Dstn, also known as Destrin, is a member of the actin-depolymerizing factor family. It regulates actin dynamics by treadmilling actin filaments and increasing globular actin pools. This function is crucial for many biological processes such as cell migration, differentiation, and development [3]. It is also associated with various pathways like the Wnt/β-catenin signaling pathway [1].

In a study on rectal cancer, Dstn was found to be highly expressed and hypomethylated in radiation-resistant tissues. Knockdown of Dstn in vitro and in vivo promoted the sensitivity of colorectal cancer cells to radiation therapy, while overexpression promoted resistance. It was also shown that Dstn binds to β-catenin, activating the Wnt/β-catenin signaling pathway, which is related to radiotherapy resistance [1]. In cardiac-specific Snrk-/-mice, Snrk binds to Dstn. Dstn downregulation reverses excess DNA damage, changes in nuclear parameters, and cellular hypertrophy caused by Snrk knockdown. This indicates that Dstn-Snrk interaction is important in cardiac hypertrophy and DNA damage [2]. In Xenopus embryogenesis, depleting Dstn led to morphants with short body axes and small heads, and impaired cell migration during neurulation [3].

In conclusion, Dstn plays essential roles in cell migration, development, and in processes related to cancer radiotherapy resistance and cardiac hypertrophy. Studies using gene-knockout or knockdown models in mice and Xenopus have revealed these functions, providing valuable insights into the molecular mechanisms underlying various biological processes and diseases.