Suppression of tumor-related glycosylation of cell surface receptors by the 16-kDa membrane subunit of vacuolar H+-ATPase

The Journal of Biological Chemistry
M A Skinner, Alan G Wildeman

Abstract

The glycosylation of integrins and other cell surface receptors is altered in many transformed cells. Notably, an increase in the number of beta1,6-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 beta1,6 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 beta1,6 branching of beta(1) integrin and the epidermal growth factor receptor. Overexpression of 16K inhibits cell adhesion and invasion. 16K contains four hydrophobic membrane-spanning alpha-helices, and its ability to influence glycosylation is localized primarily within the second and fourth membrane-spanning alpha-helices. 16K also interacts directly with the transmembrane domain of beta(1) integrin, but its effects on glycosylation were independent of its binding to beta(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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Citations

Mar 27, 2007·Biochimica Et Biophysica Acta·Jiwei ChenYiu-mo Michael Chan
Jan 18, 2006·Nature Cell Biology·Andrés Hurtado-LorenzoVladimir Marshansky
Jan 13, 2009·Cellular Microbiology·Elena Fernández-ArenasRosalía Diez-Orejas
Jul 23, 2002·The Journal of Biological Chemistry·Takayuki TorigoeKimitoshi Kohno
Aug 8, 2008·The Journal of Immunology : Official Journal of the American Association of Immunologists·Maximiliano Gabriel GutierrezGareth Griffiths
Jul 21, 2012·The Journal of Biological Chemistry·Christin OstereschHelmut Wieczorek
Oct 31, 2003·Cancer Treatment Reviews·Hiroto IzumiKimitoshi Kohno
May 26, 2004·Biochimica Et Biophysica Acta·Susan L Bellis

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