TAGLN2 polymerizes G-actin in a low ionic state but blocks Arp2/3-nucleated actin branching in physiological conditions.

Autor:	Kim HR; School of Life Sciences, GIST, Gwangju, 61005, Korea.; Immune Synapse and Cell Therapy Research Center, GIST, Gwangju, 61005, Korea., Kwon MS; School of Life Sciences, GIST, Gwangju, 61005, Korea.; World Institute of Kimchi, Gwangju, 61755, Korea., Lee S; Department of Biochemistry, College of Natural Sciences, Kangwon National University, 1, Kangwondaehak-gil, Chuncheon-si, Gangwon-do, 24341, Korea., Mun Y; School of Life Sciences, GIST, Gwangju, 61005, Korea.; Immune Synapse and Cell Therapy Research Center, GIST, Gwangju, 61005, Korea., Lee KS; School of Life Sciences, GIST, Gwangju, 61005, Korea.; Immune Synapse and Cell Therapy Research Center, GIST, Gwangju, 61005, Korea., Kim CH; School of Life Sciences, GIST, Gwangju, 61005, Korea.; Immune Synapse and Cell Therapy Research Center, GIST, Gwangju, 61005, Korea., Na BR; School of Life Sciences, GIST, Gwangju, 61005, Korea.; Immune Synapse and Cell Therapy Research Center, GIST, Gwangju, 61005, Korea., Kim BNR; School of Life Sciences, GIST, Gwangju, 61005, Korea., Piragyte I; School of Life Sciences, GIST, Gwangju, 61005, Korea.; Immune Synapse and Cell Therapy Research Center, GIST, Gwangju, 61005, Korea., Lee HS; School of Life Sciences, GIST, Gwangju, 61005, Korea.; Immune Synapse and Cell Therapy Research Center, GIST, Gwangju, 61005, Korea., Jun Y; School of Life Sciences, GIST, Gwangju, 61005, Korea., Jin MS; School of Life Sciences, GIST, Gwangju, 61005, Korea., Hyun YM; Department of Anatomy, Yonsei University College of Medicine, Seoul, 03722, Korea., Jung HS; Department of Biochemistry, College of Natural Sciences, Kangwon National University, 1, Kangwondaehak-gil, Chuncheon-si, Gangwon-do, 24341, Korea., Mun JY; Department of Biomedical Laboratory Science, College of Health Science, Eulji University, Seongnam-si, Gyeonggi-do, 13135, Korea. mjy1026@gmail.com.; Department of Structure and Function of Neural Network, Korea Brain Research Institute, Dong-gu, Daegu, Korea. mjy1026@gmail.com., Jun CD; School of Life Sciences, GIST, Gwangju, 61005, Korea. cdjun@gist.ac.kr.; Immune Synapse and Cell Therapy Research Center, GIST, Gwangju, 61005, Korea. cdjun@gist.ac.kr.
Jazyk:	angličtina
Zdroj:	Scientific reports [Sci Rep] 2018 Apr 03; Vol. 8 (1), pp. 5503. Date of Electronic Publication: 2018 Apr 03.
DOI:	10.1038/s41598-018-23816-2
Abstrakt:	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.
Databáze:	MEDLINE
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