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Related Concept Videos

Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
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Structure of Porins01:21

Structure of Porins

Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel precursors...
The Endoplasmic Reticulum01:43

The Endoplasmic Reticulum

The endoplasmic reticulum or ER makes up for more than half of the membranes in a cell and accounts for 10% of total cell volume. It is also the primary protein and lipid synthesis factory for most cell organelles, such as the Golgi apparatus, lysosomes, secretory vesicles, and the plasma membrane. Despite being the most extensive and functionally complex subcellular organelle, ER was the last to be discovered. After years of deliberation, Keith Porter and George Palade in the year 1954,...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...

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Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells
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The structure and function of the retromer protein complex.

Brett M Collins1

  • 1Institute for Molecular Bioscience, The University of Queensland, St Lucia, Brisbane, Queensland 4072, Australia. b.collins@imb.uq.edu.au

Traffic (Copenhagen, Denmark)
|June 11, 2008
PubMed
Summary

Retromer, a protein complex, sorts transmembrane proteins within the endosomal system. Its crucial role in endosome-to-Golgi transport is conserved across eukaryotes, aiding in mechanistic understanding.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Trafficking

Background:

  • Endosomal sorting of transmembrane proteins is vital for cellular function.
  • Protein assemblies regulate the transport of cargo through the endosomal system.
  • Retromer is a key peripheral membrane protein complex involved in this process.

Purpose of the Study:

  • To elucidate the role of retromer in endosomal sorting and protein transport.
  • To investigate the structural basis of retromer function.
  • To understand retromer's mechanism in endosome-to-Golgi retrieval.

Main Methods:

  • Structural studies of the core retromer complex.
  • Analysis of retromer's interactions with cargo molecules.
  • Comparative analysis with other membrane trafficking regulators.

Main Results:

  • Retromer mediates endosome-to-Golgi retrieval of lysosomal hydrolase receptors and other proteins.
  • Its function is conserved across diverse eukaryotic organisms.
  • Structural studies reveal similarities and differences with other trafficking machinery.

Conclusions:

  • Retromer plays a fundamental role in eukaryotic endosomal transport.
  • Structural insights are paving the way for a mechanistic understanding of retromer.
  • Further research on retromer will illuminate broader principles of membrane trafficking.