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Related Concept Videos

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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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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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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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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COP Coated Vesicles00:59

COP Coated Vesicles

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Membrane-enclosed structures called vesicles transport proteins and lipids across the cell. The vesicles derive their cargo from the plasma membrane, Golgi, ER, or endosome. Coated vesicles are spherical, protein-coated carriers with a 50–100 nm diameter that mediate bidirectional transport between the ER and the Golgi. The distribution of proteins between the ER and Golgi complex is dynamic and is maintained by different coated vesicles. Their formation is driven by the assembly of...
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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.
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Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
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COPI is essential for Golgi cisternal maturation and dynamics.

Midori Ishii1, Yasuyuki Suda2, Kazuo Kurokawa3

  • 1Live Cell Super-Resolution Imaging Research Team, RIKEN Center for Advanced Photonics, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.

Journal of Cell Science
|July 23, 2016
PubMed
Summary

Coat protein complex I (COPI) is essential for Golgi cisternal maturation. Depleting COPI proteins disrupts protein transport and Golgi dynamics, highlighting its role in retrograde trafficking.

Keywords:
COPICisternal maturationGolgi

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Trafficking

Background:

  • Proteins synthesized in the endoplasmic reticulum (ER) undergo maturation and sorting within the Golgi apparatus.
  • Cisternal maturation is a key mechanism for Golgi protein transport, involving retrograde movement of proteins.
  • Coat protein complex I (COPI)-coated vesicles are implicated as carriers for this retrograde transport.

Purpose of the Study:

  • To directly investigate the function of COPI in Golgi cisternal maturation.
  • To elucidate the role of COPI in the retrograde transport of Golgi-resident proteins.
  • To understand COPI's impact on the dynamics of Golgi cisternae.

Main Methods:

  • Utilized 4D live-cell imaging to observe transmembrane Golgi-resident proteins in yeast.
  • Employed COPI temperature-sensitive mutants and induced protein degradation to reduce COPI function.
  • Assessed the effects of COPI subunit inactivation (Ret1, Sec21) on cisternal progression and dynamics.

Main Results:

  • Inactivation of COPI subunits Ret1 and Sec21 significantly hindered the transition of cisternae from cis to medial and trans Golgi.
  • Depletion of COPI subunits severely restricted the movement of Golgi cisternae within the cytoplasm.
  • Demonstrated a direct link between COPI function and the progression through Golgi compartments.

Conclusions:

  • COPI proteins play an essential role in the retrograde trafficking of Golgi-resident proteins.
  • COPI is crucial for maintaining the dynamic nature and structural integrity of Golgi cisternae.
  • These findings underscore the critical involvement of COPI in Golgi apparatus function and protein sorting.