Ranbp10, also known as RAN binding protein 10, is an evolutionarily conserved and ubiquitously expressed protein. It functions as a RAN-GTP exchange factor (GEF), regulating factors involved in cellular progression. It is associated with pathways like the FBXW7/c-Myc pathway and is involved in processes such as cell proliferation, migration, and invasion. Genetic models are valuable for studying its functions [1,2].

In glioblastoma (GBM), Ranbp10 was found to be overexpressed, and high expression was linked to poor patient survival. Downregulation of Ranbp10 in GBM cells significantly inhibited cell proliferation, migration, invasion, and tumor growth. It was also shown to suppress the promoter activity of FBXW7, increasing the protein stability of c-Myc in GBM cells. Silencing of FBXW7 in Ranbp10-knockdown GBM cells could partly reverse the effects of Ranbp10 downregulation [1]. In mice lacking Ranbp10, there were altered microtubule equilibrium and impaired thrombus stability. Ranbp10-nullizygous platelets had normal adhesion but impaired stable thrombi formation. The lack of Ranbp10 led to increased β1-tubulin protein, driving α-monomers into polymerized microtubules, and agonists failed to contract the peripheral marginal band or centralize granules in mutant platelets [3]. Mutant mice with Ranbp10 deficiency also had normal platelet counts, but resting platelets had an increased geometric axis ratio, microtubule filament disorders, a prolonged bleeding time, and reduced granule release [4].

In conclusion, Ranbp10 plays essential roles in multiple biological processes. Its overexpression promotes glioblastoma progression through the FBXW7/c-Myc axis. In vivo studies using Ranbp10-deficient mice have revealed its crucial role in maintaining microtubule dynamics related to platelet shape and function, and in thrombus stability. These findings contribute to understanding diseases such as glioblastoma and platelet-related disorders [1,3,4].