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Related Concept Videos

Lipids as Anchors01:32

Lipids as Anchors

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...
Asymmetric Lipid Bilayer01:35

Asymmetric Lipid Bilayer

Biological membranes show uneven distribution of different types of lipids in the inner and outer layers, resulting in transverse asymmetric membranes. The treatment of the erythrocyte membrane with the enzyme phospholipase confirmed the asymmetric nature of the lipid bilayer. The enzyme hydrolyzes lipids into fatty acids and hydrophilic groups. The phospholipase acts only on the outer layer of the membrane, while the inner layer remains intact. The phospholipase treatment resulted in 80%...
GPI Anchoring of Proteins in the ER Membrane01:29

GPI Anchoring of Proteins in the ER Membrane

GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

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...
Membrane Domains01:18

Membrane Domains

The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...

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Detection of Protein S-Acylation using Acyl-Resin Assisted Capture
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Detection of Protein S-Acylation using Acyl-Resin Assisted Capture

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What does S-palmitoylation do to membrane proteins?

Sanja Blaskovic1, Mathieu Blanc, F Gisou van der Goot

  • 1Global Health Institute, Ecole Polytechnique Fédérale de Lausanne, Switzerland.

The FEBS Journal
|April 5, 2013
PubMed
Summary

S-palmitoylation, a reversible protein modification, acts as a molecular switch. For transmembrane proteins, this lipid modification influences conformation, membrane interactions, and protein associations, impacting cellular signaling.

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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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Acyl-PEGyl Exchange Gel Shift Assay for Quantitative Determination of Palmitoylation of Brain Membrane Proteins

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • S-palmitoylation is a reversible post-translational modification involving the addition of a C16 acyl chain to cysteines.
  • Unlike other lipid modifications, its reversibility allows it to function as a regulatory switch, akin to phosphorylation or ubiquitination.
  • While its role in soluble proteins is understood, its impact on transmembrane proteins remains less clear.

Purpose of the Study:

  • To review current knowledge on enzymes involved in S-palmitoylation and despalmitoylation.
  • To describe observed consequences of S-palmitoylation on membrane proteins.
  • To propose mechanistic consequences of S-palmitoylation for transmembrane proteins.

Main Methods:

  • Literature review of enzymes responsible for palmitate addition and removal.
  • Analysis of reported effects of S-palmitoylation on membrane proteins.
  • Theoretical proposal of direct mechanistic consequences.

Main Results:

  • Identified enzymes responsible for S-palmitoylation and its removal.
  • Documented various effects of S-palmitoylation on membrane proteins.
  • Proposed four non-mutually exclusive mechanistic consequences of S-palmitoylation on transmembrane proteins.

Conclusions:

  • S-palmitoylation is a reversible lipid modification acting as a regulatory switch.
  • Direct effects of S-palmitoylation on transmembrane proteins may include altered conformation, membrane domain association, protein interactions, and interplay with other modifications.