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J. Biol. Chem., Vol. 276, Issue 51, 48451-48457, December 21, 2001

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Suppression of Tumor-related Glycosylation of Cell Surface Receptors by the 16-kDa Membrane Subunit of Vacuolar H⁺-ATPase^*

Mhairi A. Skinner and Alan G. Wildeman^§

From the Department of Molecular Biology and Genetics, University of Guelph, Guelph, Ontario N1G 2W1, Canada

The glycosylation of integrins and other cell surface receptors is altered in many transformed cells. Notably, an increase in the number of 1,6-branched N-linked oligosaccharides correlates strongly with invasive growth of cells. An ectopic expression of the Golgi enzyme N-acetylglucosaminyltransferase V (GlcNAc-TV), which forms 1,6 linkages, promotes metastasis of a number of cell types. It is shown here that the 16-kDa transmembrane subunit (16K) of vacuolar H⁺-ATPase suppresses 1,6 branching of ₁ integrin and the epidermal growth factor receptor. Overexpression of 16K inhibits cell adhesion and invasion. 16K contains four hydrophobic membrane-spanning -helices, and its ability to influence glycosylation is localized primarily within the second and fourth membrane-spanning -helices. 16K also interacts directly with the transmembrane domain of ₁ integrin, but its effects on glycosylation were independent of its binding to ₁ integrin. These data link cell surface tumor-related glycosylation to a component of the enzyme responsible for acidification of the exocytic pathway.

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