TAGLN2 regulates T cell activation by stabilizing the actin cytoskeleton at the immunological synapse
Authors
Bo-Ra Na ; Hye-Ran Kim ; Indre Piragyte ; Hyun-Mee Oh ; Min-Sung Kwon ; Uroos Akber ; Hyun-Su Lee ; Do-Sim Park ; Woo Keun Son ; Zee-Yong Park ; Sin-Hyeog Im ; Mun-Chual Rho ; Young-Min Hyun ; Minsoo Kim ; Chang-Duk Jun
Citation
JOURNAL OF CELL BIOLOGY, Vol.209(1) : 143-162, 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.