About this Research Topic
Protein acylation are a group of post-translational modifications involving the addition of acyl groups to the lysine residue in proteins. These modifications play significant roles in various cellular processes, including signal transduction, enzymatic regulation, cell metabolism, apoptosis, and aging. Despite its importance, the underlying mechanisms governing protein acylation and deacylation remain poorly understood. Recent advances regarding this question includes the identification of novel acyltransferases and deacylases, site-specific acylation profiling, acylation in diseases and acylation crosstalk, and contribute to this field greatly.
This Research Topic aims to elucidate the mechanistic details of protein acylation, focusing on the enzymes responsible for catalyzing this modification, the substrates involved, the functional consequences of acylation events, and the related tools or methods development. Through a combination of biochemical, biophysical, and cellular approaches, this article collection hopes to shed light on the intricate regulatory networks of protein acylation and its impact on cellular physiology. Understanding these mechanisms could pave the way for developing novel therapeutic strategies for diseases associated with dysregulated protein acylation, such as cancer and metabolic disorders. The specific themes we would like contributors to address are:
• Identification and characterization of novel acyltransferases and deacylases: Investigate the enzymes responsible for diverse protein acylations.
• Explore the amino acid residues targeted for acylation and the sequence motifs influencing enzyme-substrate interactions.
• Study conformational dynamics to gain insights into enzyme-substrate interactions and acylation process.
• Development high-throughput method to delineate protein acylations and their specificities.
• Analysis of proteomes and acylomes to discover novel targeted proteins or pathways.
• Investigate the roles of protein acylation in signal transduction, cellular responses, and other cellular processes.
• Assess the functional consequences of protein acylation on protein stability, activity, and subcellular localization.
• Investigate how aberrant protein acylation contributes to diseases and pathogenesis.
This Research Topic aims to elucidate the mechanistic details of protein acylation, focusing on the enzymes responsible for catalyzing this modification, the substrates involved, the functional consequences of acylation events, and the related tools or methods development. Through a combination of biochemical, biophysical, and cellular approaches, this article collection hopes to shed light on the intricate regulatory networks of protein acylation and its impact on cellular physiology. Understanding these mechanisms could pave the way for developing novel therapeutic strategies for diseases associated with dysregulated protein acylation, such as cancer and metabolic disorders. The specific themes we would like contributors to address are:
• Identification and characterization of novel acyltransferases and deacylases: Investigate the enzymes responsible for diverse protein acylations.
• Explore the amino acid residues targeted for acylation and the sequence motifs influencing enzyme-substrate interactions.
• Study conformational dynamics to gain insights into enzyme-substrate interactions and acylation process.
• Development high-throughput method to delineate protein acylations and their specificities.
• Analysis of proteomes and acylomes to discover novel targeted proteins or pathways.
• Investigate the roles of protein acylation in signal transduction, cellular responses, and other cellular processes.
• Assess the functional consequences of protein acylation on protein stability, activity, and subcellular localization.
• Investigate how aberrant protein acylation contributes to diseases and pathogenesis.
Keywords: Protein post-translational modifications; Acylation; Sirtuin; Regulation; Enzyme specificity
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.
