Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 710, Issue -, Pages -Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2021.108999
Keywords
Tropomyosin; Neuronal isoforms; Actin filaments; Circular dichroism; Differential scanning calorimetry; Optical trap
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Funding
- Russian Science Foundation [18-74-10099]
- Russian Science Foundation [18-74-10099] Funding Source: Russian Science Foundation
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This study investigated the properties of five low molecular weight Tpm isoforms and found significant differences in their sequences variations in alternatively spliced regions, which may be important for further research on the organization and dynamics of the cytoskeleton.
Tropomyosin (Tpm) is an actin-associated protein and key regulator of actin filament structure and dynamics in muscle and non-muscle cells where it participates in many vital processes. Human non-muscle cells produce many Tpm isoforms; however, little is known yet about their structural and functional properties. In the present work, we have applied various methods to investigate the properties of five low molecular weight Tpm isoforms (Tpm3.1, Tpm3.2, Tpm3.4, Tpm3.5, and Tpm3.7), the products of TPM3 gene, which significantly differ by alternatively spliced internal exon 6 (6a or 6b) and C-terminal exon 9 (9a, 9c or 9d). Our results clearly demonstrate that the properties of these Tpm isoforms are quite different depending on sequence variations in alternatively spliced regions of their molecules. These differences can be important in further studies to explain why these Tpm isoforms play a key role in organization and dynamics of the cytoskeleton.
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