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Related Concept Videos

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.
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.
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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.
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Directing Proteins to the Rough Endoplasmic Reticulum01:34

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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...
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...
Receptor-mediated Endocytosis01:38

Receptor-mediated Endocytosis

Overview

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Related Experiment Video

Updated: Jun 2, 2026

Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells
11:05

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ARFGAP1 promotes AP-2-dependent endocytosis.

Ming Bai1, Helge Gad, Gabriele Turacchio

  • 1Division of Rheumatology, Immunology and Allergy, Brigham and Women's Hospital, and Department of Medicine, Harvard Medical School, Boston, Massachusetts 02115, USA.

Nature Cell Biology
|April 19, 2011
PubMed
Summary

ARFGAP1, a protein known in COPI transport, also interacts with the AP-2 complex. Disrupting these interactions selectively inhibits transport, revealing ARFGAP1

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Interactions

Background:

  • COPI (coat protein I) and clathrin-AP-2 (adaptor protein 2) are distinct coat proteins involved in intracellular transport.
  • A common component linking these two essential coat systems had not been previously identified.
  • ARFGAP1, a GTPase-activating protein (GAP) for ADP-ribosylation factor 1 (ARF1), is a known component of the COPI complex.

Purpose of the Study:

  • To investigate whether ARFGAP1, a known COPI component, also interacts with the AP-2 complex.
  • To determine the functional significance of ARFGAP1's interaction with both COPI and AP-2 coat proteins.
  • To elucidate the role of ARFGAP1 in AP-2-mediated endocytosis and COPI-mediated transport.

Main Methods:

  • Investigated interactions between ARFGAP1 and coatomer (COPI components) and AP-2 complex using biochemical assays.
  • Utilized selective disruption of ARFGAP1 interactions with AP-2 and coatomer.
  • Assessed the impact of disrupted interactions on specific intracellular transport pathways, including AP-2-regulated endocytosis.

Main Results:

  • Distinct regions of ARFGAP1 were shown to interact with both AP-2 and coatomer.
  • Selective disruption of ARFGAP1's interaction with either AP-2 or coatomer led to specific inhibition of their respective transport pathways.
  • ARFGAP1's GAP activity and coat function were found to be crucial for promoting AP-2 transport, mirroring its role in COPI transport.

Conclusions:

  • ARFGAP1 serves as a common link between the COPI and AP-2 coat systems.
  • ARFGAP1 plays a dual role, functioning in both COPI-mediated transport and AP-2-mediated endocytosis.
  • The dual functionality of ARFGAP1 highlights its importance in coordinating different intracellular trafficking pathways.