Unraveling Enzyme-Substrate Dynamics in Protein Acylation and Disease Implications

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Background

Protein acylation is a critical area of research within the broader field of post-translational modifications, involving the addition of acyl groups to lysine residues in proteins. These modifications are pivotal in regulating various cellular processes such as signal transduction, enzymatic activity, cell metabolism, apoptosis, and aging. Despite their significance, the precise mechanisms that govern protein acylation and deacylation remain largely elusive. Recent studies have made strides in this area by identifying novel acyltransferases and deacylases, profiling site-specific acylation, and exploring the role of acylation in diseases and its crosstalk with other cellular processes. However, there remains a substantial gap in understanding the detailed mechanistic pathways and regulatory networks involved in protein acylation, necessitating further investigation to fully elucidate these complex biological phenomena.

This research topic aims to elucidate the mechanistic details of protein acylation, with a focus on the enzymes responsible for catalyzing these modifications, the substrates involved, and the functional consequences of acylation events. By employing a combination of biochemical, biophysical, and cellular approaches, this collection of articles seeks to unravel the intricate regulatory networks of protein acylation and its impact on cellular physiology. The ultimate goal is to enhance our understanding of these mechanisms, which could lead to the development of novel therapeutic strategies for diseases associated with dysregulated protein acylation, such as cancer and metabolic disorders.

To gather further insights into the mechanistic studies on protein acylation, we welcome articles addressing, but not limited to, the following themes:

- Identification and characterization of novel acyltransferases and deacylases.
- Exploration of amino acid residues targeted for acylation and sequence motifs influencing enzyme-substrate interactions.
- Study of conformational dynamics to gain insights into enzyme-substrate interactions and the acylation process.
- Development of high-throughput methods to delineate protein acylations and their specificities.
- Analysis of proteomes and acylomes to discover novel targeted proteins or pathways.
- Investigation of the roles of protein acylation in signal transduction, cellular responses, and other cellular processes.
- Assessment of the functional consequences of protein acylation on protein stability, activity, and subcellular localization.
- Examination of 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.

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