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Related Concept Videos

Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

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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...
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Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

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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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Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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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...
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Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

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Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
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Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

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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...
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ER Retrieval Pathway01:45

ER Retrieval Pathway

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In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
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Related Experiment Video

Updated: Oct 13, 2025

Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides
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Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides

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Collagen has a unique SEC24 preference for efficient export from the endoplasmic reticulum.

Chung-Ling Lu1, Steven Ortmeier2, Jon Brudvig2

  • 1Department of Biomedical Sciences, College of Veterinary Medicine, Iowa State University, Ames, Iowa, USA.

Traffic (Copenhagen, Denmark)
|November 11, 2021
PubMed
Summary

SEC24D mutations cause skeletal defects by impairing collagen secretion. Multiple SEC24 paralogs (A-D) handle collagen and fibronectin export, explaining tissue-specific disease phenotypes.

Keywords:
COPIISEC24collagenendoplasmic reticulumsecretiontissue specificity

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In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen
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Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
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Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides

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In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen
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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • SEC24 proteins are crucial for COPII vesicle assembly and cargo sorting.
  • Vertebrates have four SEC24 paralogs (SEC24A-D) in two subgroups: SEC24A/B and SEC24C/D.
  • SEC24D mutations are linked to human osteogenesis imperfecta and craniofacial dysplasia.

Purpose of the Study:

  • To investigate the roles of SEC24 paralogs in procollagen and fibronectin secretion.
  • To understand the basis for tissue-specific phenotypes in SEC24 deficiency disorders.

Main Methods:

  • Utilized Sec24d knockout (KO) mice and cultured cells.
  • Analyzed collagen and fibronectin secretion defects.
  • Examined endoplasmic reticulum (ER) export pathways.

Main Results:

  • SEC24D is essential for collagen secretion, as evidenced by mutant fish phenotypes.
  • SEC24A and SEC24B also contribute to procollagen ER export.
  • Fibronectin 1 export requires either SEC24C or SEC24D.
  • SEC24D patient fibroblasts showed milder secretion defects than expected, indicating tissue specificity.

Conclusions:

  • Procollagen interacts with multiple SEC24 paralogs (SEC24A, SEC24B, SEC24D) for efficient ER export.
  • The involvement of different SEC24 paralogs underlies tissue-specific phenotypes observed in SEC24 deficiency disorders.