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Related Concept Videos

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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Golgi Apparatus01:49

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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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Transport Across the Golgi01:26

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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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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.
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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
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Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
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Unlocking Golgi: Why Does Morphology Matter?

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Biochemistry. Biokhimiia
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Summary
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Golgi fragmentation during stress selectively mislocalizes giantin-sensitive enzymes by impairing docking sites. This alters protein processing, differing from cytoskeleton-induced disorganization and impacting cellular homeostasis.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Pathology

Background:

  • The Golgi apparatus is crucial for cellular homeostasis, protein modification, and trafficking.
  • Golgi structure relies on golgins, including giantin, GM130, and GRASPs, which form docking sites for ER-derived cargo.
  • Golgi disorganization is observed in various pathologies and during cell division.

Purpose of the Study:

  • To analyze clinically relevant observations linking Golgi fragmentation to altered protein processing.
  • To elucidate the molecular mechanisms behind Golgi disorganization in disease states.
  • To differentiate stress-induced Golgi fragmentation from cytoskeleton-mediated alterations.

Main Methods:

  • Literature review and analysis of clinically relevant observations.
  • Comparative analysis of Golgi fragmentation mechanisms.
  • Focus on the role of golgins (giantin, GM130, GRASPs) in Golgi organization and protein trafficking.

Main Results:

  • Golgi fragmentation in ER/Golgi stress impairs the giantin docking site but not the GM130-GRASP65 complex.
  • This leads to selective mislocalization of giantin-sensitive enzymes.
  • Altered protein processing occurs due to the loss of specific enzymes and the gain of others.
  • Stress-induced Golgi fragmentation differs from cytoskeleton-induced disorganization.

Conclusions:

  • Golgi fragmentation under stress fundamentally alters protein processing pathways.
  • The selective mislocalization of enzymes due to impaired giantin docking is a key mechanism.
  • Understanding these changes is critical for comprehending Golgi's role in disease and cellular homeostasis.