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Related Concept Videos

Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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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 Matrix Proteins01:12

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Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
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Directing Proteins to the Rough Endoplasmic Reticulum01:34

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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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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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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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Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
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Protein quality control at the Golgi.

Sinead Schwabl1, David Teis1

  • 1Institute for Cell Biology, Biocenter, Medical University of Innsbruck, Austria.

Current Opinion in Cell Biology
|April 1, 2022
PubMed
Summary
This summary is machine-generated.

Protein quality control (PQC) maintains cellular health by managing misfolded proteins within organelles. This review explores novel PQC mechanisms at the Golgi apparatus, crucial for protein sorting and degradation.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Eukaryotic cells meticulously manage their proteome, targeting most proteins to specific organelles.
  • Protein homeostasis (proteostasis) is vital, relying on organelle-specific protein quality control (PQC) machineries.
  • PQC systems detect and eliminate misfolded, orphaned, or mis-localized proteins, preventing cellular damage and disease.

Purpose of the Study:

  • To discuss emerging PQC mechanisms operating at the Golgi apparatus.
  • To highlight the Golgi's role as a central hub for protein sorting and modification.
  • To focus on specific Golgi PQC pathways involved in protein retrieval and degradation.

Main Methods:

  • Review of emerging literature on Golgi PQC.
  • Analysis of protein trafficking and degradation pathways.
  • Focus on ubiquitin-dependent and -independent degradation routes.

Main Results:

  • Emerging PQC mechanisms at the Golgi apparatus are being elucidated.
  • Golgi PQC pathways facilitate the retrieval of proteins to the endoplasmic reticulum.
  • Specific pathways extract membrane proteins for proteasomal degradation or target proteins to lysosomes.

Conclusions:

  • The Golgi apparatus employs sophisticated PQC machineries to maintain proteostasis.
  • These pathways are critical for preventing proteotoxicity and maintaining organelle integrity.
  • Understanding Golgi PQC offers insights into disease mechanisms and therapeutic strategies.