Immune Synapse Formation Requires ZAP-70 Recruitment by Ezrin and CD43 Removal by Moesin
The Journal of Cell Biology
PubMed Central® ID
Immunological synapse (IS) formation involves receptor-ligand pair clustering and intracellular signaling molecule recruitment with a coincident removal of other membrane proteins away from the IS. As microfilament-membrane linkage is critical to this process, we investigated the involvement of ezrin and moesin, the two ezrin/radixin/moesin proteins expressed in T cells. We demonstrate that ezrin and moesin, which are generally believed to be functionally redundant, are differentially localized and have important and complementary functions in IS formation. Specifically, we find that ezrin directly interacts with and recruits the signaling kinase ZAP-70 to the IS. Furthermore, the activation of ezrin by phosphorylation is essential for this process. In contrast, moesin dephosphorylation and removal, along with CD43, are necessary to prepare a region of the cell cortex for IS. Thus, ezrin and moesin have distinct and critical functions in the T cell cortex during IS formation.
Calcium, cytoskeletal proteins, jurkat cells, leukosialin, lymphocyte activation, microfilament proteins, mutation, phosphorylation, precipitin tests, RNA, recombinant proteins, spodoptera, transfection
Ilani, Tal; Khanna, Chand; Zhou, Ming; Veenstra, Timothy D.; and Bretscher, Anthony, "Immune Synapse Formation Requires ZAP-70 Recruitment by Ezrin and CD43 Removal by Moesin" (2007). Pharmaceutical Sciences Faculty Publications. 363.