Binding of S100A6 to actin and the actin-tropomyosin complex

S100A6 is a low molecular weight Ca -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 bin...

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Bibliographic Details
Published in:Scientific reports 2020-07, Vol.10 (1), p.12824-12824, Article 12824
Main Authors: Jurewicz, Ewelina, Robaszkiewicz, Katarzyna, Moraczewska, Joanna, Filipek, Anna
Format: Article
Language:English
Subjects:
Actin
Actin Cytoskeleton - metabolism
Actin Cytoskeleton - physiology
Actins - metabolism
Animals
Calcium-binding protein
Fibroblasts
Filaments
Functional morphology
Gene expression
Isoforms
Mice
Microfilaments
Molecular weight
NIH 3T3 Cells
Protein Binding
Protein Isoforms
Proteins
S100 Calcium Binding Protein A6 - metabolism
Sedimentation & deposition
Tropomyosin
Tropomyosin - metabolism
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Summary:S100A6 is a low molecular weight Ca -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 -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.
ISSN:2045-2322
2045-2322
DOI:10.1038/s41598-020-69752-y