Twinfilin-2 (TWF2)

Twinfilin-2 (TWF2) is an evolutionarily conserved actin-binding protein characterized by two ADF-H (actin-depolymerizing factor homology) domains, which confer its ability to bind actin monomers and heterodimeric capping protein with high affinity[1][3]. TWF2 is structurally and functionally similar to Twinfilin-1, but multiple isoforms of Twinfilin-2 exist that are differentially expressed in tissues—one form is predominant in non-muscle tissues, while another is muscle-specific[1]. TWF2 plays a crucial role in regulating dynamic cytoskeletal rearrangements by capping the barbed ends of actin filaments, sequestering actin monomers (especially ADP-G-actin), and facilitating the proper turnover and assembly of actin networks[1][3]. In neuronal cells, TWF2 is a critical regulator of neurite extension and dendritic spine morphology, influencing synaptic connectivity and brain architecture[2]. Genetic and proteomic studies implicate TWF2 in both neurodevelopmental processes and neurodegenerative diseases such as Alzheimer’s disease[2]. Currently, TWF2 is not an established direct therapeutic target, and no drugs are known to interact with it; rather, it serves as a key cytoskeletal regulator with potential relevance as a biomarker for synaptic health[2].

Other names

Twinfilin actin binding protein 2PTK9LMSTP011hA6RPA6RPA6rA6-related proteinProtein tyrosine kinase 9-likeTwinfilin-1-like protein