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Related Concept Videos

Transport Across the Golgi01:26

Transport Across the Golgi

3.8K
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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Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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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.
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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Golgi Apparatus01:49

Golgi Apparatus

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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 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...
2.0K
Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

6.5K
Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
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COP Coated Vesicles00:59

COP Coated Vesicles

7.4K
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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Related Experiment Video

Updated: May 11, 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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Golgi Localized Arl15 Regulates Cargo Transport and Cell Adhesion.

Prerna Sharma1, Pooja Hoovina Venkatesh1, Shalini Samal1

  • 1Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore, India.

Traffic (Copenhagen, Denmark)
|April 17, 2025
PubMed
Summary

Arf-like 15 (Arl15) regulates Golgi cargo transport, impacting cell adhesion and spreading. Its depletion causes mislocalization of key proteins, affecting cell surface dynamics.

Keywords:
Arf1Arl15STX6 and cell tractionscaveolin‐2

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

  • Cell Biology
  • Molecular Biology
  • Biophysics

Background:

  • Arf-like GTPases (Arls) are crucial for membrane trafficking and cytoskeletal organization.
  • Arl15 has been genetically linked to type-2 diabetes and rheumatoid arthritis, but its function in vesicular transport is unclear.
  • Previous studies suggest Arl15 involvement in magnesium homeostasis and TGFβ signaling.

Purpose of the Study:

  • To elucidate the role of Arf-like 15 (Arl15) in vesicular transport and its impact on cellular mechanobiology.
  • To investigate the localization and functional requirements of Arl15 in the Golgi apparatus.
  • To determine the cellular consequences of Arl15 depletion on cell adhesion and spreading.

Main Methods:

  • Fluorescence microscopy of Arl15-GFP HeLa cells to determine localization.
  • Depletion studies using siRNA to assess Arl15 function.
  • Expression of dominant-negative Arl15 mutants to probe GTPase-independent roles.
  • Traction force microscopy to quantify cell adhesion and spreading forces.

Main Results:

  • Arl15 localizes to the Golgi and cell surface, with Golgi localization dependent on palmitoylation and Arf1.
  • Arl15 depletion leads to mislocalization of Golgi cargo, including caveolin-2 and STX6.
  • Cells depleted of Arl15 exhibit enhanced cell spreading and increased adhesion strength, generating higher tractions.

Conclusions:

  • Arf-like 15 (Arl15) plays a significant role in regulating cargo transport from the Golgi.
  • Arl15 influences cell surface processes, including cell adhesion and spreading, through its role in vesicular trafficking.
  • These findings link Arl15 function in protein trafficking to cellular mechanobiology and potential disease relevance.