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Related Concept Videos

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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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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Coat Assembly and GTPases01:33

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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
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GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
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Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
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Asparagusic Golgi Trackers.

Saidbakhrom Saidjalolov1, Xiao-Xiao Chen1, Julia Moreno1

  • 1Department of Organic Chemistry, University of Geneva, CH-1211 Geneva, Switzerland.

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|November 1, 2024
PubMed
Summary
This summary is machine-generated.

Thiol-mediated uptake (TMU) of asparagusic acid derivatives (AspA) occurs in the Golgi apparatus via thioester exchange. New AspA probes enable selective Golgi labeling for advanced microscopy, imaging cellular dynamics without genetic modification.

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Imaging

Background:

  • Thiol-mediated uptake (TMU) is a cellular process involving dynamic covalent exchange networks.
  • The precise cascade and final steps of TMU for asparagusic acid derivatives (AspA) were not fully understood.

Purpose of the Study:

  • To elucidate the complete cascade of TMU for AspA, identifying the terminal exchange partners and cellular location.
  • To develop novel AspA-based probes for selective and efficient labeling of the Golgi apparatus.

Main Methods:

  • Investigated the TMU cascade of AspA derivatives, focusing on disulfide and thioester exchange mechanisms.
  • Synthesized AspA conjugated with pH-sensitive fluoresceins, red-shifted silicon-rhodamines, and mechanosensitive flipper probes.
  • Utilized fluorescence microscopy, including stimulated emission depletion (STED) microscopy, in living and fixed cells.

Main Results:

  • Demonstrated that the AspA TMU cascade terminates in the Golgi apparatus (G) with a shift to thioester exchange involving palmitoyl transferases.
  • AspA probes selectively labeled the Golgi apparatus in various cell types without requiring cellular engineering.
  • AspA trackers exhibited high speed, simplicity, and compatibility with advanced imaging techniques like STED microscopy, and could discriminate Golgi/ER and cis/trans compartments.

Conclusions:

  • AspA probes provide a versatile tool for Golgi apparatus research, enabling visualization of cellular dynamics, membrane properties, and trafficking.
  • The developed probes facilitate imaging of Golgi morphology, anterograde vesicular trafficking, and membrane order/tension.
  • These AspA-based Golgi trackers offer significant advantages for studying Golgi function and TMU in biological systems.