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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.
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
Introduction to Membrane Traffic01:44

Introduction to Membrane Traffic

The ER, Golgi apparatus, endosomes, and lysosomes work in tandem to modify, sort, and package proteins and lipids. An integrated membrane trafficking network facilitates the back and forth shuttling of molecules within different organelles in the same cell or across the cell membrane.
The transport of soluble and membrane proteins is mediated by transport vesicles that collect cargo from one cellular compartment and deliver it to another by fusing with the target organelle membrane. The Rab...
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
Bacterial Translocation and Protein Secretion01:26

Bacterial Translocation and Protein Secretion

Bacterial protein secretion involves translocation systems to ensure proteins reach their designated locations, including the plasma membrane, periplasm, outer membrane, or the external environment. These translocation systems are vital for bacterial physiology, supporting processes like membrane assembly, enzymatic activity in the periplasm, and interactions with the external environment. The division of labor between Sec and Tat pathways ensures efficiency in handling proteins with diverse...
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...

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Related Experiment Video

Updated: May 14, 2026

Reconstitution of Msp1 Extraction Activity with Fully Purified Components
05:52

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Published on: August 10, 2021

Expanding proteostasis by membrane trafficking networks.

Darren M Hutt1, William E Balch

  • 1Department of Cell Biology and Department of Chemical Physiology, The Skaggs Institute for Chemical Biology and the Dorris Institute for Neurological Diseases, The Scripps Research Institute, La Jolla, California 92037, USA.

Cold Spring Harbor Perspectives in Biology
|February 22, 2013
PubMed
Summary

Proteostasis, essential for all life, is advanced in eukaryotes by a trafficking proteostasis network (TPN). This TPN utilizes membrane trafficking to create compartments, controlling protein folding and cellular function.

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Last Updated: May 14, 2026

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Using Caenorhabditis elegans as a Model System to Study Protein Homeostasis in a Multicellular Organism
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Using Caenorhabditis elegans as a Model System to Study Protein Homeostasis in a Multicellular Organism

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JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics
07:28

JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics

Published on: October 19, 2021

Area of Science:

  • Cell Biology
  • Biochemistry
  • Evolutionary Biology

Background:

  • Proteostasis, the maintenance of protein homeostasis, is fundamental across Archaea, Bacteria, and Eukarya.
  • Eukaryotes possess complex subcellular compartmentalization, unlike the single compartment of microbes.
  • The proteostasis network (PN) manages protein generation, protection, and degradation.

Purpose of the Study:

  • To investigate the role of membrane trafficking in eukaryotic proteostasis.
  • To propose the concept of a "trafficking PN" (TPN) as an advanced arm of the PN in eukaryotes.
  • To elucidate how TPN-generated compartments influence protein folding and cellular diversity.

Main Methods:

  • Examination of evidence linking coat, tether, and fusion (CTF) membrane trafficking components to the TPN.
  • Analysis of how TPN establishes compartments through integrated cargo-specific trafficking signatures (TRaCKS).
  • Application of the Anfinsen principle to understand the role of local environment in protein structure within TPN compartments.

Main Results:

  • Eukaryotic compartments are formed by CTF membrane trafficking, constituting the TPN.
  • TRaCKS dictate the temporal and spatial regulation of protein folding biology.
  • TPN-generated endomembrane compartments provide "quinary" structural control, modifying protein structures beyond primary sequence.

Conclusions:

  • The trafficking PN represents an evolutionarily advanced system for managing proteostasis in eukaryotes.
  • Endomembrane compartments, driven by the TPN, are crucial for eukaryotic function and diversity.
  • The concept of Anfinsen compartments unifies understanding of endomembrane biology's purpose.