Journal
JOURNAL OF CELL BIOLOGY
Volume 209, Issue 1, Pages 143-162Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201407130
Keywords
-
Categories
Funding
- Bio & Medical Technology Development Program [2011-0030157]
- Basic Science Research Program [2012R1A2A1A03002115]
- National Research Foundation of Korea - Ministry of Education [2013R1A6A3A04064259]
- Cell Dynamics Research Center Program through the National Research Foundation grants - Ministry of Science, ICT (Imagination, Creativity, and Science Technology) and Future Planning, Korea
- Bio-Imaging Research Center at GIST
- Ministry of Science, ICT & Future Planning, Republic of Korea [IBS-R005-D1-2015-A00] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
- National Research Foundation of Korea [2013R1A6A3A04064259, 2012R1A2A1A03002115, 21A20131212125] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available