Editorial: Cytoskeleton in the focus of anti-cancer therapy: In a search of novel biomarkers and combinatorial therapy approaches

Frontiers in Pharmacology, 2022

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DOI 10.3389/fphar.2022.1069821
Data confidence 70 medium
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Abstract

Cytoskeletal Components as Biomarkers and Targets for Anti-Cancer Therapy: How Treatment of the Cytoskeleton can Inhibit Tumor ProgressionThe development of targeted chemotherapy demands detailed molecular analysis of cancers to generate precision chemotherapy programs.While standard differential cancer diagnostic is based on the morphological features of cancer tissue with the inclusion of some molecular characteristics, a more comprehensive characterization of cancer cells focused on the upregulation or downregulation of specific proteins for highly efficient therapy is needed.In response to this demand, we collected this Special Issue.Analyzing actin cytoskeleton in the current volume, Dugina et al. discuss the differential expression of actin isoforms in cancer cells with emphasis on the correlation of expression profile with cancer cell motility.Epithelial cells express two major actin isoforms-β-actin and γ-actin with clear spatial separation between them.A growing body of evidence shows that elevated level of γ-actin directly correlates with enhanced cell motility and cancer progression.Of special interest might be the down-regulation of β-actin in tumor tissues.This raises a question about possible alternative regulation of actin isoforms during cancer development.Search for the factor(s) regulating actin isoform expression is of great interest and requires further investigation.In cancer cells, some signaling pathways may be altered or completely lost.This feature often results in the uncontrolled growth of cancer cells.Interestingly, alteration or loss of normal regulatory pathways could be used for anti-cancer therapy.One of the examples is the loss of substrate rigidity sensing discussed by Tijore et al. in the current volume.Several proteins, including tropomyosin 2.1, filamin A, and myosin IIA involved