Glycosylation of Tetraspanin Tspan-1 at Four Distinct Sites Promotes Its Transition Through the Endoplasmic Reticulum

Title: Glycosylation of Tetraspanin Tspan-1 at Four Distinct Sites Promotes Its Transition Through the Endoplasmic Reticulum

Volume: 16 Issue: 10

Author(s): Claus-Jurgen Scholz, Georg Sauer and Helmut Deissler

Affiliation:

Keywords: EGFP fusion proteins, ovarian carcinoma cells, glycosylation, Tetraspanins

Abstract: We showed that Tspan-1, a tetraspanin overexpressed in many human cancers, harbours oligosaccharides at all four potential N-glycosylation sites. Its most abundant form contained only mannose-rich sugar chains but two distinct glycosylation sites could also contain complex carbohydrates. Glycosylation seemed to be required for correct folding and subsequent transition through the endoplasmic reticulum.

Cite this article as:

Scholz Claus-Jurgen, Sauer Georg and Deissler Helmut, Glycosylation of Tetraspanin Tspan-1 at Four Distinct Sites Promotes Its Transition Through the Endoplasmic Reticulum, Protein & Peptide Letters 2009; 16 (10) . https://dx.doi.org/10.2174/092986609789071234