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Related Concept Videos

Golgi Matrix Proteins01:12

Golgi Matrix Proteins

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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.
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
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Golgi Apparatus01:49

Golgi Apparatus

99.4K
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 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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Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

16.1K
Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
16.1K
Transport Across the Golgi01:26

Transport Across the Golgi

5.7K
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...
5.7K
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

4.2K
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...
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Related Experiment Video

Updated: Dec 28, 2025

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
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Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass

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ER-Golgi membrane contact sites.

Rossella Venditti1,2, Maria Chiara Masone1, Maria Antonietta De Matteis1,2

  • 1Telethon Institute of Genetics and Medicine, Pozzuoli (Naples), Italy.

Biochemical Society Transactions
|February 18, 2020
PubMed
Summary
This summary is machine-generated.

Membrane contact sites (MCSs) between the endoplasmic reticulum (ER) and Golgi apparatus are crucial for cell function. Recent studies reveal their structure, components, and roles in lipid transfer, though regulation and TGN functions need further investigation.

Keywords:
endoplasmic reticulumgolgi apparatusmembrane contact sitesphosphatidylinositol

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Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays
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Related Experiment Videos

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Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
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Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays
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Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Organelle Biology

Background:

  • Membrane contact sites (MCSs) are specialized regions where organelle membranes appose, facilitating molecular exchange.
  • ER-Golgi MCSs, known since the 1960s, have been challenging to study due to methodological limitations.
  • These sites involve tethers, functional proteins (lipid/ion exchange), and regulatory enzymes.

Purpose of the Study:

  • To report recent advancements in understanding ER-Golgi MCSs.
  • To identify key morphological features, components, and functions of these MCSs.
  • To highlight remaining questions regarding their regulation and role in TGN functions.

Main Methods:

  • Utilized advanced methodological approaches to visualize and study ER-Golgi MCSs.
  • Characterized the morphological features of these specific MCSs.
  • Identified key protein components and their functional roles.

Main Results:

  • Progress has been made in visualizing and characterizing ER-Golgi MCSs.
  • Lipid transfer proteins and their exchange functions at MCSs are relatively well-understood.
  • The study identified some components and roles of ER-Golgi MCSs.

Conclusions:

  • ER-Golgi MCSs are crucial for cellular processes, particularly lipid exchange.
  • Significant unknowns remain concerning the regulation of these MCSs.
  • Further research is needed to elucidate their role in TGN sorting, trafficking, and disease.