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Related Concept Videos

Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
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...
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...
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

Overview

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Related Experiment Video

Updated: Jul 3, 2026

Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis
07:31

Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis

Published on: July 16, 2020

Structural changes of membrane-anchored native PrP(C).

Kerstin Elfrink1, Julian Ollesch, Jan Stöhr

  • 1Institut fuer Physikalische Biologie, Heinrich-Heine-Universitaet Duesseldorf, Universitaetsstrasse 1, 40225 Duesseldorf, Germany.

Proceedings of the National Academy of Sciences of the United States of America
|August 2, 2008
PubMed
Summary
This summary is machine-generated.

Cellular prion protein refolding into beta-sheets is induced by lipid membrane anchoring. This membrane-specific transition, absent in solution, may be crucial for prion diseases development.

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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

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Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis
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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

Area of Science:

  • Biochemistry
  • Neuroscience
  • Structural Biology

Background:

  • Protein misfolding and aggregation are implicated in neurodegenerative disorders like Alzheimer and prion diseases.
  • Previous prion protein studies often lacked essential posttranslational modifications, such as the lipid anchor.

Purpose of the Study:

  • To investigate the secondary structure changes of a fully posttranslationally modified cellular prion protein upon binding to a raft-like lipid membrane.
  • To understand the role of the glycosylphosphatidylinositol (GPI) anchor in prion protein-membrane interactions and structural transitions.

Main Methods:

  • Utilized time-resolved Fourier-transform infrared (FTIR) spectroscopy.
  • Studied a cellular prion protein featuring N-glycosylations and its natural GPI anchor.
  • Analyzed membrane anchoring effects using molecular sensitivity.

Main Results:

  • Membrane anchoring, above a specific concentration threshold, induced prion protein refolding into intermolecular beta-sheets.
  • This beta-sheet transition was observed exclusively upon membrane binding and not in solution.
  • The study highlights a membrane-specific conformational change.

Conclusions:

  • Lipid membrane anchoring can trigger a significant structural transition in the cellular prion protein.
  • This membrane-induced refolding into beta-sheets is a critical event potentially contributing to the pathogenesis of prion diseases.
  • The GPI anchor plays a key role in mediating these disease-relevant structural changes.