Page last updated: 2024-10-24

protein depalmitoylation

Definition

Target type: biologicalprocess

The removal of palymitoyl groups from a lipoprotein. [GOC:hjd]

Protein depalmitoylation is a crucial biological process involving the removal of palmitic acid, a saturated fatty acid, from proteins. Palmitoylation, the attachment of palmitic acid, is a reversible modification that plays a significant role in regulating protein function, localization, and interactions. Depalmitoylation, catalyzed by a family of enzymes called palmitoyl protein thioesterases (PPTs), reverses this process, impacting these key aspects of protein behavior.

The process begins with the recognition and binding of the palmitoylated protein by the PPT enzyme. This interaction is often facilitated by specific amino acid sequences or motifs within the protein. Once bound, the PPT enzyme utilizes a hydrolytic mechanism to break the thioester bond between the palmitic acid and the cysteine residue on the protein. This reaction releases free palmitic acid and the depalmitoylated protein.

Depalmitoylation exerts a range of biological effects, influencing various cellular processes:

- **Protein localization:** Depalmitoylation can promote the relocation of proteins from the plasma membrane to other cellular compartments. For example, depalmitoylation of certain signaling proteins can lead to their internalization and degradation, thus modulating signal transduction pathways.
- **Protein-protein interactions:** Depalmitoylation can disrupt or enhance protein-protein interactions. By removing the palmitate moiety, the protein's hydrophobic properties are altered, impacting its ability to interact with other proteins or membrane components.
- **Protein activity:** Depalmitoylation can regulate the activity of proteins by altering their conformation or accessibility to other molecules. This can influence enzymatic activity, signaling cascades, and other cellular functions.

In summary, protein depalmitoylation is a dynamic process that fine-tunes protein function through the removal of palmitic acid. This reversible modification plays a critical role in regulating protein localization, interactions, and activity, influencing a wide array of cellular processes.'
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Proteins (2)

ProteinDefinitionTaxonomy
Acyl-protein thioesterase 2An acyl-protein thioesterase 2 that is encoded in the genome of human. [PRO:DNx, UniProtKB:O95372]Homo sapiens (human)
Acyl-protein thioesterase 1An acyl-protein thioesterase 1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:O75608]Homo sapiens (human)

Compounds (5)

CompoundDefinitionClassesRoles
benzo(b)thiophene-2-boronic acidbenzo(b)thiophene-2-boronic acid: inhibits AmpC beta-lactamase; structure in first source
benzeneboronic acidboronic acids
1,1'-biphenyl-4-yl-boronic acid
palmostatin bpalmostatin B: inhibits acyl protein thioesterase 1; structure in first source
palmostatin mpalmostatin M: inhibits acyl protein thioesterases 1 and 2; structure in first source