About this Research Topic
Actin-binding proteins account for 20% of the total cellular proteins that can bind actin and regulate the functions of actin filaments. Accompanying the evolution of actin during three billion years, actin-binding proteins diverged in prokaryotes and eukaryotes, participating in multiple essential cellular processes such as proliferation, secretion, migration and contraction. New distinct biochemical and biological properties of these proteins have been found. For example, transgelin-2, previously regarded as a redundant protein, has recently been shown to relax the myosin cytoskeleton in airway smooth muscle cells by acting as a receptor. Espin is not only a metastatic regulator for melanoma but also a potential biomarker of disease progression.
Different actin-binding proteins have different structures; some proteins have acquired distinct crystal structures whereas others are considered intrinsically disordered proteins (IDP). The numerous emerging functions, complex underlying mechanisms and the special structures of actin-binding proteins has attracted the attention of current biological researchers and may provide key insights into actin-cytoskeletal regulation and corresponding drug development in the future.
This Research Topic aims to provide researchers with an exclusive platform to publish their latest discoveries in actin-binding proteins in addition to discussing the concerns and advances in the field through Reviews and Original Research articles. The collection is open to research covering all aspects of actin-binding proteins including, but not limited to:
• Evolution of actin binding proteins;
• Novel cellular and physiological functions of actin binding proteins;
• Biochemical and structural studies on actin binding proteins;
• Molecular mechanisms of actin binding protein in critical biological processes;
• Development of tools and techniques for actin binding proteins research.
Keywords: Actin-Binding Proteins, Function, Structure, Evolution, Transgelin-2
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