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Related Concept Videos

Membrane Proteins01:30

Membrane Proteins

Plasma membranes have integral transmembrane proteins involved in facilitated transport. These proteins are collectively referred to as transport proteins, and they function as either channels for the material or as carriers themselves. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids and a hydrophilic channel through their core that provides a hydrated opening for solutes to pass through the membrane layers. Passage through the channel allows...
Formation of Lipopolysaccharides01:19

Formation of Lipopolysaccharides

Lipopolysaccharides (LPS) are crucial components of the outer membrane of Gram-negative bacteria, serving both structural and functional roles. It contributes to membrane stability and protects bacteria from host immune responses. LPS is composed of three major regions—lipid A, a core oligosaccharide, and an O antigen. The biosynthesis and assembly of LPS involve a highly coordinated set of enzymatic reactions and transport mechanisms. Additionally, LPS is recognized as an endotoxin, triggering...
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,...
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...
Membrane Asymmetry Regulating Transporters01:19

Membrane Asymmetry Regulating Transporters

Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

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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Related Experiment Video

Updated: Jul 16, 2026

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes
08:49

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes

Published on: March 14, 2021

Glycolipid transfer proteins.

Rhoderick E Brown1, Peter Mattjus

  • 1The Hormel Institute, University of Minnesota-Hormel Institute, 801 16th Ave NE, Austin, MN 55912, USA. reb@umn.edu

Biochimica Et Biophysica Acta
|February 27, 2007
PubMed
Summary

Glycolipid transfer proteins (GLTPs) accelerate glycolipid transfer between membranes. Their unique structure and function establish GLTPs as a new eukaryotic protein superfamily with an enigmatic biological role.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Glycolipid transfer proteins (GLTPs) are small, soluble proteins facilitating intermembrane glycolipid transfer in vitro.
  • GLTPs exhibit specificity for beta-linked glycolipids, encompassing both sphingoid and glycerol backbones.
  • While biochemical properties are well-studied, the precise biological function of GLTP remains elusive.

Purpose of the Study:

  • To elucidate the structural and functional characteristics of Glycolipid Transfer Proteins (GLTPs).
  • To differentiate GLTPs from other known glycolipid-binding proteins.
  • To establish GLTPs as a distinct protein superfamily.

Main Methods:

  • 3D structural analysis of GLTPs.
  • Biochemical assays to study membrane surface interactions.

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Arabidopsis thaliana Polar Glycerolipid Profiling by Thin Layer Chromatography (TLC) Coupled with Gas-Liquid Chromatography (GLC)

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Defining Substrate Specificities for Lipase and Phospholipase Candidates
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Defining Substrate Specificities for Lipase and Phospholipase Candidates

Published on: November 23, 2016

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Last Updated: Jul 16, 2026

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes
08:49

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes

Published on: March 14, 2021

Arabidopsis thaliana Polar Glycerolipid Profiling by Thin Layer Chromatography (TLC) Coupled with Gas-Liquid Chromatography (GLC)
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Arabidopsis thaliana Polar Glycerolipid Profiling by Thin Layer Chromatography (TLC) Coupled with Gas-Liquid Chromatography (GLC)

Published on: March 18, 2011

Defining Substrate Specificities for Lipase and Phospholipase Candidates
08:59

Defining Substrate Specificities for Lipase and Phospholipase Candidates

Published on: November 23, 2016

  • Comparative analysis with other lipid-binding proteins.

    • Main Results:

    • GLTPs possess a unique 3D architecture enabling specific glycolipid binding and membrane targeting.
    • Liganded structures reveal distinct lipid-binding modes.
    • GLTPs differ significantly from other known glycolipid-binding proteins.

    Conclusions:

    • GLTPs represent a novel protein superfamily in eukaryotes.
    • The unique structure of GLTP underpins its specialized glycolipid transfer function.
    • Further research is needed to fully understand the biological significance of GLTPs.