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Abstract
TAGLN is an actin-binding protein family that comprises three isoforms with theorized roles in smooth muscle differentiation, tumour development, lymphocyte activation, and brain chemistry. However, their fundamental characteristics in regulation of the actin-based cytoskeleton are not fully understood. Here we show that TAGLN2 (including TAGLN1 and TAGLN3) extensively nucleates G-actin polymerization under low-salt conditions, where polymerization would be completely suppressed. The calponin homology domain and actin-binding loop are essential to mechanically connect two adjacent G-actins, thereby mediating multimeric interactions. However, TAGLN2 blocked the Arp2/3 complex binding to actin filaments under physiological salt conditions, thereby inhibiting branched actin nucleation. In HeLa and T cells, TAGLN2 enhanced filopodium-like membrane protrusion. Collectively, the dual functional nature of TAGLN2—G-actin polymerization and Arp2/3 complex inhibition—may account for the mechanisms of filopodia development at the edge of Arp2/3-rich lamellipodia in various cell types.
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Details
1 School of Life Sciences, GIST, Gwangju, Korea; Immune Synapse and Cell Therapy Research Center, GIST, Gwangju, Korea
2 School of Life Sciences, GIST, Gwangju, Korea; World Institute of Kimchi, Gwangju, Korea
3 Department of Biochemistry, College of Natural Sciences, Kangwon National University, 1, Kangwondaehak-gil, Chuncheon-si, Gangwon-do, Korea
4 School of Life Sciences, GIST, Gwangju, Korea
5 Department of Anatomy, Yonsei University College of Medicine, Seoul, Korea
6 Department of Biomedical Laboratory Science, College of Health Science, Eulji University, Seongnam-si, Gyeonggi-do, Korea; Department of Structure and Function of Neural Network, Korea Brain Research Institute, Dong-gu, Daegu, Korea