Related Experiment Video
Updated: Jun 28, 2025
07:27
Optimized Incorporation of Alkynyl Fatty Acid Analogs for the Detection of Fatty Acylated Proteins using Click Chemistry
Published on: April 9, 2021
5.2K
Modulators for palmitoylation of proteins and small molecules
Zeshuai Fan1, Yuchen Hao1, Yidan Huo1
1Key Laboratory of Pharmaceutical Quality Control of Hebei Province, College of Pharmaceutical Sciences, Hebei University, Baoding, 071002, China.
European Journal of Medicinal Chemistry
|April 15, 2024
Summary
Palmitoylation, a key lipid modification, regulates cell functions and is crucial for treating diseases like cancer. This review covers its types, enzymes, and inhibitors for therapeutic development.
Area of Science:
- Biochemistry and Molecular Biology
- Cellular and Physiological Processes
- Drug Discovery and Development
Background:
- Palmitoylation is an essential lipid modification regulating critical cellular functions.
- It plays a significant role in diverse physiological processes.
- Dysregulation of palmitoylation is implicated in diseases such as cancer and neurological disorders.
Purpose of the Study:
- To provide a comprehensive overview of palmitoylation.
- To detail the regulatory enzymes involved, including palmitoyltransferases and depalmitoylases.
- To discuss current therapeutic strategies, focusing on available inhibitors.
Main Methods:
- Literature review of existing research on palmitoylation.
- Categorization of palmitoylation into N-, O-, and S-palmitoylation.
- Analysis of regulatory enzymes and their inhibitors.
Main Results:
- Palmitoylation is classified into three distinct types: N-palmitoylation, O-palmitoylation, and S-palmitoylation.
- Key enzymes regulating palmitoylation include palmitoyltransferases and depalmitoylases.
- A range of broad-spectrum and selective inhibitors targeting these enzymes have been identified.
Conclusions:
- Palmitoylation is a vital cellular process with therapeutic potential for various diseases.
- Understanding the enzymes and inhibitors of palmitoylation is crucial for developing targeted therapies.
- Further research into selective inhibitors could lead to novel treatments for cancer and neurological disorders.
Related Concept Videos
02:04Covalently Linked Protein Regulators
6.8K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
These groups modify specific amino acids in a protein....
6.8K
01:32Lipids as Anchors
5.6K
In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains...
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains...
5.6K
01:16Calmodulin-dependent Signaling
5.1K
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
5.1K
01:19Regulation of Metabolism
9.4K
Cellular needs and conditions vary from cell to cell and change within individual cells over time. For example, the required enzymes and energetic demands of stomach cells are different from those of fat storage cells, skin cells, blood cells, and nerve cells. Furthermore, a digestive cell works much harder to process and break down nutrients during the time that closely follows a meal compared with many hours after a meal. As these cellular demands and conditions vary, so do the amounts and...
9.4K
01:45Regulation of Nuclear Protein Sorting
2.4K
Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
2.4K
01:58Cooperative Allosteric Transitions
7.9K
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
7.9K