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

 Hye-Ran Kim  ;  Min-Sung Kwon  ;  Sangmin Lee  ;  YeVin Mun  ;  Kyung-Sik Lee  ;  Chang-Hyun Kim  ;  Bo-Ra Na  ;  Bit Na Rae Kim  ;  Indre Piragyte  ;  Hyun-Su Lee  ;  Youngsoo Jun  ;  Mi Sun Jin  ;  Young-Min Hyun  ;  Hyun Suk Jung  ;  Ji Young Mun  ;  Chang-Duk Jun 
 Scientific Reports, Vol.8(1) : 5503, 2018 
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 Scientific Reports 
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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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1. College of Medicine (의과대학) > Dept. of Anatomy (해부학교실) > 1. Journal Papers
Yonsei Authors
Hyun, Young-Min(현영민) ORCID logo https://orcid.org/0000-0002-0567-2039
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