Copper, endoproteolytic processing of the prion protein and cell signalling

Abstract

Recently, understanding of many molecular interactions has progressed appreciably and cellular events once thought to be by-products of more important reactions or to be detrimental to cellular function are now known to be part of complex interactions of the cell with its environment. Numerous proteins can elicit differing effects depending upon post-translational modification events such as complex glycosylation and endoproteolytic cleavage or through binding co-factors including metal ions; the prion protein (PrP) is likely one such example. Its absolute requirement for pathogenesis has made the function of PrP an area of intense study but with apparently inconsistent results. This may, in..