The ubiquitin-proteasome system (UPS) is a protein degradation system which is highly selective and depends on adenosine triphosphate (ATP) for energy supply in eukaryotic cells. About 80% of proteins are degraded by this system. UPS is composed of ubiquitin, E1 ubiquitin-activating enzymes, E2 ubiquitin-conjugating enzymes, E3 ubiquitin-ligase enzymes, 26S proteasome and deubiquitinases (DUBs). Similar to ubiquitination, SUMOylation is a post-transcriptional modification mediated by unique E1 and E2 ligases and multiple E3 ligases with consumption of ATP to conjugate the SUMOb- Small Ubiquitin-like Modifier - (SUMO1/2/3) small peptides to target proteins. SUMO proteins are similar to ubiquitin and are considered members of the ubiquitin-like protein family. Sumoylation can modify over 6,000 proteins involved in many physiological and pathological processes.
Ubiquitination/Ubiquitin-like modifications play an important role in various aspects of cellular processes, such as protein localization, metabolism, function, regulation and degradation. Ubiquitination and sumoylation have been widely involved in the regulation of crucial physiological processes, such as DNA damage repair, cell cycle, cell proliferation, apoptosis, cell differentiation, transcription regulation, signal transduction, vesicle transport, autophagy, immunity, etc. In addition, ubiquitination and sumoylation are involved in the pathological processes leading to eye diseases, inflammation, tumorigenesis and other diseases. Therefore, in recent years, the molecular mechanisms mediating these processes have received increasing interest for the identification of molecular targets that could lead to the development of new drugs. Given their crucial role in cellular function, a deeper understanding of ubiquitination/sumoylation-mediated signaling pathways and their regulatory mechanisms is needed, in order to identify novel molecular players as well as novel therapeutic targets for treatment of cancer and other diseases.
This Research Topic aims to highlight the latest advances in understanding the molecular mechanisms of ubiquitination and sumoylation, their regulation in different signaling pathways involved in human disease, as well as in the identification of potential therapeutic targets for drug development.
Areas to be covered may include, but are not limited to:
• Ubiquitination/deubiquitination/sumoylation/desumoylation signaling pathways e.g. P53/p63/TGF-beta/NF-kB/Wnt/innate immune signaling, etc.;
• Ubiquitin and Ubiquitin-like modifications in tumorigenesis, cancer progression, metastasis and tumor microenvironment;
• The interplay between UPS and autophagy, cell death and apoptosis;
• Sumoylation regulation of transcription factors and major signaling components in ocular diseases;
• Sumoylation regulation of apoptotic components involved in cancer and ocular diseases.
The ubiquitin-proteasome system (UPS) is a protein degradation system which is highly selective and depends on adenosine triphosphate (ATP) for energy supply in eukaryotic cells. About 80% of proteins are degraded by this system. UPS is composed of ubiquitin, E1 ubiquitin-activating enzymes, E2 ubiquitin-conjugating enzymes, E3 ubiquitin-ligase enzymes, 26S proteasome and deubiquitinases (DUBs). Similar to ubiquitination, SUMOylation is a post-transcriptional modification mediated by unique E1 and E2 ligases and multiple E3 ligases with consumption of ATP to conjugate the SUMOb- Small Ubiquitin-like Modifier - (SUMO1/2/3) small peptides to target proteins. SUMO proteins are similar to ubiquitin and are considered members of the ubiquitin-like protein family. Sumoylation can modify over 6,000 proteins involved in many physiological and pathological processes.
Ubiquitination/Ubiquitin-like modifications play an important role in various aspects of cellular processes, such as protein localization, metabolism, function, regulation and degradation. Ubiquitination and sumoylation have been widely involved in the regulation of crucial physiological processes, such as DNA damage repair, cell cycle, cell proliferation, apoptosis, cell differentiation, transcription regulation, signal transduction, vesicle transport, autophagy, immunity, etc. In addition, ubiquitination and sumoylation are involved in the pathological processes leading to eye diseases, inflammation, tumorigenesis and other diseases. Therefore, in recent years, the molecular mechanisms mediating these processes have received increasing interest for the identification of molecular targets that could lead to the development of new drugs. Given their crucial role in cellular function, a deeper understanding of ubiquitination/sumoylation-mediated signaling pathways and their regulatory mechanisms is needed, in order to identify novel molecular players as well as novel therapeutic targets for treatment of cancer and other diseases.
This Research Topic aims to highlight the latest advances in understanding the molecular mechanisms of ubiquitination and sumoylation, their regulation in different signaling pathways involved in human disease, as well as in the identification of potential therapeutic targets for drug development.
Areas to be covered may include, but are not limited to:
• Ubiquitination/deubiquitination/sumoylation/desumoylation signaling pathways e.g. P53/p63/TGF-beta/NF-kB/Wnt/innate immune signaling, etc.;
• Ubiquitin and Ubiquitin-like modifications in tumorigenesis, cancer progression, metastasis and tumor microenvironment;
• The interplay between UPS and autophagy, cell death and apoptosis;
• Sumoylation regulation of transcription factors and major signaling components in ocular diseases;
• Sumoylation regulation of apoptotic components involved in cancer and ocular diseases.
