The cation-independent mannose-6-phosphate receptor binds to soluble GPI-linked proteins via mannose-6-phosphate

Paula J. Green, Michael A. J. Ferguson, Peter J. Robinson, Ten Feizi

    Research output: Contribution to journalArticle

    9 Citations (Scopus)

    Abstract

    The cation-independent mannose-6-phosphate/insulin-like growth factor II receptor has been observed to bind to soluble forms of glycosyl-phosphatidylinositol-linked molecules, one of mammalian origin (rat Thy-1) and two of protozoan origins. Of the two phosphate groups found on the soluble forms of the protozoan glycosyl-phosphatidylinositol-linked molecules: (i) the internal mannose-6-phosphate diester (which forms a part of the ethanolamine bridge) and (ii) the inositol-1,2 cyclic phosphate group (which arises after cleavage of the membrane associated form with phosphatidylinositol-specific phospholipase C), only the former appears to be recognized by the mannose-6-phosphate/insulin-like growth factor II receptor, as mild acid hydrolysis which destroys the latter has been observed not to affect the receptor binding site.
    Original languageEnglish
    Pages (from-to)34-38
    Number of pages5
    JournalFEBS Letters
    Volume360
    Issue number1
    DOIs
    Publication statusPublished - 20 Feb 1995

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