Protein S-palmitoylation, the most common lipid modification with the 16-carbon fatty acid palmitate, provides an important mechanism for regulating protein trafficking and function. The unique reversibility of protein palmitoylation allows proteins to rapidly shuttle between intracellular membrane compartments. Importantly, this palmitate cycling can be regulated by some physiological stimuli, contributing to cellular homeostasis and plasticity. Although the enzyme responsible for protein palmitoylation had been long elusive, DHHC family proteins, conserved from plants to mammals, have recently emerged as palmitoyl acyl transferases. Integrated approaches including advanced proteomics, live-cell imaging, and molecular genetics are beginning to clarify the molecular machinery for palmitoylation reaction in diverse aspects of cellular functions.
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Protein palmitoylation in hepatic diseases: Functional insights and therapeutic strategies.
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The First Affiliated Hospital of Xinxiang Medical University, Xinxiang, Henan, PR China; Institute of Psychiatry and Neuroscience of Xinxiang Medical University, Xinxiang, Henan, PR China; Laboratory of Genetic Regulators in the Immune System, School of Medical Technology, Xinxiang Medical University, Xinxiang, Henan, PR China. Electronic address:
Background: Liver pathologies represent a spectrum of conditions ranging from fatty liver to the aggressive hepatocellular carcinoma (HCC), as well as parasitic infections, which collectively pose substantial global health challenges. S-palmitoylation (commonly referred to as palmitoylation), a post-translational modification (PTM) characterized by the covalent linkage of a 16-carbon palmitic acid (PA) chain to specific cysteine residues on target proteins, plays a pivotal role in diverse cellular functions and is intimately associated with the liver's physiological and pathological states.
Aim Of Review: This study aims to elucidate how protein palmitoylation affects liver disease pathophysiology and evaluates its potential as a target for diagnostic and therapeutic interventions.
The blue-light receptor CRY1 serves as a switch to balance photosynthesis and plant defense.
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CAS Center for Excellence in Molecular Plant Sciences (CEMPS), Institute of Plant Physiology and Ecology (SIPPE), Chinese Academy of Sciences, Shanghai 200031, People's Republic of China; College of Life Sciences and Oceanography, Shenzhen University, Shenzhen 518060, People's Republic of China. Electronic address:
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Protein S-palmitoylation is a reversible form of protein lipidation in which the formation of a thioester bond occurs between a cysteine (Cys) residue of a protein and a 16-carbon fatty acid chain. This modification is catalyzed by a family of palmitoyl acyl transferases, the DHHC enzymes, so called because of their Asp-His-His-Cys (DHHC) catalytic motif. Deregulation of DHHC enzymes has been linked to various diseases, including cancer and infections.
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Article Synopsis
- Postoperative cognitive dysfunction (POCD) is a complication related to surgery involving cognitive decline, potentially influenced by neuroinflammation, ferroptosis, and mitochondrial fatty acid metabolism, particularly via the protein Carnitine palmitoyl transferase 1a (CPT1A).
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- Results showed that higher levels of CPT1A improved mitochondrial function and reduced oxidative stress and inflammation in astrocytes, which benefitted neuron health, while these effects depended on functional mitochondrial respiration, as demonstrated when treatments disrupted this process.
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