Special Issue "Protein Post-translational Modifications in Signal Transduction and Diseases"
Deadline for manuscript submissions: closed (31 October 2020) | Viewed by 51858
Interests: protein phosphorylation; acidic protein kinases; tyrosine kinases; kinase inhibitors, signal transduction; post-translational modifications; cancer; cystic fibrosis
Special Issues, Collections and Topics in MDPI journals
Special Issue in International Journal of Molecular Sciences: Protein Phosphorylation in Genetic Diseases
Special Issue in Kinases and Phosphatases: Research on Protein Phosphorylation in Genetic Diseases
Special Issue in Kinases and Phosphatases: Past, Present and Future of Protein Kinase CK2 Research
Post-translational modifications (PTMs) are well-known covalent processing events that can affect virtually all aspects of the functionality and the signalling of a protein, influencing its folding, stability, localization, and binding partners. It is therefore not surprising that altered levels of PTMs may be involved in different human diseases, including cancer, neurodegeneration, diabetes and inflammatory diseases, and the enzymes regulating their turnover are pharmacological targets of primary importance.
Among PTMs, protein phosphorylation is the most extensively studied, and its role in signalling transduction is widely accepted, but hundreds of other modifications have been identified to date, and new ones are still under identification. Notably, the complexity increases because the crosstalk between PTMs is widespread. The same amino acid can be modified by different competing PTMs—lysine residues, for example, can be modified by the addition of chemical groups, such as acetylation and methylation; the addition of complex molecules, such as glycation; or the addition of other protein molecules, such as ubiquitylation and sumoylation, and the biological outcome changes according the type of modification that prevails. Moreover, most commonly, the same protein is subjected to different PTMs in multiple sites, which can affect each other by simply changing either protein folding or chemical surface. The PhosphositePlus database indeed collects almost 500.000 PTMs in about 20,000 non-redundant proteins, which means an average of about 25 PTMs for protein.
The sum of the PTMs of a protein, functioning in a combinatory manner, define the so called PTM code, which, together with the dynamic nature of many PTMs, permits precisely fine-tuning any biological process, and transducing any microenvironment change into a rapid and specific cell response.
In this regard, we invite investigators to contribute original research and review articles that will stimulate the continuing efforts to understand how protein functions are affected by different types of PTMs, not limited to phosphorylation, in order to develop strategies for their identification and characterization, and to highlight the interactions between PTMs under normal and pathological processes.
The editors are particularly interested in the following topics:
- Identification and characterization of PTMs
- Structural and functional alteration of a protein following PTMs
- Methodological developments in the PTMs field
- Proteins involved in PTMs signalling: writers, erasers, and readers
- PTMs crosstalk
- Pato-physiological role of PTMs
Prof. Mauro Salvi
Dr. Claudio D‘Amore
Manuscript Submission Information
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