
Molecular editing of cellular responses by the high-affinity receptor for IgE.
Cellular responses elicited by cell surface receptors differ according to stimulus strength. We investigated how the high-affinity receptor for immunoglobulin E (IgE) modulates the response of mast cells to a high- or low-affinity stimulus. Both high- and low-affinity stimuli elicited similar receptor phosphorylation; however, differences were observed in receptor cluster size, mobility, distribution, and the cells' effector responses. Low-affinity stimulation increased receptor association with the Src family kinase Fgr and shifted signals from the adapter LAT1 to the related adapter LAT2. LAT1-dependent calcium signals required for mast cell degranulation were dampened, but the role of LAT2 in chemokine production was enhanced, altering immune cell recruitment at the site of inflammation. These findings uncover how receptor discrimination of stimulus strength can be interpreted as distinct in vivo outcomes.
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Related Subject Headings
- src-Family Kinases
- Receptors, IgE
- Proto-Oncogene Proteins
- Phosphoproteins
- Mice
- Membrane Proteins
- Mast Cells
- Inflammation
- Immunoglobulin E
- General Science & Technology
Citation

Published In
DOI
EISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- src-Family Kinases
- Receptors, IgE
- Proto-Oncogene Proteins
- Phosphoproteins
- Mice
- Membrane Proteins
- Mast Cells
- Inflammation
- Immunoglobulin E
- General Science & Technology