Comparative structural and functional studies of low molecular weight tropomyosin isoforms, the TPM3 gene products

Marchenko, Marina A.; Nefedova, Victoria V.; Yampolskaya, Daria S.; Borzova, Vera A.; Kleymenov, Sergey Y.; Nabiev, Salavat R.; Никитина, Л. В.; Matyushenko, Alexander M.; Levitsky, Dmitrii I.

doi:10.1016/j.abb.2021.108999

Cited by 6 publications

(7 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The stiffness of all thin filaments is statistically different from that of F-actin (Table 2). Comparing experimental data for thin filaments with other LMW cytoplasmic Tpm isoforms and TPM3 gene products [31], we can conclude that the Tpm1.8 and Tpm1.9 isoforms provide greater actin fiber stiffness. We can assume that such high bending stiffness parameters obtained for these isoforms may be associated with the very high affinity and strength of end-to-end interactions for the Tpm1.8 and Tpm1.9 isoforms.…”

Section: Functional Peculiarities Of Tpm18 and Tpm19 Complexes With F...mentioning

confidence: 87%

“…The solution viscosities of these isoforms are also much higher than those obtained for the isoforms of the TPM3 gene products (Tpm3.1, Tpm3.2. Tpm3.4, Tpm3.5, Tpm3.7) [31], as well as the Tpm4.2 isoform [33].…”

Section: Discussionmentioning

confidence: 98%

“…To study the structural properties of the Tpm1.8 and Tpm1.9 molecules, we used the DSC method. It can be noted that these isoforms have a common DSC profile characteristic for Tpm molecules [31][32][33]. In the profile, three domains can be distinguished, cooperatively melting in the temperature range from 30 to 70 • C. The presence of three calorimetric domains in the Tpm structure means that the molecule can be divided into three parts that melt cooperatively and independently of each other.…”

Section: Structural Properties Of Tpm18 and Tpm19 Isoformsmentioning

confidence: 99%

“…To study the stability of the F-actin complex with Tpm, we recorded changes in the light scattering upon heating. Usually, the stability of the complex with actin depends on the stability of the C-terminal part of the Tpm molecule, which is expressed by the coincidence of the melting temperatures of the 2nd calorimetric domain in the DSC profile and the dissociation temperature of the complex [31][32][33]. However, no such dependence was found for the Tpm1.8 or Tpm1.9 isoforms.…”

Section: Interaction Between F-actin and Tpm18 And Tpm19mentioning

confidence: 99%

See 3 more Smart Citations

Functional and Structural Properties of Cytoplasmic Tropomyosin Isoforms Tpm1.8 and Tpm1.9

Lapshina,

Nefedova,

Nabiev

et al. 2024

IJMS

Self Cite

View full text Add to dashboard Cite

The actin cytoskeleton is one of the most important players in cell motility, adhesion, division, and functioning. The regulation of specific microfilament formation largely determines cellular functions. The main actin-binding protein in animal cells is tropomyosin (Tpm). The unique structural and functional diversity of microfilaments is achieved through the diversity of Tpm isoforms. In our work, we studied the properties of the cytoplasmic isoforms Tpm1.8 and Tpm1.9. The results showed that these isoforms are highly thermostable and differ in the stability of their central and C-terminal fragments. The properties of these isoforms were largely determined by the 6th exons. Thus, the strength of the end-to-end interactions, as well as the affinity of the Tpm molecule for F-actin, differed between the Tpm1.8 and Tpm1.9 isoforms. They were determined by whether an alternative internal exon, 6a or 6b, was included in the Tpm isoform structure. The strong interactions of the Tpm1.8 and Tpm1.9 isoforms with F-actin led to the formation of rigid actin filaments, the stiffness of which was measured using an optical trap. It is quite possible that the structural and functional features of the Tpm isoforms largely determine the appearance of these isoforms in the rigid actin structures of the cell cortex.

show abstract

Section: Functional Peculiarities Of Tpm18 and Tpm19 Complexes With F...mentioning

confidence: 87%

Section: Discussionmentioning

confidence: 98%

Section: Structural Properties Of Tpm18 and Tpm19 Isoformsmentioning

confidence: 99%

Section: Interaction Between F-actin and Tpm18 And Tpm19mentioning

confidence: 99%

See 2 more Smart Citations

Functional and Structural Properties of Cytoplasmic Tropomyosin Isoforms Tpm1.8 and Tpm1.9

Lapshina,

Nefedova,

Nabiev

et al. 2024

IJMS

Self Cite

View full text Add to dashboard Cite

show abstract

“…The tropomyosin 3 (TPM3) gene is located in subband 1, band 3, region 2, long arm of chromosome 1(1q21.3). The TPM3 protein can interact with actin, affecting muscle cell contraction and other cytoskeletal activity (8,9). Meanwhile, TPM3 gene-related rearrangement has been widely reported in malignant tumors and other diseases, such as colorectal cancer, thyroid cancer, and lung cancer (10)(11)(12).…”

Section: Introductionmentioning

confidence: 99%

MiR-107 inhibits the malignant biological behavior of esophageal squamous cell carcinoma by targeting TPM3

Zhang¹,

Zhang²,

Jiang³

et al. 2022

J Gastrointest Oncol

View full text Add to dashboard Cite

Background: Esophageal squamous cell carcinoma (ESCC) is a highly lethal and aggressive tumor. Our previous study revealed that tropomyosin 3 (TPM3) is up-regulated in the late stage of ESCC and promotes epithelial-mesenchymal transition (EMT) via MMP2/MMP9. However, we have not yet explored the upstream regulator of TPM3. In this study, miR-107, a microRNA molecule, was predicted as an inhibitor targeting TPM3, and in vivo and in vitro experiments confirmed this hypothesis. Methods: Western blot and fluorescence quantitative polymerase chain reaction (qPCR) were applied to analyze the expression of miR-107 and TPM3. Flow cytometry, cell counting kit-8 (CCK8) assay, woundhealing assay, colony formation assay, transwell assay, and a BALB/c nude mouse (male, 8 weeks old, 20±2 g) model were used to detect the function of miR-107 and TPM3 in ESCC. Dual-luciferase assay was used to analyze the suppressed TPM3 expression induced by miR-107. Rescue experiments were also conducted in our research. Results:The cell and nude mouse models verified that TPM3 promotes proliferation, invasion and metastasis, and inhibits apoptosis, which is the opposite effect of miR-107 in ESCC. Meanwhile, the expression of TPM3 was up-regulated in the ESCC sample and cell lines, and miR-107 was down-regulated correspondingly. Dual-luciferase detection confirmed that miR-107 decreased the expression of TPM3 by targeting the 3'-untranslated region (3'-UTR) at the end of the TPM3 transcript. Further experiments verified that TPM3 could rescue the tumor suppression effect derived from miR-107.Conclusions: MiR-107 negatively regulates TPM3 expression and plays a tumor suppression role in ESCC.

show abstract

Simultaneous Identification and Species Differentiation of Major Allergen Tropomyosin in Crustacean and Shellfish by Infrared Spectroscopic Chemometrics

Luan

et al. 2023

Food Chemistry

View full text Add to dashboard Cite

Comparative structural and functional studies of low molecular weight tropomyosin isoforms, the TPM3 gene products

Cited by 6 publications

References 34 publications

Functional and Structural Properties of Cytoplasmic Tropomyosin Isoforms Tpm1.8 and Tpm1.9

Functional and Structural Properties of Cytoplasmic Tropomyosin Isoforms Tpm1.8 and Tpm1.9

MiR-107 inhibits the malignant biological behavior of esophageal squamous cell carcinoma by targeting TPM3

Simultaneous Identification and Species Differentiation of Major Allergen Tropomyosin in Crustacean and Shellfish by Infrared Spectroscopic Chemometrics

Contact Info

Product

Resources

About