Related Experiment Video
Updated: Jun 1, 2026
08:24
Imaging Molecular Adhesion in Cell Rolling by Adhesion Footprint Assay
Published on: September 27, 2021
Human glycolipid transfer protein (GLTP) expression modulates cell shape.
Yongguang Gao1, Taeowan Chung, Xianqiong Zou
1The Hormel Institute, University of Minnesota, Austin, Minnesota, United States of America.
Plos One
|June 1, 2011
Summary
Overexpression of glycolipid transfer protein (GLTP) dramatically alters cell shape, causing cells to round up. This phenotype is linked to GLTP
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Glycolipid transfer protein (GLTP) facilitates glycosphingolipid (GSL) transfer via its characteristic GLTP-fold.
- GLTP-folds are crucial for nonvesicular intracellular glycolipid trafficking and are found in proteins like FAPP2.
- The capacity of GLTP-folds to modify cell phenotype has not been previously investigated.
Purpose of the Study:
- To investigate the effects of human glycolipid transfer protein (GLTP) overexpression on cell phenotype.
- To determine the role of GLTP's lipid transfer activity and protein interactions in observed cellular changes.
- To identify potential protein partners regulating GLTP-mediated cellular responses.
Main Methods:
- Transfection of human cell lines (HeLa, HEK-293, A549) with GLTP and mutant constructs (W96A-GLTP).
- Phenotypic analysis of cell shape, motility (wound healing assays), and endocytosis (cholera toxin uptake).
- Yeast two-hybrid screening and immuno-pulldown assays to identify GLTP interacting proteins, including δ-catenin.
Main Results:
- GLTP overexpression induced a marked cell rounding phenotype in HeLa and HEK-293 cells within 48 hours.
- The cell rounding phenotype correlated with impaired motility and endocytosis but not increased apoptosis.
- GLTP's lipid transfer activity and interaction with δ-catenin were critical for inducing the rounded cell shape.
Conclusions:
- Human GLTP overexpression triggers significant cell shape alterations, representing the first described phenotypic changes associated with GLTP.
- The observed cell rounding is dependent on GLTP's glycolipid transfer capability and its interaction with δ-catenin.
- These findings reveal a novel regulatory mechanism involving GLTP and δ-catenin in modulating cell phenotype.
More Related Videos
Related Concept Videos
01:19Formation 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...
01:30Membrane 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...
01:29GPI 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,...
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,...
02:14GTPases and their Regulation
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, also known...
Large G-proteins, also known...
01:24Oligosaccharide Assembly
Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
Multiple sugar molecules that may or may...
01:05Proteoglycans
Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...