Lipid-Linked Heparan Sulfate Proteoglycan

Abstract

The covalent addition of lipids to the protein core of heparan sulfate proteoglycans provides novel molecular bonds between these gene products and the plasma membrane. Glypiation of proteoglycans is involved in apical sorting, membrane targeting and it provides a mechanism for rapid enzymatic release of surface proteoglycans. Fatty acylation of proteoglycans mediates hydrophobic interactions and possibly receptor-mediated binding, it can provide a novel mechanism for intracellular proteoglycan/proteoglycan interaction and may play a direct role in turnover. Identification of the fine structural requirements and complex enzymatic machinery involved in lipid anchoring will establish the functional sigmficance for these novel post-translational modifications of proteoglycans.