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Science 22 December 1989:
Vol. 246. no. 4937, pp. 1608 - 1611
DOI: 10.1126/science.2531918
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Articles
Science, Vol 246, Issue 4937, 1608-1611
Copyright © 1989 by American Association for the Advancement of Science
Mechanisms for regulating expression of membrane isoforms of Fc gamma RIII (CD16)
ML Hibbs,
P Selvaraj,
O Carpen,
TA Springer,
H Kuster,
MH Jouvin,
and
JP Kinet
Department of Pathology, Harvard Medical School, Boston, MA 02115.
Granulocyte and natural killer (NK) cell Fc receptors for immunoglobulin G (CD16) differ in only a few amino acids, yet have phosphatidylinositol glycan (PIG) or polypeptide membrane anchors, respectively. Mutagenesis shows that anchoring is regulated by a serine residue near the PIG anchor attachment site in the extracellular domain. The NK cell isoform was not expressed on the surface of COS cells unless cotransfected with a subunit that was expressed in NK cells and that was identical to the gamma subunit of the high affinity IgE Fc receptor (Fc epsilon RI). However, the CD16 sequence and not expression of the gamma subunit is dominant in regulating PIG reanchoring.
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