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Related Concept Videos

Lipids as Anchors01:32

Lipids as Anchors

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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...
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Protein Import into the Peroxisomes01:27

Protein Import into the Peroxisomes

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Cells contain membrane-bound organelles called peroxisomes that oxidize organic molecules by transferring hydrogen atoms to oxygen, producing hydrogen peroxide. Peroxisomes enzymatically convert the released hydrogen peroxide into water and oxygen.
Peroxisomal Protein Import:
Peroxisomes lack the genetic machinery required to code for their own proteins. Hence, most peroxisomal membrane, lumenal and transmembrane proteins are synthesized in the cytoplasm or ER and transported to the peroxisome...
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Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

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Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
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Cytoskeletal Linker Proteins - Plakins01:09

Cytoskeletal Linker Proteins - Plakins

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Plakins are large proteins with binding domains for microtubules, microfilaments, intermediate filaments, and membrane-associated protein complexes at cell junctions. Plakin functions are evolutionarily conserved and are primarily involved in organizing the different components of the cytoskeleton by crosslinking them to each other and connecting them to the cell-matrix and cell adhesion complexes. They are also known to interact with signal transducers, serve as scaffolds for signaling...
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Inborn Errors of Metabolism01:20

Inborn Errors of Metabolism

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Phenylketonuria (PKU) is a protein metabolism disorder characterized by high blood levels of the amino acid phenylalanine. This results from a mutation in the gene responsible for phenylalanine hydroxylase, an enzyme that converts phenylalanine into tyrosine. When this enzyme is deficient, phenylalanine builds up in the blood, leading to symptoms such as vomiting, rashes, seizures, growth deficiency, and severe mental retardation. An early diagnosis and a diet restricting phenylalanine intake...
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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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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.
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Related Experiment Video

Updated: Apr 26, 2026

Detection of Protein Palmitoylation in Cultured Hippocampal Neurons by Immunoprecipitation and Acyl-Biotin Exchange ABE
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Detection of Protein Palmitoylation in Cultured Hippocampal Neurons by Immunoprecipitation and Acyl-Biotin Exchange ABE

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Palmitoylation and depalmitoylation defects.

Thorsten Hornemann1

  • 1Institute for Clinical Chemistry, University Hospital Zurich, Raemistrasse 100, CH-8091, Zurich, Switzerland, thorsten.hornemann@usz.ch.

Journal of Inherited Metabolic Disease
|August 6, 2014
PubMed
Summary

Palmitoylation, the attachment of fatty acids to proteins, is crucial for neuronal function. Defects in this process and its reversal are linked to human diseases, highlighting its pathological significance.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Palmitoylation is the enzymatic attachment of fatty acids to proteins, occurring in eukaryotes.
  • It can be reversible (S-palmitoylation) or irreversible (N-palmitoylation).
  • S-palmitoylation is dynamically regulated by palmitoyl acyltransferases (PATs) and acyl protein thioesterases.

Purpose of the Study:

  • To review the pathological changes associated with defects in protein palmitoylation and depalmitoylation.
  • To highlight the critical role of enzymes regulating protein palmitoylation in biological processes.
  • To discuss the link between palmitoylation-related genes and human diseases.

Main Methods:

  • Literature review of scientific articles on protein palmitoylation.

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Detection of Protein S-Acylation using Acyl-Resin Assisted Capture
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Detection of Protein Palmitoylation in Cultured Hippocampal Neurons by Immunoprecipitation and Acyl-Biotin Exchange ABE
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Acyl-PEGyl Exchange Gel Shift Assay for Quantitative Determination of Palmitoylation of Brain Membrane Proteins
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Detection of Protein S-Acylation using Acyl-Resin Assisted Capture
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  • Analysis of studies linking palmitoylation enzymes to cellular functions.
  • Compilation of data on human diseases associated with palmitoylation gene defects.

    • Main Results:

    • Protein palmitoylation dynamically regulates neuronal protein assembly and localization.
    • Eight palmitoylation-related genes have been identified as associated with human diseases.
    • Dysregulation of palmitoylation/depalmitoylation contributes to various pathological conditions.

    Conclusions:

    • Protein palmitoylation is essential for normal cellular function, particularly in neurons.
    • Defects in the palmitoylation pathway are implicated in human pathologies.
    • Further research into palmitoylation is crucial for understanding and treating related diseases.