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Related Concept Videos

Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

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...
Rab Cascades01:25

Rab Cascades

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.
COP Coated Vesicles00:59

COP Coated Vesicles

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 different...
Rab Proteins01:14

Rab Proteins

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...
Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

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...
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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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Related Experiment Video

Updated: May 20, 2026

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
08:55

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

Published on: December 29, 2017

Vesicle trafficking: ROP-RIC roundabout.

Angus S Murphy1, Wendy Ann Peer

  • 1Department of Horticulture and Landscape Architecture, Purdue University, West Lafayette, IN 47907, USA. murphy@purdue.edu

Current Biology : CB
|July 28, 2012
PubMed
Summary
This summary is machine-generated.

Small GTPases regulate protein recycling and cell growth by controlling protein activity. Recent studies show ROP-RIC signaling directs PIN protein removal in plant cells.

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The Microscopy-Based Assay to Study and Analyze the Recycling Endosomes using SNARE Trafficking
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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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Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
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Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells
11:05

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:

  • Plant cell biology
  • Molecular mechanisms of cell growth
  • Protein trafficking and signaling

Background:

  • Dynamic protein recycling is crucial for cellular functions, including cytoskeletal dynamics and cell shape.
  • Small GTPases are key regulators, modulating protein activity to influence these processes.
  • Understanding protein recycling is vital for comprehending cell polarity and responses to environmental cues.

Purpose of the Study:

  • To elucidate the role of ROP-RIC signaling in controlling the endocytosis of PIN proteins.
  • To investigate how protein recycling mechanisms impact plant cell growth and morphology.
  • To provide insights into the regulation of polar growth and asymmetric cell shape.

Main Methods:

  • Analysis of ROP-RIC signaling pathways in plant cells.
  • Investigating the regulation of PIN protein endocytosis.
  • Utilizing live-cell imaging in leaf pavement and root cells.

Main Results:

  • ROP-RIC activity was demonstrated to control PIN endocytosis in plant cells.
  • This regulation impacts cytoskeletal dynamics, affecting cell shape.
  • The findings highlight a mechanism for controlling polar growth.

Conclusions:

  • ROP-RIC signaling is a critical regulator of PIN protein trafficking.
  • This pathway influences cell polarity and asymmetric growth in plants.
  • The study advances our understanding of protein recycling in developmental processes.