Abstract
Abstract Microvilli are abundant on the surfaces of circulating lymphocytes. However, factors that regulate microvilli formation on lymphocytes are not completely understood. Moreover, definitive roles of microvilli have not been fully addressed. Here we identified that TAGLN2—an actin-binding protein predominantly expressed in T cells— specifically localizes at the microvilli on T cells. Ectopic expression of TAGLN2 enhanced microvilli protrusion at the initial development of immunological synapse, and the opposite results were obtained by TAGLN2 depletion. Obviously, T-cell activation was influenced by the microvilli structures on T cells. Of interest was that TAGLN2 blocks Arp2/3 complex binding to actin filaments that leads to the inhibition of actin branch. Electron microscopy-based helical image analysis revealed that the main sites of TAGLN2 binding on actin share the Arp2/3 complex binding sites. These results demonstrate a novel function of TAGLN2 that contributes to enhance T-cell antigen recognition, and hence T-cell activation.
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