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Science 22 December 1989:
Vol. 246. no. 4937, pp. 1611 - 1613
DOI: 10.1126/science.2531919
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Articles

Science, Vol 246, Issue 4937, 1611-1613
Copyright © 1989 by American Association for the Advancement of Science

articles

Membrane anchoring of a human IgG Fc receptor (CD16) determined by a single amino acid

LL Lanier, S Cwirla, G Yu, R Testi, and JH Phillips

Becton Dickinson Monoclonal Center, Inc., Mountain View, CA 94043.

CD16 is a low-affinity immunoglobulin G (IgG) Fc receptor that is expressed on natural killer (NK) cells, granulocytes, activated macrophages, and some T lymphocytes. Two similar genes, CD16-I and CD16-II, encode membrane glycoproteins that are anchored by phosphatidylinositol (PI)-glycan and transmembrane polypeptides, respectively. The primary structural requirements for PI-linkage were examined by constructing a series of hybrid cDNA molecules. Although both cDNA's have an identical COOH-terminal hydrophobic segment, CD16-I has Ser203 whereas CD16-II has Phe203. Conversion of Phe to Ser in CD16-II permits expression of a PI-glycan-anchored glycoprotein, whereas conversion of Ser to Phe in CD16-I prevents PI-glycan linkage.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
NK Cells: Null No More.
L. L. Lanier (2007)
J. Immunol. 179, 3385-3388
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Identification of a Novel Fc{gamma}RIIIa{alpha}-Associated Molecule That Contains Significant Homology to Porcine Cathelin.
S. E. Sweeney and Y. B. Kim (2004)
J. Immunol. 172, 1203-1212
   Abstract »    Full Text »    PDF »
The IgG Binding Site of Human Fc[IMAGE]RIIIB Receptor Involves CC` and FG Loops of the Membrane-proximal Domain.
A. Tamm, A. Kister, K. U. Nolte, J. E. Gessner, and R. E. Schmidt (1996)
J. Biol. Chem. 271, 3659-3666
   Abstract »    Full Text »    PDF »


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