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Related Concept Videos

Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
COP Coated Vesicles00:59

COP Coated Vesicles

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 different...
Transport Across the Golgi01:26

Transport Across the Golgi

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...
Golgi Matrix Proteins01:12

Golgi Matrix Proteins

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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Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

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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Clathrin Coated Vesicles

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Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
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Coat-tether interaction in Golgi organization.

Yusong Guo1, Vasu Punj, Debrup Sengupta

  • 1Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA 15213, USA.

Molecular Biology of the Cell
|April 25, 2008
PubMed
Summary
This summary is machine-generated.

Golgi apparatus organization relies on the COPI coat complex and the p115 tethering factor. Their interaction, mediated by specific motifs, is crucial for vesicle tethering and Golgi biogenesis.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Golgi apparatus biogenesis is essential for cellular function.
  • The COPI vesicle coat complex is implicated in Golgi organization, but its mechanism remains unclear.
  • The vesicle tethering factor p115 plays a role in Golgi structure.

Purpose of the Study:

  • To elucidate the mechanism by which the COPI coat complex mediates Golgi apparatus biogenesis.
  • To investigate the interaction between COPI subunits and vesicle tethering factors.
  • To identify the molecular determinants of Golgi organization.

Main Methods:

  • Structural modeling of the COPI subunit betaCOP.
  • Gene replacement studies with mutated betaCOP versions.
  • Co-immunoprecipitation assays to detect protein interactions.
  • Inhibition assays using specific peptide motifs in permeabilized cells.

Main Results:

  • A conserved FW motif in betaCOP's C-terminal appendage domain was identified.
  • Mutations in the betaCOP FW motif disrupted Golgi organization, similar to p115 depletion.
  • betaCOP directly binds to p115, dependent on the betaCOP FW motif and p115's head domain (E(19)E(21)).
  • Specific inhibitors targeting the betaCOP FW motif or p115 EE motif impaired Golgi assembly.

Conclusions:

  • Golgi organization is dependent on the interaction between betaCOP and p115.
  • Vesicle tethering at the Golgi likely involves direct binding of p115 to the COPI coat.
  • The identified interaction provides a mechanistic link between COPI function and Golgi biogenesis.