About this Research Topic
Protein phosphorylation is one of the most abundant reversible post-translational modifications in eukaryotes. It is involved in virtually all cellular processes by regulating protein function, localization and stability and by mediating protein-protein interactions. Furthermore, aberrant protein phosphorylation is implicated in the onset and the progression of human diseases such as cancer and neurodegenerative disorders.
In the last years, tens of thousands of in vivo phosphorylation events have been identified by large-scale quantitative phospho-proteomics experiment suggesting that a large fraction of the proteome might be regulated by phosphorylation. This data explosion is increasingly enabling the development of computational approaches, often combined with experimental validation, aiming at prioritising phospho-sites and assessing their functional relevance or uncovering the specificity determinants of protein kinases/phosphatases and phospho-residue recognition domains. In this context, several interesting issues are still open regarding phosphorylation, including a better understanding of the interplay between phosphorylation and allosteric regulation, agents and mechanisms disrupting or promoting abnormal phosphorylation in several diseases, the identification and modulation of novel phosphorylation inhibitors, and so forth. The determinants of kinase and phosphatase recognition and binding specificity are still unknown in several cases, as well as the impact of disease mutations on phosphorylation-mediated signalling.
The objective of this Research Topic is to stimulate researchers to describe and discuss the progress of the research in the field of protein phosphorylation and examine yet unanswered questions in order to gain an exhaustive picture of the research status from different perspectives, going from protein sequence to structure, evolution, genomics, transcriptomics and proteomics with a particular focus on the role of protein phosphorylation in disease.
Potential subjects of interest include, but are not limited to:
− Kinase and phosphatase substrate specificity;
− Functional characterization of kinase-substrate and phosphatase-substrate relationships;
− Generation and/or analysis of phosphorylation networks in both health and disease;
− Interplay between phosphorylation and allosteric mechanisms/regulation;
− Description of novel phospho-protein three-dimensional structures;
− Computational methods for the prediction of phosphorylation sites and/or kinase specificity;
− Experimental procedures for the identification and/or validation of new phosphorylation events;
− Effect of disease mutations on kinases, phosphatases and phosphoproteins function and their interaction ability;
− The role of phosphorylation in protein misfolding and aggregation.
− Cases of phosphorylation deregulation in specific diseases;
− Alternative splicing and phosphorylation;
− Non-coding RNAs involved in phosphorylation regulation;
− Evolutionary studies related to phosphorylation.
Authors are encouraged to submit: reviews, mini-reviews, methods articles, perspective and original research articles.
In the last years, tens of thousands of in vivo phosphorylation events have been identified by large-scale quantitative phospho-proteomics experiment suggesting that a large fraction of the proteome might be regulated by phosphorylation. This data explosion is increasingly enabling the development of computational approaches, often combined with experimental validation, aiming at prioritising phospho-sites and assessing their functional relevance or uncovering the specificity determinants of protein kinases/phosphatases and phospho-residue recognition domains. In this context, several interesting issues are still open regarding phosphorylation, including a better understanding of the interplay between phosphorylation and allosteric regulation, agents and mechanisms disrupting or promoting abnormal phosphorylation in several diseases, the identification and modulation of novel phosphorylation inhibitors, and so forth. The determinants of kinase and phosphatase recognition and binding specificity are still unknown in several cases, as well as the impact of disease mutations on phosphorylation-mediated signalling.
The objective of this Research Topic is to stimulate researchers to describe and discuss the progress of the research in the field of protein phosphorylation and examine yet unanswered questions in order to gain an exhaustive picture of the research status from different perspectives, going from protein sequence to structure, evolution, genomics, transcriptomics and proteomics with a particular focus on the role of protein phosphorylation in disease.
Potential subjects of interest include, but are not limited to:
− Kinase and phosphatase substrate specificity;
− Functional characterization of kinase-substrate and phosphatase-substrate relationships;
− Generation and/or analysis of phosphorylation networks in both health and disease;
− Interplay between phosphorylation and allosteric mechanisms/regulation;
− Description of novel phospho-protein three-dimensional structures;
− Computational methods for the prediction of phosphorylation sites and/or kinase specificity;
− Experimental procedures for the identification and/or validation of new phosphorylation events;
− Effect of disease mutations on kinases, phosphatases and phosphoproteins function and their interaction ability;
− The role of phosphorylation in protein misfolding and aggregation.
− Cases of phosphorylation deregulation in specific diseases;
− Alternative splicing and phosphorylation;
− Non-coding RNAs involved in phosphorylation regulation;
− Evolutionary studies related to phosphorylation.
Authors are encouraged to submit: reviews, mini-reviews, methods articles, perspective and original research articles.
Important Note: All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.
