Mechanisms for regulating expression of membrane isoforms of FcγRIII (CD16)

Margaret L. Hibbs; Periasamy Selvaraj; Olli Carpén; Timothy A. Springer; Helmut Kuster; Marie Hélène E. Jouvin; Jean Pierre Kinet

doi:10.1126/science.2531918

Mechanisms for regulating expression of membrane isoforms of FcγRIII (CD16)

Margaret L. Hibbs, Periasamy Selvaraj, Olli Carpén, Timothy A. Springer, Helmut Kuster, Marie Hélène E. Jouvin, Jean Pierre Kinet

Immunology Alfred Hospital

Research output: Contribution to journal › Article › Research › peer-review

162 Citations (Scopus)

Abstract

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 γ subunit of the high affinity IgE Fc receptor (Fc∈RI). However, the CD16 sequence and not expression of the γ subunit is dominant in regulating PIG reanchoring.

Original language	English
Pages (from-to)	1608-1611
Number of pages	4
Journal	Science
Volume	246
Issue number	4937
DOIs	https://doi.org/10.1126/science.2531918
Publication status	Published - 1 Jan 1989

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abstract = "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 γ subunit of the high affinity IgE Fc receptor (Fc∈RI). However, the CD16 sequence and not expression of the γ subunit is dominant in regulating PIG reanchoring.",

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AU - Hibbs, Margaret L.

AU - Selvaraj, Periasamy

AU - Carpén, Olli

AU - Springer, Timothy A.

AU - Kuster, Helmut

AU - Jouvin, Marie Hélène E.

AU - Kinet, Jean Pierre

PY - 1989/1/1

Y1 - 1989/1/1

N2 - 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 γ subunit of the high affinity IgE Fc receptor (Fc∈RI). However, the CD16 sequence and not expression of the γ subunit is dominant in regulating PIG reanchoring.

AB - 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 γ subunit of the high affinity IgE Fc receptor (Fc∈RI). However, the CD16 sequence and not expression of the γ subunit is dominant in regulating PIG reanchoring.

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Mechanisms for regulating expression of membrane isoforms of FcγRIII (CD16)

Abstract

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