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- W2003990908 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." @default.
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- W2003990908 date "1999-01-01" @default.
- W2003990908 modified "2023-09-26" @default.
- W2003990908 title "Targeting of MAL, a Putative Element of the Apical Sorting Machinery, to Glycolipid-Enriched Membranes Requires a Pre-Golgi Sorting Event" @default.
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- W2003990908 doi "https://doi.org/10.1006/bbrc.1998.0122" @default.
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