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Journal of Cell Science, Vol 105, Issue 3 831-840, Copyright © 1993 by Company of Biologists

JOURNAL ARTICLES

Carboxyl terminus structural requirements for glycosyl-phosphatidylinositol anchor addition to cell surface proteins

C Beghdadi-Rais, M Schreyer, M Rousseaux, P Borel, RJ Eisenberg, GH Cohen, C Bron and N Fasel
Institute of Biochemistry, University of Lausanne, Epalinges, Switzerland.

Glycosyl phosphatidylinositol (GPI)-anchored proteins contain in their COOH-terminal region a peptide segment that is thought to direct glycolipid addition. This signal has been shown to require a pair of small amino acids positioned 10-12 residues upstream of an hydrophobic C-terminal domain. We analysed the contribution of the region separating the anchor acceptor site and the C-terminal hydrophobic segment by introducing amino acid deletions and substitutions in the spacer element of the GPI-anchored Thy-1 glycoprotein. Deletions of 7 amino acids in this region, as well as the introduction of 2 charged residues, prevented the glycolipid addition to Thy-1, suggesting that the length and the primary sequence of the spacer domain are important determinants in the signal directing GPI anchor transfer onto a newly synthesized polypeptide. Furthermore, we tested these rules by creating a truncated form of the normally transmembranous Herpes simplex virus I glycoprotein D (gDI) and demonstrating that when its C-terminal region displays all the features of a GPI-anchored protein, it is able to direct glycolipid addition onto another cell surface molecule.
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© The Company of Biologists Ltd 1993