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Updated: May 2, 2026

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
Published on: July 5, 2018
IgG1 cytoplasmic tail is essential for cell surface expression in Igβ down-regulated cells
Kagefumi Todo1, Orie Koga1, Miwako Nishikawa1
1Center for Innovation in Immunoregulative Technology and Therapeutics, Graduate School of Medicine, Kyoto University, Yoshidakonoecho, Sakyoku, Kyoto 606-8501, Japan.
The IgG1 B cell receptor's (BCR) cytoplasmic tail is crucial for T-dependent immune responses. Phosphorylation of a tyrosine residue on the IgG cytoplasmic tail regulates BCR surface expression, especially when signaling molecules are down-regulated.
Area of Science:
- Immunology
- Molecular Biology
- Cell Signaling
Background:
- Cytoplasmic tails of B cell receptors (BCRs) are vital for immune responses.
- Tyrosine phosphorylation in IgG2a BCR cytoplasmic tails modulates signaling.
Purpose of the Study:
- To investigate if IgG cytoplasmic tail phosphorylation regulates BCR surface expression.
- To analyze the role of tyrosine residues in IgG1 BCR surface expression.
Main Methods:
- Established and analyzed cell lines expressing wild-type and mutated IgG1 BCR.
- Utilized A20 B cell line and non-B lineage cells.
- Investigated Igβ-down-regulated B cell lines.
Main Results:
- IgG1 BCR expression was normal on A20 cells, irrespective of the cytoplasmic tail.
- Mutated IgG1 BCR (tyrosine to glutamic acid mimic) showed highest surface expression on non-B cells and Igβ-down-regulated B cells.
Conclusions:
- The tyrosine residue in the IgG cytoplasmic tail is essential for efficient IgG BCR surface expression.
- This regulation is particularly important when BCR-associated signaling molecules, like Igβ, are down-regulated.
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