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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 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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Protein Folding Quality Check in the RER01:29

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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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Vesicular Tubular Clusters01:45

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After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
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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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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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Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
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The Dsc complex and its role in Golgi quality control.

Yannick Weyer1, David Teis1

  • 1Institute of Molecular Biochemistry, Biocenter, Medical University of Innsbruck, 6020 Innsbruck, Austria.

Biochemical Society Transactions
|September 26, 2024
PubMed
Summary

Cellular quality control mechanisms prevent defective membrane proteins from accumulating. The defective for SREBP cleavage (Dsc) ubiquitin ligase complex at the Golgi apparatus specifically targets orphaned proteins, preventing cellular damage.

Keywords:
Golgiquality controlubiquitin

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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Protein Quality Control

Background:

  • Membrane proteins are essential for cellular functions, but their synthesis, folding, and trafficking are error-prone.
  • Defective or mis-localized membrane proteins can compromise organelle integrity and cellular health.
  • Cellular quality control systems are crucial for managing these proteins.

Purpose of the Study:

  • To review the mechanisms of selective membrane protein quality control.
  • To highlight the role of the Golgi apparatus in this process.
  • To focus on the defective for SREBP cleavage (Dsc) ubiquitin ligase complex in detecting orphaned proteins.

Main Methods:

  • Review of existing literature on membrane protein quality control.
  • Focus on endoplasmic reticulum (ER) to Golgi apparatus trafficking pathways.
  • Analysis of the function of the Dsc ubiquitin ligase complex.

Main Results:

  • Membrane protein biogenesis involves complex, error-prone steps.
  • Quality control mechanisms monitor folding, quantity, and localization.
  • The Golgi apparatus employs selective mechanisms, including the Dsc complex, to identify and eliminate defective membrane proteins.

Conclusions:

  • Selective membrane protein quality control at the Golgi is vital for cellular health.
  • The Dsc ubiquitin ligase complex plays a key role in detecting and degrading orphaned membrane proteins.
  • Preventing mis-localization of defective proteins maintains organelle integrity.