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Related Concept Videos

Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

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Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
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Protein Translocation Machinery on the ER Membrane01:28

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

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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.
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Septins01:19

Septins

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Septins are protein filaments forming the cytoskeleton along with the microtubules, microfilaments, intermediate filaments, and other accessory proteins. In 1971 while studying the cell division cycle in mutant Saccharomyces cerevisiae Harwell et al. first identified the septin-related genes playing a crucial role in yeast cytokinesis. Fluorescence microscopy revealed that these proteins localize at the budding neck as rings. These ring-like proteins were then named Septins by John Pringle, and...
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Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

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Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
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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
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Related Experiment Video

Updated: Jul 10, 2025

Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution
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Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution

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Structural Study of the Exocyst Subunit Human Sec6.

Jiatian Guo1, Kunrong Mei1

  • 1School of Pharmaceutical Science and Technology, Tianjin University, Tianjin, China.

Studies in Health Technology and Informatics
|November 26, 2023
PubMed
Summary

The exocyst complex

Area of Science:

  • Cell biology
  • Molecular biology
  • Biochemistry

Background:

  • Vesicular transport is essential for eukaryotic cell function.
  • The exocyst complex mediates secretory vesicle tethering to the plasma membrane during exocytosis.
  • Understanding exocyst complex assembly and its interaction with SNARE proteins is crucial.

Purpose of the Study:

  • To investigate the structure of the human exocyst subunit Sec6 (HuSec6).
  • To generate truncated forms of HuSec6 for structural analysis.
  • To provide a foundation for studying exocyst-SNARE interactions.

Main Methods:

  • Bioinformatics analysis to design truncated HuSec6 constructs.
  • Protein expression and purification in E. coli.
  • X-ray diffraction for crystal structure determination.
Keywords:
ExocystX-ray diffractionbioinformation analysiscrystalprotein purificationsubunit

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Main Results:

  • Two truncated forms of HuSec6 (HuSec6 121-734 and HuSec6 121-745) were successfully designed.
  • Proteins were expressed and purified to >95% purity.
  • Protein crystals suitable for X-ray diffraction were obtained, yielding data to ~9 Å resolution.

Conclusions:

  • The study successfully produced truncated HuSec6 proteins and crystals.
  • These findings lay the groundwork for future crystal structure analysis of HuSec6.
  • This research will aid in elucidating the exocyst complex assembly and its role in vesicular transport.