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- W2801471226 abstract "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." @default.
- W2801471226 created "2018-05-17" @default.
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- W2801471226 date "2018-04-03" @default.
- W2801471226 modified "2023-10-16" @default.
- W2801471226 title "TAGLN2 polymerizes G-actin in a low ionic state but blocks Arp2/3-nucleated actin branching in physiological conditions" @default.
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- W2801471226 doi "https://doi.org/10.1038/s41598-018-23816-2" @default.
- W2801471226 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5883021" @default.
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