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Harnessing Ribonucleoprotein Granule Biology for Cancer Therapy: The Central Role of Protein Modifications
Dengxiong Li1, Qingxin Yu2,3, Ruicheng Wu4,5
1Department of Urology, The First Affiliated Hospital of Zhejiang Chinese Medical University (Zhejiang Provincial Hospital of Chinese Medicine), Hangzhou, China.
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.
Insights
Ribonucleoprotein (RNP) granule modifications, like phosphorylation and acetylation, impact cancer development and treatment. Understanding these protein modifications is key for advancing RNP-based cancer therapies.
Area of Science:
- Biochemistry
- Molecular Biology
- Oncology
Background:
- Aberrant ribonucleoprotein (RNP) granule expression and function are implicated in cancer initiation, progression, and treatment response.
- Protein modifications play a crucial role in mediating interactions between cancer and RNP granules or associated proteins.
Purpose of the Study:
- To summarize and discuss the intricate interactions between RNPs and various protein modifications within the context of cancer.
- To facilitate the clinical translation of RNP-based therapies by elucidating these complex molecular mechanisms.
Main Methods:
- Literature review and synthesis of existing studies on RNP modifications in cancer.
- Analysis of reported protein modifications affecting RNP granules, including phosphorylation, ubiquitination, SUMOylation, methylation, crotonylation, and acetylation.
- Identification of modifications not yet reported on RNPs, such as glycosylation, fucosylation, and PARylation.
Main Results:
- RNPs can undergo several types of protein modifications, including phosphorylation, ubiquitination, SUMOylation, methylation, crotonylation, and acetylation.
- These modifications can occur competitively on RNPs, influencing RNP granule expression and function.
- RNP granule modifications are observed in cancer cells, immune cells, and stromal cells, impacting therapeutic efficacy.
Conclusions:
- Protein modifications on RNP granules offer a basis for developing novel antitumor therapies.
- The structural complexity of RNPs and the current depth of research present significant challenges for clinical translation of RNP-based strategies.
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