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Related Concept Videos

Transport Across the Golgi01:26

Transport Across the Golgi

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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

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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

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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 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.
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Golgi Apparatus01:09

Golgi Apparatus

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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.
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Related Experiment Video

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Application of High-speed Super-resolution SPEED Microscopy in Live Primary Cilium
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A GDI/GDF-like system for sorting and shuttling ciliary proteins.

Shehab Ismail1

  • 1a CR-UK Beatson Institute , Glasgow , UK.

Small Gtpases
|August 4, 2016
PubMed
Summary

Prenylated proteins like Rab and Rho are solubilized by guanosine dissociation inhibitors (GDIs). Researchers propose that GDI displacement factors (GDFs) and Arl3GTP localization in cilia mediate cargo sorting.

Area of Science:

  • Lipid modifications in protein post-translational processes.
  • Small GTPases, prenylation, and membrane targeting.

Background:

  • Rab and Rho proteins are prenylated and require guanosine dissociation inhibitors (GDIs) for membrane targeting.
  • GDI displacement factors (GDFs) are hypothesized to release Rab/Rho proteins at their destinations.
  • Alternative mechanisms suggest GTP loading suffices for Rab protein targeting.

Purpose of the Study:

  • To investigate the role of GDI displacement factors (GDFs) in cargo sorting.
  • To explore the function of Arl2 and Arl3 in the localization of prenylated proteins.
  • To understand the mechanism of prenylated protein targeting to cilia.

Main Methods:

  • Investigating the interaction between prenylated proteins, GDIs, and GDFs.
  • Analyzing the localization of Arl2 and Arl3, particularly Arl3GTP.
Keywords:
Arl2; Arl3; Cilia; GDF; GDI; GSF; PDE6D; protein sorting; Rab; Rho

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  • Studying protein targeting to cilia.

    • Main Results:

    • Differential release of cargo by Arl2 and Arl3 is proposed as a key sorting mechanism.
    • Localization of active Arl3GTP within cilia is crucial for this process.
    • PDE6D, structurally similar to Rho GDI, solubilizes and targets prenylated proteins, including to cilia.

    Conclusions:

    • Cargo sorting relies on the differential release mediated by Arl2 and Arl3.
    • The localization of Arl3GTP in cilia is essential for targeting prenylated proteins.
    • This mechanism provides insight into the precise delivery of lipid-modified proteins.