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TAGLN2 polymerizes G-actin in a low ionic state but blocks Arp2/3-nucleated actin branching in physiological conditions
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 underst...
Autores principales: | , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5883021/ https://www.ncbi.nlm.nih.gov/pubmed/29615809 http://dx.doi.org/10.1038/s41598-018-23816-2 |
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author | 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 |
author_facet | 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 |
author_sort | Kim, Hye-Ran |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-5883021 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-58830212018-04-09 TAGLN2 polymerizes G-actin in a low ionic state but blocks Arp2/3-nucleated actin branching in physiological conditions 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 Sci Rep Article 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. Nature Publishing Group UK 2018-04-03 /pmc/articles/PMC5883021/ /pubmed/29615809 http://dx.doi.org/10.1038/s41598-018-23816-2 Text en © The Author(s) 2018 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article 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 TAGLN2 polymerizes G-actin in a low ionic state but blocks Arp2/3-nucleated actin branching in physiological conditions |
title | TAGLN2 polymerizes G-actin in a low ionic state but blocks Arp2/3-nucleated actin branching in physiological conditions |
title_full | TAGLN2 polymerizes G-actin in a low ionic state but blocks Arp2/3-nucleated actin branching in physiological conditions |
title_fullStr | TAGLN2 polymerizes G-actin in a low ionic state but blocks Arp2/3-nucleated actin branching in physiological conditions |
title_full_unstemmed | TAGLN2 polymerizes G-actin in a low ionic state but blocks Arp2/3-nucleated actin branching in physiological conditions |
title_short | TAGLN2 polymerizes G-actin in a low ionic state but blocks Arp2/3-nucleated actin branching in physiological conditions |
title_sort | tagln2 polymerizes g-actin in a low ionic state but blocks arp2/3-nucleated actin branching in physiological conditions |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5883021/ https://www.ncbi.nlm.nih.gov/pubmed/29615809 http://dx.doi.org/10.1038/s41598-018-23816-2 |
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