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Coat Assembly and GTPases01:33

Coat Assembly and GTPases

3.5K
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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Rab Proteins01:14

Rab Proteins

4.0K
Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
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Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

2.4K
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...
2.4K
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

8.3K
Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
8.3K
Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

8.1K
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...
8.1K
Rab Cascades01:25

Rab Cascades

2.8K
Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
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Related Experiment Video

Updated: May 1, 2026

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells
10:27

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells

Published on: March 9, 2012

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PTRF-Cavin, a conserved cytoplasmic protein required for caveola formation and function.

Michelle M Hill1, Michele Bastiani, Robert Luetterforst

  • 1Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Australia.

Cell
|January 15, 2008
PubMed
Summary

Protopoly(proline-rich transmembrane protein) (PTRF), also known as Cavin, is essential for forming cell surface caveolae. Its absence prevents caveolae development and leads to caveolin degradation.

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In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes
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In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes

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Purification of the Cystic Fibrosis Transmembrane Conductance Regulator Protein Expressed in Saccharomyces cerevisiae

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Related Experiment Videos

Last Updated: May 1, 2026

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells
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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Caveolae are vital plasma membrane invaginations involved in cellular processes like lipid regulation and endocytosis.
  • The molecular machinery governing caveolae formation and stability remained incompletely understood.

Purpose of the Study:

  • To identify proteins crucial for caveolae biogenesis and function.
  • To elucidate the role of Protopoly(proline-rich transmembrane protein) (PTRF), also known as Cavin, in caveolae formation.

Main Methods:

  • Comparative proteomics was employed to identify potential caveolar coat proteins.
  • PTRF-Cavin expression and localization were studied in prostate cancer PC3 cells and zebrafish notochord development.
  • Functional assays involved PTRF-Cavin knockdown and expression studies to assess caveolae formation and caveolin dynamics.

Main Results:

  • PTRF-Cavin was identified as a key protein selectively associating with mature caveolae at the plasma membrane.
  • Lack of PTRF-Cavin expression correlated with the absence of caveolae and flat plasma membranes in both cell and organism models.
  • PTRF-Cavin expression induced caveolae formation, while its knockdown reduced caveolae density and increased caveolin mobility and degradation.

Conclusions:

  • PTRF-Cavin is indispensable for the formation of caveolae.
  • PTRF-Cavin plays a critical role in stabilizing caveolin within immobile caveolae structures.
  • This study establishes PTRF-Cavin as a required component for caveolae biogenesis and maintenance.