are poorly understood, suggesting directions for future research.


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