Details

Autor(en) / Beteiligte

• Kim, Hye-Ran
• Kwon, Min-Sung
• Lee, Sangmin
• Mun, YeVin
• Lee, Kyung-Sik
• Kim, Chang-Hyun
• Na, Bo-Ra
• Kim, Bit Na Rae
• Piragyte, Indre
• Lee, Hyun-Su
• Jun, Youngsoo
• Jin, Mi Sun
• Hyun, Young-Min
• Jung, Hyun Suk
• Mun, Ji Young
• Jun, Chang-Duk

Titel

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

Ist Teil von

• Scientific reports, 2018-04, Vol.8 (1), p.5503-15, Article 5503

Ort / Verlag

England: Nature Publishing Group

Erscheinungsjahr

2018

Link zum Volltext

Quelle

Free E-Journal (出版社公開部分のみ）

Beschreibungen/Notizen

• 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.