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Related Concept Videos

Golgi Apparatus01:49

Golgi Apparatus

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.The Golgi apparatus is a major sorting and dispatch station for the products of the ER. Newly arriving vesicles enter...
Golgi Apparatus01:09

Golgi Apparatus

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...
Golgi Apparatus01:09

Golgi Apparatus

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...
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.
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
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...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

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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Related Experiment Video

Updated: Jul 2, 2026

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
13:08

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

Published on: August 10, 2017

WHAMMing into the Golgi.

Garret L Hayes1, Suzanne R Pfeffer

  • 1Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305-5307, USA.

Developmental Cell
|August 13, 2008
PubMed
Summary
This summary is machine-generated.

Researchers identified WHAMM, a protein that promotes actin polymerization and organizes microtubules, impacting Golgi complex structure and function. This discovery highlights the cytoskeleton

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Last Updated: Jul 2, 2026

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
13:08

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Published on: August 10, 2017

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP
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Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells

Published on: February 21, 2019

Area of Science:

  • Cell biology
  • Cytoskeletal dynamics
  • Secretory pathway organization

Background:

  • The Golgi complex is crucial for protein modification and transport.
  • Cytoskeletal elements like actin and microtubules play roles in organelle positioning and function.
  • Actin nucleation-promoting factors regulate actin dynamics.

Purpose of the Study:

  • To identify novel proteins involved in Golgi complex organization.
  • To elucidate the role of WHAMM in cytoskeletal regulation and secretory pathway function.

Main Methods:

  • Protein identification and characterization.
  • Biochemical assays for actin polymerization and microtubule binding.
  • Cellular imaging to assess WHAMM localization and Golgi structure.

Main Results:

  • WHAMM (Waste Hexagonal And Microtubule-associated protein) was identified as a multifunctional protein.
  • WHAMM stimulates Arp2/3-mediated actin polymerization.
  • WHAMM binds and organizes microtubules and influences Golgi complex structure and efficiency.
  • WHAMM localizes to the Golgi complex entry face, a novel finding for actin nucleation-promoting factors.

Conclusions:

  • WHAMM is a key regulator linking actin dynamics and microtubule organization to Golgi complex function.
  • The localization of WHAMM highlights the critical role of the cytoskeleton in organizing the secretory pathway.