Understanding protein function within living cells is crucial for basic research and therapeutic development. Protein kinetics in living cells provide more relevant insights compared to studies in reconstituted systems, reflecting the true physiological context, including interactions with cellular components, physiological concentrations of ions and cofactors, and dynamic cellular changes. In this environment, proteins interact with various molecules including proteins, nucleic acids and lipids, resulting in behaviors that cannot be measured precisely by reconstituted systems. Post-translational modifications, such as phosphorylation and glycosylation, further impact protein kinetics and function, which are best observed in living cells.
Cellular compartmentalization influences protein kinetics, availability, and function based on localization within the plasma membrane, cytoplasm, nucleus, or other organelles. Dynamic regulatory processes, such as feedback mechanisms and signaling pathways, also affect protein behavior in ways that are difficult to replicate outside living cells. Physiological expression levels and multiple isoforms of proteins exhibit distinct kinetics and functions, shaped by the cellular context, including stress responses and metabolic states.
However, measuring protein kinetics in living cells poses significant challenges due to the complexity of the environment, the need for high temporal and spatial resolution, and limited accessibility to specific compartments. Non-invasive techniques must avoid disrupting cellular physiology, and fluorescent tagging can potentially alter protein behavior. Additionally, accurate quantification is complicated by background noise, varying local concentrations of interacting molecules, and maintaining high signal-to-noise ratios during live-cell imaging, while avoiding phototoxicity and photobleaching. The large datasets generated require advanced computational tools for analysis, and biological variability between cells further limits the scope and accuracy of such studies. These challenges emphasize the need for interdisciplinary collaboration and innovative experimental techniques.
This collection seeks contributions that advance our understanding and capabilities in measuring protein kinetics in living cells, with a focus on experimental innovations that address these challenges, together with single molecule and ensemble measurements.
Keywords:
protein kinetics, protein function, in vivo, protein-protein kinetics
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.
Understanding protein function within living cells is crucial for basic research and therapeutic development. Protein kinetics in living cells provide more relevant insights compared to studies in reconstituted systems, reflecting the true physiological context, including interactions with cellular components, physiological concentrations of ions and cofactors, and dynamic cellular changes. In this environment, proteins interact with various molecules including proteins, nucleic acids and lipids, resulting in behaviors that cannot be measured precisely by reconstituted systems. Post-translational modifications, such as phosphorylation and glycosylation, further impact protein kinetics and function, which are best observed in living cells.
Cellular compartmentalization influences protein kinetics, availability, and function based on localization within the plasma membrane, cytoplasm, nucleus, or other organelles. Dynamic regulatory processes, such as feedback mechanisms and signaling pathways, also affect protein behavior in ways that are difficult to replicate outside living cells. Physiological expression levels and multiple isoforms of proteins exhibit distinct kinetics and functions, shaped by the cellular context, including stress responses and metabolic states.
However, measuring protein kinetics in living cells poses significant challenges due to the complexity of the environment, the need for high temporal and spatial resolution, and limited accessibility to specific compartments. Non-invasive techniques must avoid disrupting cellular physiology, and fluorescent tagging can potentially alter protein behavior. Additionally, accurate quantification is complicated by background noise, varying local concentrations of interacting molecules, and maintaining high signal-to-noise ratios during live-cell imaging, while avoiding phototoxicity and photobleaching. The large datasets generated require advanced computational tools for analysis, and biological variability between cells further limits the scope and accuracy of such studies. These challenges emphasize the need for interdisciplinary collaboration and innovative experimental techniques.
This collection seeks contributions that advance our understanding and capabilities in measuring protein kinetics in living cells, with a focus on experimental innovations that address these challenges, together with single molecule and ensemble measurements.
Keywords:
protein kinetics, protein function, in vivo, protein-protein kinetics
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.