Studies on the impact of acetyl-cysteine on metabolism

NIH RePORTER · NIH · R21 · $194,381 · view on reporter.nih.gov ↗

Abstract

Cells integrate nutrient sensing and metabolism to coordinate proper cellular responses to a particular nutrient source. One way this occurs is via post-translational modifications of proteins. Acetyl-lysine is among the most studied modification and regulates dynamic processes ranging from chromatin and gene expression to metabolism. Our preliminary data presented in this application expand upon the acetylation landscape and describe a new protein modification called acetyl-cysteine. This modification is abundant across the proteome and is enriched on proteins involved in metabolism. These early data reveal key gaps in our understanding of the acetylation landscape: what is the tissue distribution of this new modification? Under which physiological conditions does this modification change? Which proteins are modified? What is the cellular consequence of cysteine hyperacetylation? Is this relevant for aging? There is a critical need to understand the full range of protein modifications in order to better understand physiological nutrient sensing and how it is perturbed in the setting of disease. Although it is widely accepted that lysine modifications can participate in intracellular nutrient sensing and is dysregulated with aging, no data exists on acetyl-cysteine. Therefore, the single objective of this exploratory grant application is to determine the site(s), consequences, and physiologic mediators of cysteine acetylation. Aim 1 will investigate the prevalence of cysteine acetylation by tissue type and metabolic state. In a complementary parallel approach, Aim 2 will characterize the effects of cysteine acetylation on protein activity. This project is significant because it uncovers a previously overlooked protein modification. Furthermore, given cysteine’s central role in redox homeostasis, it is poised to play a central role in metabolic homeostasis. We put forth conceptual and technical innovations that will both follow directed hypotheses and allow unbiased discovery of the most important aspects of this new protein modification. Successful completion of this project will reveal a new aspect of intracellular signaling and metabolic homeostasis that could influence our understanding of redox biology and metabolism during aging.

Key facts

NIH application ID
10745731
Project number
5R21AG080334-02
Recipient
DUKE UNIVERSITY
Principal Investigator
Matthew D Hirschey
Activity code
R21
Funding institute
NIH
Fiscal year
2024
Award amount
$194,381
Award type
5
Project period
2022-12-01 → 2024-11-30