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Binding of S100A6 to actin and the actin–tropomyosin complex
S100A6 is a low molecular weight Ca(2+)-binding protein belonging to the S100 family. Many reports indicate that in the cell S100A6 has an influence on the organization of actin filaments, but so far no direct interaction between S100A6 and actin has been shown. In the present study we investigated...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7393103/ https://www.ncbi.nlm.nih.gov/pubmed/32733033 http://dx.doi.org/10.1038/s41598-020-69752-y |
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author | Jurewicz, Ewelina Robaszkiewicz, Katarzyna Moraczewska, Joanna Filipek, Anna |
author_facet | Jurewicz, Ewelina Robaszkiewicz, Katarzyna Moraczewska, Joanna Filipek, Anna |
author_sort | Jurewicz, Ewelina |
collection | PubMed |
description | S100A6 is a low molecular weight Ca(2+)-binding protein belonging to the S100 family. Many reports indicate that in the cell S100A6 has an influence on the organization of actin filaments, but so far no direct interaction between S100A6 and actin has been shown. In the present study we investigated binding of S100A6 to actin and the actin–tropomyosin complex. The analyses were performed on G- and F-actin and two tropomyosin isoforms—Tpm1.6 and Tpm1.8. Using purified proteins and a variety of biochemical approaches we have shown that, in a Ca(2+)-bound form, S100A6 directly interacts with G- and F-actin and with tropomyosin, preferentially with isoform Tpm1.8. S100A6 and tropomyosin bind to the same population of filaments and the presence of tropomyosin on the microfilament facilitates the binding of S100A6. By applying proximity ligation assay we have found that in NIH3T3 fibroblasts S100A6 forms complexes both with actin and with tropomyosin. These results indicate that S100A6, through direct interactions with actin and tropomyosin, might regulate the organization and functional properties of microfilaments. |
format | Online Article Text |
id | pubmed-7393103 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-73931032020-08-03 Binding of S100A6 to actin and the actin–tropomyosin complex Jurewicz, Ewelina Robaszkiewicz, Katarzyna Moraczewska, Joanna Filipek, Anna Sci Rep Article S100A6 is a low molecular weight Ca(2+)-binding protein belonging to the S100 family. Many reports indicate that in the cell S100A6 has an influence on the organization of actin filaments, but so far no direct interaction between S100A6 and actin has been shown. In the present study we investigated binding of S100A6 to actin and the actin–tropomyosin complex. The analyses were performed on G- and F-actin and two tropomyosin isoforms—Tpm1.6 and Tpm1.8. Using purified proteins and a variety of biochemical approaches we have shown that, in a Ca(2+)-bound form, S100A6 directly interacts with G- and F-actin and with tropomyosin, preferentially with isoform Tpm1.8. S100A6 and tropomyosin bind to the same population of filaments and the presence of tropomyosin on the microfilament facilitates the binding of S100A6. By applying proximity ligation assay we have found that in NIH3T3 fibroblasts S100A6 forms complexes both with actin and with tropomyosin. These results indicate that S100A6, through direct interactions with actin and tropomyosin, might regulate the organization and functional properties of microfilaments. Nature Publishing Group UK 2020-07-30 /pmc/articles/PMC7393103/ /pubmed/32733033 http://dx.doi.org/10.1038/s41598-020-69752-y Text en © The Author(s) 2020 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 Jurewicz, Ewelina Robaszkiewicz, Katarzyna Moraczewska, Joanna Filipek, Anna Binding of S100A6 to actin and the actin–tropomyosin complex |
title | Binding of S100A6 to actin and the actin–tropomyosin complex |
title_full | Binding of S100A6 to actin and the actin–tropomyosin complex |
title_fullStr | Binding of S100A6 to actin and the actin–tropomyosin complex |
title_full_unstemmed | Binding of S100A6 to actin and the actin–tropomyosin complex |
title_short | Binding of S100A6 to actin and the actin–tropomyosin complex |
title_sort | binding of s100a6 to actin and the actin–tropomyosin complex |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7393103/ https://www.ncbi.nlm.nih.gov/pubmed/32733033 http://dx.doi.org/10.1038/s41598-020-69752-y |
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