# Harnessing Ribonucleoprotein Granule Biology for Cancer Therapy: The Central Role of Protein Modifications

## TL;DR

This paper explores how protein modifications affect RNP granules in cancer, offering insights for developing new cancer therapies.

## Contribution

The paper highlights the role of various protein modifications in RNP granule biology and their implications for cancer therapy.

## Key findings

- RNPs can undergo phosphorylation, ubiquitination, SUMOylation, methylation, crotonylation, and acetylation.
- Modifications on RNPs influence granule expression and function, impacting cancer treatment efficacy.
- Glycosylation, fucosylation, and PARylation on RNPs remain unreported in cancer research.

## Abstract

Aberrant expression or dysfunction of ribonucleoprotein (RNP) granules usually contribute to cancer initiation, progression, and therapeutic response. In the process, protein modification importantly mediates the interactions between cancer and RNPs/associated proteins. Therefore, we tried to summarize and discuss the complex interactions between RNPs and various protein modifications in cancers, facilitating the clinical translation of RNP-based therapies. Studies have shown that RNPs can directly undergo phosphorylation, ubiquitination, SUMOylation, methylation, crotonylation, and acetylation, but no studies have reported glycosylation, fucosylation, or PARylation on RNPs. These modifications can competitively occur on RNPs, affecting the RNP granule expression and function. Cancer cells, immune cells, and stromal cells can undergo RNP granule modifications, consequently mediating current treatment efficacy. These results provide the basis of RNP granule-based antitumor therapy. However, the structural complexity of RNPs and limited research depth pose significant key for clinical translation.