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The Journal of Immunology, 2002, 168: 541-544.
Copyright © 2002 by The American Association of Immunologists

Cutting Edge

Cutting Edge: Negative Regulation of Immune Synapse Formation by Anchoring Lipid Raft to Cytoskeleton Through Cbp-EBP50-ERM Assembly1

Katsuhiko Itoh2,*,{dagger}, Masahiro Sakakibara2,*,{dagger}, Sho Yamasaki*, Arata Takeuchi*, Hisashi Arase3,*, Masaru Miyazaki{dagger}, Nobuyuki Nakajima{dagger}, Masato Okada§ and Takashi Saito4,*,{ddagger}

* Department of Molecular Genetics and {dagger} General Surgery, Graduate School of Medicine, Chiba University, Chiba, Japan; and {ddagger} Cell Signaling Team, RIKEN Research Center of Allergy and Immunology, and § Department of Oncogene Research, Research Institute for Microbial Diseases, Osaka University, Suita City, Osaka, Japan

Ag recognition by T lymphocytes induces immune synapse formation and recruitment of signaling molecules into a lipid raft. Cbp/PAG is a Csk-associated membrane adapter protein exclusively localized in a lipid raft. We identified NHERF/EBP50 as a Cbp-binding molecule, which connects the membrane raft and cytoskeleton by binding to both Cbp through its PDZ domain and ezrin-radixin-moesin through the C terminus. Overexpression of Cbp reduced the mobility of the raft on the cell surface of unstimulated T cells and prevented synapse formation and subsequent T cell activation, whereas a mutant incapable of EBP50 binding restored both synapse formation and activation. These results suggest that anchoring of lipid raft to the cytoskeleton through Cbp-EBP50-ezrin-radixin-moesin assembly regulates membrane dynamism for synapse formation and T cell activation.




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