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Related Concept Videos

GPI Anchoring of Proteins in the ER Membrane01:29

GPI Anchoring of Proteins in the ER Membrane

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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,...
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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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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.
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IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

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Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and...
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Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
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GTPases and their Regulation02:14

GTPases and their Regulation

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Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒  small G-proteins consisting of a single domain and large multi-domain G-proteins.
Large G-proteins,...
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Related Experiment Video

Updated: Aug 2, 2025

Comparing the Affinity of GTPase-binding Proteins using Competition Assays
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Comparing the Affinity of GTPase-binding Proteins using Competition Assays

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GPI anchors: Regulated as needed.

Auxiliadora Aguilera-Romero1,2, Manuel Muñiz1,2

  • 1Department of Cell Biology, Faculty of Biology, University of Seville, Seville, Spain.

The Journal of Cell Biology
|April 13, 2023
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Summary
This summary is machine-generated.

Researchers discovered a new way cells control the creation of GPI anchors, which attach proteins to cell membranes. This finding reveals a novel on-demand regulation of GPI precursor biosynthesis.

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Glycosylphosphatidylinositol (GPI) anchoring is a crucial post-translational modification in eukaryotic cells.
  • GPI anchors link cell surface proteins to the plasma membrane, playing vital roles in cell signaling and adhesion.

Purpose of the Study:

  • To investigate the regulatory mechanisms governing GPI anchor biosynthesis.
  • To identify novel control points in the production of GPI glycolipid precursors.

Main Methods:

  • The study by Liu et al. (2023) employed advanced molecular and cell biology techniques.
  • Investigated the biosynthesis pathway of GPI glycolipid precursors.

Main Results:

  • The research suggests, for the first time, an "on-demand" regulation of GPI glycolipid precursor biosynthesis.
  • This indicates a dynamic control system for GPI anchor production.

Conclusions:

  • The findings reveal a previously unknown layer of regulation in GPI anchor modification.
  • This discovery opens new avenues for understanding cell surface protein localization and function.