Two forms of the low-affinity Fc receptor for IgE differentially mediate endocytosis and phagocytosis: identification of the critical cytoplasmic domains.

Abstract:

:We have previously identified two species of the low-affinity human Fc receptor for IgE, Fc epsilon RIIa and Fc epsilon RIIb, which differ only in a short stretch of amino acids at the N-terminal cytoplasmic end. Their differential expressions on B cells and monocytes suggest that Fc epsilon RIIa and Fc epsilon RIIb are involved in B-cell function and IgE-mediated immunity, respectively. Here we show that Fc epsilon RII-mediated endocytosis is observed only in Fc epsilon RIIa-expressing cells, whereas IgE-dependent phagocytosis is observed only in Fc epsilon RIIb-expressing cells, demonstrating the functional difference between Fc epsilon RIIa and Fc epsilon RIIb. Furthermore, site-directed mutagenesis revealed that the tyrosine residue in the Fc epsilon RIIa-specific region is important for endocytosis, and the Asn-Pro residues in the Fc epsilon RIIb-specific region are required for phagocytosis. These findings suggest that endocytosis and phagocytosis are functionally separable phenomena involving distinct amino acid residues.

authors

Yokota A,Yukawa K,Yamamoto A,Sugiyama K,Suemura M,Tashiro Y,Kishimoto T,Kikutani H

doi

10.1073/pnas.89.11.5030

keywords:

subject

Has Abstract

pub_date

1992-06-01 00:00:00

pages

5030-4

issue

11

eissn

0027-8424

issn

1091-6490

journal_volume

89

pub_type

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