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Related Concept Videos

Transport Across the Golgi01:26

Transport Across the Golgi

5.8K
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 Apparatus01:49

Golgi Apparatus

99.6K
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

21.0K
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...
21.0K
Overview of Protein Sorting and Transport01:45

Overview of Protein Sorting and Transport

21.4K
Eukaryotic cells have different membrane-bound organelles with distinct protein requirements. The process by which proteins are targeted to a specific organelle is called protein sorting.
Protein sorting can be of two types: signal-based sorting and vesicle-based trafficking. In signal-based sorting, specific amino acid sequences called sorting signals target proteins to the proper location inside the cell either via gated transport or by protein translocation.  In gated transport, folded...
21.4K
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

3.0K
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...
3.0K
Introduction to Membrane Traffic01:44

Introduction to Membrane Traffic

9.2K
The ER, Golgi apparatus, endosomes, and lysosomes work in tandem to modify, sort, and package proteins and lipids. An integrated membrane trafficking network facilitates the back and forth shuttling of molecules within different organelles in the same cell or across the cell membrane.
The transport of soluble and membrane proteins is mediated by transport vesicles that collect cargo from one cellular compartment and deliver it to another by fusing with the target organelle membrane. The Rab...
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Related Experiment Video

Updated: Jan 5, 2026

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-to-Golgi Transport: A Sizeable Problem.

Janine McCaughey1, David J Stephens1

  • 1Cell Biology Laboratories, School of Biochemistry, Faculty of Life Sciences, University Walk, University of Bristol, Bristol BS8 1TD, UK.

Trends in Cell Biology
|October 22, 2019
PubMed
Summary
This summary is machine-generated.

Metazoans need to secrete large extracellular matrix (ECM) proteins for development. New research challenges traditional models of ECM protein transport, suggesting novel mechanisms at the endoplasmic reticulum (ER)-Golgi interface.

Keywords:
COPIIGolgicollagenendoplasmic reticulumtraffickingvesicle

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Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells
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Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells

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Live-cell Imaging of Endocytic Transport using Functionalized Nanobodies in Cultured Cells
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Related Experiment Videos

Last Updated: Jan 5, 2026

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
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Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells
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Live-cell Imaging of Endocytic Transport using Functionalized Nanobodies in Cultured Cells
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Live-cell Imaging of Endocytic Transport using Functionalized Nanobodies in Cultured Cells

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Developmental Biology

Background:

  • Metazoans rely on regulated secretion of extracellular matrix (ECM) for tissue function and development.
  • Secreting large ECM proteins, like procollagen, poses significant challenges to cellular transport machinery.
  • The precise spatiotemporal organization of the endoplasmic reticulum (ER)-Golgi interface in this process remains incompletely understood.

Purpose of the Study:

  • To review and discuss current models of ER-Golgi transport dynamics.
  • To highlight recent advances in understanding the secretion of large ECM proteins.
  • To challenge established concepts of vesicular transport for matrix proteins.

Main Methods:

  • Review of recent literature.
  • Analysis of findings from gene engineering studies.
  • Interpretation of super-resolution microscopy data.

Main Results:

  • Recent advances reveal the complex spatiotemporal organization of the ER-Golgi interface.
  • Established models of vesicular transport for large ECM proteins are being challenged.
  • Evidence suggests the involvement of less-defined carriers and direct organelle connections.

Conclusions:

  • The transport of large ECM proteins is more complex than previously thought.
  • Novel mechanisms, potentially involving direct ER-Golgi connections, are implicated in ECM secretion.
  • Further research is needed to fully elucidate the dynamics of ER-Golgi transport for matrix proteins.