Cfl1, also known as cofilin, is a critical member of the actin depolymerizing factor (ADF) family. It plays a pivotal role in regulating actin cytoskeleton dynamics by cutting and depolymerizing actin filaments, which is essential for various biological events such as cell migration, proliferation, and maintaining the balance of immune responses [2]. It is also involved in pathways related to autophagy and metabolic reprogramming [3,4].

In chronic myeloid leukemia (CML), the expression of CFL1 was lower in patients compared to healthy controls but significantly upregulated after imatinib therapy. Lower CFL1 expression before treatment predicted a better response to imatinib, suggesting its role in CML response during therapy [1]. In hepatocellular carcinoma, CFL1 is highly expressed in sorafenib-insensitive patients and promotes serine synthesis and metabolism, impairing sorafenib sensitivity. Silencing CFL1 with nanoparticles enhanced the sensitivity of hepatocellular carcinoma to sorafenib [4]. In gastric cancer, CFL1 expression was increased in cancer tissues compared to marginal and normal tissues, and its down-regulation in AGS cells inhibited cell migration, indicating it may function as an oncogenic gene [5]. In primary Sjögren's syndrome, the migratory capacity of bone marrow mesenchymal stem cells was reduced, along with decreased CFL1 expression. Overexpression of CFL1 restored the migratory capacity by regulating CCR1 expression [6].

In conclusion, Cfl1 is crucial for maintaining normal cellular functions related to the actin cytoskeleton, cell migration, and proliferation. Its dysregulation is associated with multiple diseases including leukemia, liver cancer, gastric cancer, and autoimmune diseases. The study of Cfl1 in disease models provides insights into the underlying mechanisms of these diseases and potential therapeutic targets.