About this Research Topic
In the last two decades, it was discovered that proteomes are much more complex than their corresponding genomes. One of the main reasons is that most proteins exist in several modified forms, with many thousands of post-translational modification (PTM) sites being predicted to exist. Currently, there are more than 600 different known PTMs that have been reported in plants, most of which have been proven to play very important roles. PTMs, such as phosphorylation, ubiquitylation, acetylation, have been shown to be involved in many biological functions in plants, including signal transduction, differentiation, hormone perception, transformation, and metabolism. Because of these, regulation by PTMs is a major focus in proteomics studies.
It is well known that PTMs can regulate protein activity, localization, recycling and interaction with other cellular constituents. A given PTM might function differently because of its different target proteins, and different PTMs might function similarly, which makes it necessary to comprehensively profile the proteome at the PTM level. To facilitate such study, techniques that apply to the enrichment of PTM-containing proteins (or peptides) and mass spectrometric identification of PTMs, as well as PTM predictions, should be developed. More importantly, PTM level proteomics studies should be performed under physiologically relevant contexts, in order to obtain functional insights. To achieve this, attention should focus on method development and improvement.
Studies in the field of plant proteomics focusing on PTMs are all welcome, together with relevant functional characterization and hypothesis-driven physiological insights. The themes include but are not limited to the development of techniques, software and databases, profiling of PTM-level sub-proteomes, the discovery of new PTMs, and functional characterization of PTMs in specific biological processes.
Submissions of review, original research, short communication and commentaries are welcome.
Please note that descriptive collections of proteins will not be considered for review unless they are expanded and provide mechanistic and/or physiological insights into the biological system or process being studied.
It is well known that PTMs can regulate protein activity, localization, recycling and interaction with other cellular constituents. A given PTM might function differently because of its different target proteins, and different PTMs might function similarly, which makes it necessary to comprehensively profile the proteome at the PTM level. To facilitate such study, techniques that apply to the enrichment of PTM-containing proteins (or peptides) and mass spectrometric identification of PTMs, as well as PTM predictions, should be developed. More importantly, PTM level proteomics studies should be performed under physiologically relevant contexts, in order to obtain functional insights. To achieve this, attention should focus on method development and improvement.
Studies in the field of plant proteomics focusing on PTMs are all welcome, together with relevant functional characterization and hypothesis-driven physiological insights. The themes include but are not limited to the development of techniques, software and databases, profiling of PTM-level sub-proteomes, the discovery of new PTMs, and functional characterization of PTMs in specific biological processes.
Submissions of review, original research, short communication and commentaries are welcome.
Please note that descriptive collections of proteins will not be considered for review unless they are expanded and provide mechanistic and/or physiological insights into the biological system or process being studied.
Keywords: Affinity purification, Cell signaling, Mass spectrometry, Proteomics, PTMs
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