Proteasomes and Cellular Senescence: An Age-Related Connection
A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".
Deadline for manuscript submissions: 30 August 2024 | Viewed by 1025
Special Issue Editor
Special Issue Information
Dear Colleagues,
The proteasome complex is responsible for protein degradation and turnover. The proteasome consists of protein subunits arranged in a cylindrical structure with a hollow core. Proteasome comprises 19S regulatory particles, which recognize ubiquitinated substrates, and 20S core particles, which degrade them. The 20S core particle is the proteolytic component of the proteasome complex. Generally, polyubiquitinated substrates are recognized by intrinsic ubiquitin receptors present on the 19S (Rpn1, Rpn10, and Rpn13). The extrinsic receptors, also known as UBL-UBA shuttle proteins (Rad23, Dsk2, and Ddi1), interact with ubiquitinated proteins and deliver them to proteasome for degradation. However, several studies reported an age-related decline in proteasome activity. On the contrary, a high proteasome activity or level is crucial for cancer cell survival. As proteasome is a critical component in the protein quality control pathway, and various therapeutic modalities such as targeted protein degradation rely on this degradation machinery, identifying factors regulating proteolytic activity is fundamental in this field. It is important to note that the relationship between proteasome activity and aging is complex and multifaceted. Hence, this Special Issue aims to provide an overview of the current understanding of the age-dependent changes in proteasome activity, which could in turn help identify the key negative regulators of proteasome. This underlying insight could set a stage for future strategies to improve the effectiveness of targeted therapy and promote healthy aging, thereby reducing the risk of age-related diseases.
Potential topics include, but are not limited to, the following:
- Effect of protein aggregation on proteasome activity;
- Age-dependent decline in proteasome activity;
- Ubiquitin-dependent and -independent substrate regulation via proteasome;
- Intrinsic and extrinsic proteasome receptors;
- Signaling pathways regulating proteasome activity;
- Post-translational modification of proteasome subunits;
- Dysregulated protein turnover during aging.
Dr. Aniruddha Das
Guest Editor
Manuscript Submission Information
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Keywords
- proteasomes
- aging
- proteasome receptors
- post-translational modification
