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 PMID:25869671  

TAGLN2 regulates T cell activation by stabilizing the actin cytoskeleton at the immunological synapse.

Bo-Ra Na | Hye-Ran Kim | Indre Piragyte | Hyun-Mee Oh | Min-Sung Kwon | Uroos Akber | Hyun-Su Lee | Do-Sim Park | Woo Keun Song | Zee-Yong Park | Sin-Hyeog Im | Mun-Chual Rho | Young-Min Hyun | Minsoo Kim | Chang-Duk Jun
The Journal of cell biology | 2015

The formation of an immunological synapse (IS) requires tight regulation of actin dynamics by many actin polymerizing/depolymerizing proteins. However, the significance of actin stabilization at the IS remains largely unknown. In this paper, we identify a novel function of TAGLN2--an actin-binding protein predominantly expressed in T cells--in stabilizing cortical F-actin, thereby maintaining F-actin contents at the IS and acquiring LFA-1 (leukocyte function-associated antigen-1) activation after T cell receptor stimulation. TAGLN2 blocks actin depolymerization and competes with cofilin both in vitro and in vivo. Knockout of TAGLN2 (TAGLN2(-/-)) reduced F-actin content and destabilized F-actin ring formation, resulting in decreased cell adhesion and spreading. TAGLN2(-/-) T cells displayed weakened cytokine production and cytotoxic effector function. These findings reveal a novel function of TAGLN2 in enhancing T cell responses by controlling actin stability at the IS.

Pubmed ID: 25869671

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