The cellular proteome is highly spatiotemporally regulated. The dynamic movement of proteins between organelles is essential for cellular processes such as signaling, growth, proliferation, and programmed cell death. Aberrant protein localizations are associated with a wide range of diseases. Deep profiling and quantification of subcellular proteome could contribute to the understanding of the underneath biological functions of protein regulation in various parts and/or compartments of cells. Moreover, the extra layer of post-translational modifications (PTMs) extends the regulatory complexity of how subcellular proteome performs at different levels, in both spatial and timely manners. These include, but are not limited to: phosphorylation, glycosylation, ubiquitylation, methylation, acetylation, and sumoylation. Novel techniques for analyzing the localization, distribution, and abundance of proteins within subcellular structures, including for example fluorescent imaging, enzyme-catalyzed protein proximity labeling, organelle purification, and biochemical subcellular fractionation are also recent research hotspots.
In this Research Topic, we are aiming for two major goals, which are the understanding of regulatory roles of the subcellular proteome and its post-translational modifications (PTMs), as well as the development of advanced technologies and applications. To further our insights into the subcellular proteome, deeper biological interpretation and novel techniques are the key. More specific and/or comprehensive annotations of subcellular proteome and its PTMs will be crucial. Establishing clearer and more straightforward links between the subcellular proteome and its PTM with certain diseases such as cancer, autoimmune diseases, and chronic kidney disease will be very valuable for disease-based research. For technical development, efficient enrichment and/or fractionation of certain subcellular compartments is important. PTM studies have suffered from limitations due to the low abundances of many PTMs. Measuring the stoichiometry of PTM occupation is crucial to the understanding of its regulatory mechanism, therefore, the development of sensitive and quantitative PTM analysis methods in a subcellular context is essential.
This Research Topic aims to cover recent promising research trends in exploring subcellular proteome and its PTMs. Areas to be covered in this Research Topic may include, but are not limited to:
• Role of post-translational modifications in subcellular protein regulation
• Biological interpretation of subcellular proteome, such as signaling pathways and therapeutic response
• Post-translational modification landscape of subcellular populations
• Proteome landscape of subcellular populations
• Novel techniques, both experimental and computational, in probing subcellular proteome.
The cellular proteome is highly spatiotemporally regulated. The dynamic movement of proteins between organelles is essential for cellular processes such as signaling, growth, proliferation, and programmed cell death. Aberrant protein localizations are associated with a wide range of diseases. Deep profiling and quantification of subcellular proteome could contribute to the understanding of the underneath biological functions of protein regulation in various parts and/or compartments of cells. Moreover, the extra layer of post-translational modifications (PTMs) extends the regulatory complexity of how subcellular proteome performs at different levels, in both spatial and timely manners. These include, but are not limited to: phosphorylation, glycosylation, ubiquitylation, methylation, acetylation, and sumoylation. Novel techniques for analyzing the localization, distribution, and abundance of proteins within subcellular structures, including for example fluorescent imaging, enzyme-catalyzed protein proximity labeling, organelle purification, and biochemical subcellular fractionation are also recent research hotspots.
In this Research Topic, we are aiming for two major goals, which are the understanding of regulatory roles of the subcellular proteome and its post-translational modifications (PTMs), as well as the development of advanced technologies and applications. To further our insights into the subcellular proteome, deeper biological interpretation and novel techniques are the key. More specific and/or comprehensive annotations of subcellular proteome and its PTMs will be crucial. Establishing clearer and more straightforward links between the subcellular proteome and its PTM with certain diseases such as cancer, autoimmune diseases, and chronic kidney disease will be very valuable for disease-based research. For technical development, efficient enrichment and/or fractionation of certain subcellular compartments is important. PTM studies have suffered from limitations due to the low abundances of many PTMs. Measuring the stoichiometry of PTM occupation is crucial to the understanding of its regulatory mechanism, therefore, the development of sensitive and quantitative PTM analysis methods in a subcellular context is essential.
This Research Topic aims to cover recent promising research trends in exploring subcellular proteome and its PTMs. Areas to be covered in this Research Topic may include, but are not limited to:
• Role of post-translational modifications in subcellular protein regulation
• Biological interpretation of subcellular proteome, such as signaling pathways and therapeutic response
• Post-translational modification landscape of subcellular populations
• Proteome landscape of subcellular populations
• Novel techniques, both experimental and computational, in probing subcellular proteome.
