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Related Concept Videos

Golgi Apparatus01:49

Golgi Apparatus

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As they leave the Endoplasmic Reticulum (ER), properly folded and assembled proteins are selectively packaged into vesicles. These vesicles are transported by microtubule-based motor proteins and fuse together to form vesicular tubular clusters, subsequently arriving at the Golgi apparatus, a eukaryotic endomembrane organelle that often has a distinctive ribbon-like appearance.
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Golgi Apparatus01:09

Golgi Apparatus

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Properly folded and assembled proteins are selectively packaged into vesicles that exit the ER. Motor proteins transport these vesicles to the Golgi apparatus for adding modifications that make these proteins functional at their destination.
The Golgi apparatus is a eukaryotic organelle that has a distinctive ribbon-like appearance. It is a primary sorting and dispatch station for cargo arriving from the ER. Newly arriving vesicles enter the cis face of the Golgi, closest to the ER, and are...
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Transport Across the Golgi01:26

Transport Across the Golgi

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While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
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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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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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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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Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
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Sending out molecules from the TGN.

Bulat R Ramazanov1, Mai Ly Tran1, Julia von Blume1

  • 1Department of Cell Biology, Yale University School of Medicine, New Haven, CT, USA.

Current Opinion in Cell Biology
|March 11, 2021
PubMed
Summary

Understanding how soluble proteins are sorted and exported from the trans-Golgi network (TGN) is key. Novel protein/lipid machinery and TGN dynamics, including TGN/ER contact sites, are crucial for this process.

Keywords:
Cargo sortingER-TGN contact sitesGolgi apparatusLipid domainsSecreted proteinsTGN

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The sorting and export of secreted cargo proteins from the trans-Golgi network (TGN) is critical for cellular function and organismal health.
  • Misfolded or mis-sorted proteins can lead to diseases like cancer and neurological disorders.
  • While transmembrane protein sorting is understood, the mechanisms for soluble protein export remain largely unknown.

Purpose of the Study:

  • To review recent advancements in understanding the sorting and export of soluble proteins from the TGN.
  • To highlight novel protein and lipid machinery involved in cargo packing into TGN-derived vesicles.
  • To explore the role of TGN structure, dynamics, and TGN/endoplasmic reticulum (ER) contact sites in protein export.

Main Methods:

  • Literature review of recent research in membrane trafficking and protein sorting.
  • Analysis of studies identifying novel protein and lipid factors in TGN cargo packaging.
  • Examination of research linking TGN structural dynamics and TGN/ER contact sites to protein export.

Main Results:

  • Identification of novel protein and lipid machinery facilitating the packaging of soluble proteins into TGN-derived transport carriers.
  • Uncovered link between cargo sorting and export processes.
  • Significant role of TGN structure, dynamics, and TGN/ER contact sites in efficient protein export.

Conclusions:

  • Recent progress has shed light on the mechanisms of soluble protein sorting and export from the TGN.
  • Novel molecular players and structural TGN features are crucial for efficient secretion.
  • Further research into these mechanisms holds promise for understanding and treating secretion-related diseases.