Camsap2, short for calmodulin-regulated spectrin-associated protein 2, is a microtubule minus-end-targeting protein. It plays a crucial role in microtubule organization, participating in processes like microtubule nucleation, stabilization, and release from the γ-tubulin ring complex (γ-TuRC). It is involved in multiple signaling pathways such as Trio/Rac1, JNK/c-Jun, and TGF-β, and is of great biological importance in cell migration, polarity, and intracellular transport [2,3,6,7].

In hepatocellular carcinoma, Camsap2 is upregulated and drives metastasis by mediating noncentrosomal microtubule acetylation. Depletion of Camsap2 transforms the noncentrosomal microtubule array into a radial centrosomal pattern, impairing cell migration and invasion [1]. In colorectal cancer, high Camsap2 expression promotes cell migration, invasion, and metastasis through activation of the JNK/c-Jun/MMP-1 signaling pathway. Silencing Camsap2 leads to the opposite effects [3]. In lung cancer, Camsap2 enhances metastasis by mediating RASAL2 degradation, and its knockdown inhibits cell motility in vitro and metastasis in vivo [4]. In gastric cancer, high Camsap2 expression promotes invasion and metastasis possibly by upregulating TGF-β signaling to promote epithelial-mesenchymal transition (EMT) [6]. In Sertoli cells, Camsap2 knockdown promotes tight junction barrier function and blocks perfluorooctanesulfonate (PFOS)-induced cell injury by regulating microtubule and actin dynamics [5].

In conclusion, Camsap2 is essential for microtubule-related cellular functions. Gene knockout or knockdown models of Camsap2 in various cancer types and cell systems have revealed its oncogenic role in promoting cancer cell migration, invasion, and metastasis. These findings suggest that targeting Camsap2-mediated pathways could be a potential therapeutic strategy for treating related cancers [1,3,4,6].