Visualizing the in vitro assembly of tropomyosin/actin filaments using TIRF microscopy

Janco, Miro; Dedova, Irina; Bryce, Nicole S.; Hardeman, Edna C.; Gunning, Peter W.

doi:10.1007/s12551-020-00720-6

Cited by 8 publications

(3 citation statements)

References 56 publications

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“…Tpm4 is one gene type of tropomyosin isoforms. Tropomyosin is a major regulatory protein of cytoskeleton and is localized along actin filaments modulating the interaction of actin and myosin (Khaitlina, 2015;Janco et al, 2020). As illustrated in Figure 6D, the level of TPM4 was decreased in CCNY downregulating cells and enhanced in CCNY upregulated cells.…”

Section: Ccnyc/pftk1 Complex Modulates Intracellular Cytoskeleton Via Tpm4mentioning

confidence: 93%

Cytoplasmic Localization Isoform of Cyclin Y Enhanced the Metastatic Ability of Lung Cancer via Regulating Tropomyosin 4

Zhao

Jiang

Teng

et al. 2021

Front. Cell Dev. Biol.

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Cyclin Y (CCNY) is a novel cyclin and highly conserved in metazoan species. Previous studies from our and other laboratory indicate that CCNY play a crucial role in tumor progression. There are two CCNY isoform which has different subcellular distributions, with cytoplasmic isoform (CCNYc) and membrane distribution isoform (CCNYm). However, the expression and function of CCNY isoforms is still unclear. We firstly found CCNYc was expressed in natural lung cancer tissue and cells through the subcellular distribution. Co-IP and immunofluorescence showed that both CCNYm and CCNYc could interact with PFTK1. Further studies illustrated that CCNYc but not CCNYm enhanced cell migration and invasion activity both in vivo and vitro. The function of CCNYc could be inhibited by suppression of PFTK1 expression. In addition, our data indicated that tropomyosin 4 (TPM4), a kind of actin-binding proteins, was down-regulated by suppression of CCNY. F-actin assembly could be controlled by CCNYc as well as PFTK1 and TPM4. As a result, CCNY was mainly expressed in lung cancer. CCNYc could promote cell motility and invasion. It indicated that CCNYc/PFTK1 complex could promote cell metastasis by regulating the formation of F-actin via TPM4.

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Section: Ccnyc/pftk1 Complex Modulates Intracellular Cytoskeleton Via Tpm4mentioning

confidence: 93%

Cytoplasmic Localization Isoform of Cyclin Y Enhanced the Metastatic Ability of Lung Cancer via Regulating Tropomyosin 4

Zhao

Jiang

Teng

et al. 2021

Front. Cell Dev. Biol.

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“…In addition to the above discussed proteins, numerous other actin partners are involved in the assembly and regulation of actin bundles. Among the most notable, no less than 40 human tropomyosin isoforms orchestrate the dynamics and accessibility of actin to severing and treadmilling [ 379 ]. In coordination with tropomyosin, tropomodulin caps and halts the dynamics at filaments pointed ends [ 380 ].…”

Section: Assembly and Disassembly Of Actin Bundlesmentioning

confidence: 99%

Actin Bundles Dynamics and Architecture

2023

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Cells use the actin cytoskeleton for many of their functions, including their division, adhesion, mechanosensing, endo- and phagocytosis, migration, and invasion. Actin bundles are the main constituent of actin-rich structures involved in these processes. An ever-increasing number of proteins that crosslink actin into bundles or regulate their morphology is being identified in cells. With recent advances in high-resolution microscopy and imaging techniques, the complex process of bundles formation and the multiple forms of physiological bundles are beginning to be better understood. Here, we review the physiochemical and biological properties of four families of highly conserved and abundant actin-bundling proteins, namely, α-actinin, fimbrin/plastin, fascin, and espin. We describe the similarities and differences between these proteins, their role in the formation of physiological actin bundles, and their properties—both related and unrelated to their bundling abilities. We also review some aspects of the general mechanism of actin bundles formation, which are known from the available information on the activity of the key actin partners involved in this process.

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“…The bulk of the scientific content of this Issue was constituted by twenty-two topical review articles that spanned different areas of cardiac research. Some particularly noteworthy examples dealt with growth factor directed therapy for cardiac muscle repair (White and Chong 2020 ); cardiomyocyte fluoresce-based microscopy methods (Janco et al 2020 ; Pandzic et al 2020 ; Hassan et al 2020 ); cellular mechano-transduction and shape determinants on cell growth regulation (Esfahani and Knöll 2020 ; Pruna and Ehler 2020 ; Harley et al 2020 ); synthetic biology approaches to the study of motor proteins (Linke et al 2020 ); use of plasma technology in surgical equipment surface treatment (Harley et al 2020 ); and the regulatory pathways and structural roles of profilin (Davey and Moens 2020 ).…”

Section: Highlights Of 2020mentioning

confidence: 99%