# Nuclear pore complex protein RANBP2 and related SUMOylation in solid malignancies

## TL;DR

This paper reviews the role of RANBP2, a nuclear pore protein involved in SUMOylation, in cancer and its potential as a therapeutic target.

## Contribution

Highlights RANBP2 as a novel and underexplored SUMO E3 ligase with relevance in solid tumor development.

## Key findings

- RANBP2 is a key player in SUMOylation and cell cycle regulation in cancer.
- Its role in tumorigenesis suggests potential as a therapeutic target.
- More research is needed to validate its clinical applicability in cancer treatment.

## Abstract

The growing interest in post-translational protein modification, particularly in SUMOylation, is driven by its crucial role in cell cycle regulation. SUMOylation affects various cell cycle regulators, including oncogenes, suggesting its relevance in cancer. SUMO E3 ligases are pivotal in this process, exhibiting diverse functionalities through structural domains and subcellular localizations. A less-explored SUMO E3 ligase, RANBP2, a component of the vertebrate nuclear pore complex, emerges as a central player in cellular cycle processes, as well as in tumorigenesis. The current studies illuminate the importance of RANBP2 and underscore the need for more extensive studies to validate its clinical applicability in neoplastic interventions. Our review elucidates the significance of RANBP2 across various types of malignancies. Additionally, it delves into exploring RANBP2 as a prospective therapeutic target for cancer treatment, offering insights into the avenues that scholars should pursue in their subsequent research endeavors. Thus, further investigation into RANBP2's role in solid tumorigenesis is eagerly awaited.