Pharmaceutical Sciences Faculty Publications

Immune Synapse Formation Requires ZAP-70 Recruitment by Ezrin and CD43 Removal by Moesin

Document Type

Article

Publication Date

11-19-2007

Journal Title

The Journal of Cell Biology

ISSN

1540-8140

Volume

179

Issue

4

First Page

733

Last Page

746

DOI

10.1083/jcb.200707199

PubMed ID

18025306

PubMed Central® ID

PMC2080902

Abstract

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.

Keywords

Calcium, cytoskeletal proteins, jurkat cells, leukosialin, lymphocyte activation, microfilament proteins, mutation, phosphorylation, precipitin tests, RNA, recombinant proteins, spodoptera, transfection

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