Protein ubiquitination is a powerful post-translational modulator of cellular functions and is tightly controlled by the action of hundreds of regulatory (E1, E2, E3) and deubiquitinating enzymes (DUBs). Unlike most post-translational modifiers such as phosphorylation or acetylation, ubiquitination can be highly customized through further post-translational modification of ubiquitin itself, thereby coding for a distinct cellular outcome. Dysregulation of this intrinsic process is often associated with diseases that include cancer, autoimmunity, Alzheimer, and Parkinson’s disease.
Next to ubiquitin, a number of ubiquitin-like proteins (e.g. Sumo, Nedd8, Isg15, Ufm1, Fat10) can also be attached to proteins increasing the complexity of and fine-tuning cellular responses even further. To advance our understanding of one of the most complex and widespread signaling networks in biology, activity-based probes (ABPs), assay reagents as well as advanced proteomics techniques are key. Characterization of this dynamic field is imminent as the development of inhibitors of Ubiquitin(-like) system components has gained significant increase in interest recently.
The aim of the current Research Topic is to cover promising, recent, and novel research trends in the ubiquitin and ubiquitin-like field. Areas to be covered in this Research Topic may include, but are not limited to:
- Development of Activity Based Probes
- Application of the ubiquitin(-like) based toolbox in the study of the ubiquitin landscape
- Therapeutic strategies (e.g Assay development, PROTACs)
- Ubiquitin(-like) variants
- Advanced proteomic techniques
Protein ubiquitination is a powerful post-translational modulator of cellular functions and is tightly controlled by the action of hundreds of regulatory (E1, E2, E3) and deubiquitinating enzymes (DUBs). Unlike most post-translational modifiers such as phosphorylation or acetylation, ubiquitination can be highly customized through further post-translational modification of ubiquitin itself, thereby coding for a distinct cellular outcome. Dysregulation of this intrinsic process is often associated with diseases that include cancer, autoimmunity, Alzheimer, and Parkinson’s disease.
Next to ubiquitin, a number of ubiquitin-like proteins (e.g. Sumo, Nedd8, Isg15, Ufm1, Fat10) can also be attached to proteins increasing the complexity of and fine-tuning cellular responses even further. To advance our understanding of one of the most complex and widespread signaling networks in biology, activity-based probes (ABPs), assay reagents as well as advanced proteomics techniques are key. Characterization of this dynamic field is imminent as the development of inhibitors of Ubiquitin(-like) system components has gained significant increase in interest recently.
The aim of the current Research Topic is to cover promising, recent, and novel research trends in the ubiquitin and ubiquitin-like field. Areas to be covered in this Research Topic may include, but are not limited to:
- Development of Activity Based Probes
- Application of the ubiquitin(-like) based toolbox in the study of the ubiquitin landscape
- Therapeutic strategies (e.g Assay development, PROTACs)
- Ubiquitin(-like) variants
- Advanced proteomic techniques