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MBC in Press, published online ahead of print January 31, 2007
Mol. Biol. Cell 10.1091/mbc.E05-11-1073

A more recent version of this article appeared on April 1, 2007
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Submitted on November 23, 2005
Revised on January 8, 2007
Accepted on January 24, 2007

Activated FPR and Fc{varepsilon}RI Occupy Common Domains for Signaling and Internalization

Mei Xue,*{dagger} Genie Hsieh,{ddagger} Mary Ann Raymond-Stintz,* Janet Pfeiffer,* Diana Roberts,{sect} Stanly L. Steinberg,{sect} Janet M. Oliver,* Eric R. Prossnitz,{dagger} Diane Lidke,* and Bridget S. Wilson*

*Department of Pathology and Cancer Research and Treatment Center, {dagger}Department of Cell Biology and Physiology, {sect}Department of Mathematics and Statistics, and {ddagger}Department of Electrical and Computer Engineering, University of New Mexico, Albuquerque, NM 87131

Monitoring Editor: Jennifer Lippincott-Schwartz

Immune cells display multiple cell surface receptors that integrate signals for survival, proliferation, migration and degranulation. Here, immunogold labeling is used to map the plasma membrane distributions of two separate receptors, the N-formyl peptide receptor (FPR) and the high-affinity IgE receptor (F{varepsilon}RI). We show that the FPR forms signaling clusters in response to monovalent ligand. These domains recruit Gi, followed by the negative regulatory molecule, arrestin2. There are low levels of colocalization of FPR with Fc{varepsilon}RI in unstimulated cells, shown by computer simulation to be a consequence of receptor density. Remarkably, there is a large increase in receptor coclustering when cells are simultaneously treated with fMLF and IgE plus polyvalent antigen. The close proximity of two active receptors may promote localized cross-talk, leading to enhanced IP3 production and secretion. Some cointernalization and trafficking of the two receptors can be detected by live cell imaging, but the bulk of FPR and Fc{varepsilon}RI segregate over time. This segregation is associated with more efficient internalization of cross-linked Fc{varepsilon}RI than of arrestin-desensitized FPR. The observation of receptors in lightly-coated membrane invaginations suggests that, despite the lack of caveolin, hematopoietic cells harbor caveolae-like structures that are candidates for nonclathrin mediated endocytosis.

Address correspondence to: Bridget S. Wilson (bwilson{at}salud.unm.edu)






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