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  • Title: Targeting of MAL, a putative element of the apical sorting machinery, to glycolipid-enriched membranes requires a pre-golgi sorting event.
    Author: Puertollano R, Alonso MA.
    Journal: Biochem Biophys Res Commun; 1999 Jan 27; 254(3):689-92. PubMed ID: 9920802.
    Abstract:
    The MAL proteolipid is a nonglycosylated polytopic membrane protein with specific residence in glycolipid-enriched membrane (GEM) microdomains. MAL has been proposed as an element of the machinery for apical transport in polarized epithelial cells. Previous work demonstrated that MAL requires its four carboxyl-terminal amino acids to be targeted to GEMs. In the present work, we have engineered MAL with N-glycosylation consensus sequences to delimit the site at which commitment of MAL to access into GEMs takes place. Comparison of engineered MAL proteins bearing either an intact or a truncated carboxyl terminus revealed that whereas the former acquired endo H-sensitive and endo H-resistant mature glycosylation, the protein with a deleted carboxyl terminus did not. These results indicate that although MAL incorporation into GEMs takes place mainly in the Golgi, commitment of MAL to enter GEMs is a pre-Golgi event.
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