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Related Concept Videos

Microtubule Associated Motor Proteins01:32

Microtubule Associated Motor Proteins

Eukaryotic cells have different motor proteins for transporting various cargo within the cell. These motor proteins differ based on the filament they associate with, the direction they move within the cell, and the type of cargo they transport. Motor proteins that associate with microtubules are known as microtubule-associated motor proteins. There are two families of microtubule-associated motor proteins —Kinesins and Dyneins. Both these proteins assist in the transport of cellular cargos...
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
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...
The Movement of Organelles and Vesicles01:43

The Movement of Organelles and Vesicles

In eukaryotic cells,  cytoskeletal filaments such as actin, microtubules, and intermediate filaments form a mesh-like cytoskeletal network. These filaments serve as tracks for transporting cellular cargo. Specialized motor proteins use the chemical energy stored in adenosine triphosphate (ATP) for this transport. During interphase, microtubules are polarized, with the plus-end towards the cell periphery and the minus-end towards the cell center. Two microtubule-associated motor proteins,...
Microtubule Associated Proteins (MAPs)01:42

Microtubule Associated Proteins (MAPs)

Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...
Microtubules in Cell Motility01:24

Microtubules in Cell Motility

Microtubules are thick hollow cylindrical proteins that help form the cytoskeleton. Microtubules have varied roles in the cell. These filaments help form cellular appendages like cilia and flagella, which are responsible for locomotion. The cilia arise from basal bodies, separated from the main body by a membrane-like structure forming the transition zone. This zone is the gate for the entry of lipids and proteins, creating a unique composition of lipids and proteins in the ciliary membrane and...

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Related Experiment Video

Updated: May 19, 2026

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro
08:53

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro

Published on: January 11, 2017

Dynactin's pointed-end complex is a cargo-targeting module.

Ting-Yu Yeh1, Nicholas J Quintyne, Brett R Scipioni

  • 1Department of Biology, Johns Hopkins University, Baltimore, MD 21218, USA.

Molecular Biology of the Cell
|August 25, 2012
PubMed
Summary
This summary is machine-generated.

Dynactin

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Cargo Loading onto Kinesin Powered Molecular Shuttles
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Cargo Loading onto Kinesin Powered Molecular Shuttles

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Characterizing the Composition of Molecular Motors on Moving Axonal Cargo Using "Cargo Mapping" Analysis
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Characterizing the Composition of Molecular Motors on Moving Axonal Cargo Using "Cargo Mapping" Analysis

Published on: October 30, 2014

Related Experiment Videos

Last Updated: May 19, 2026

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro
08:53

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro

Published on: January 11, 2017

Cargo Loading onto Kinesin Powered Molecular Shuttles
09:00

Cargo Loading onto Kinesin Powered Molecular Shuttles

Published on: November 3, 2010

Characterizing the Composition of Molecular Motors on Moving Axonal Cargo Using "Cargo Mapping" Analysis
11:09

Characterizing the Composition of Molecular Motors on Moving Axonal Cargo Using "Cargo Mapping" Analysis

Published on: October 30, 2014

Area of Science:

  • Cell Biology
  • Molecular Motors
  • Cytoskeletal Dynamics

Background:

  • Dynactin is crucial for cytoplasmic dynein motor function, enhancing processivity and acting as a cargo adaptor.
  • The precise mechanisms by which dynactin interacts with various subcellular binding partners are not fully understood.
  • The "pointed-end complex" is hypothesized to play a role in dynactin's cargo specification.

Purpose of the Study:

  • To characterize interactions within the dynactin pointed-end complex.
  • To investigate the role of the pointed-end complex in dynactin's interactions with endomembranes.
  • To elucidate how specific dynactin subunits contribute to dynactin stability and subcellular localization.

Main Methods:

  • Chemical cross-linking
  • RNA interference (RNAi) for gene silencing
  • Protein overexpression studies

Main Results:

  • Arp11 and p62 subunits are essential for dynactin stability and nuclear envelope binding.
  • p27 and p25 are peripheral subunits; their removal reduces membrane binding but not dynactin integrity.
  • Depletion of p27/p25 impairs endosome trafficking but not mitotic spindle formation.

Conclusions:

  • The dynactin pointed-end complex is a bipartite domain critical for dynactin stability.
  • Specific subunits within the pointed-end complex mediate interactions with diverse subcellular structures, including endomembranes.
  • Dynactin's interaction with cargoes is regulated by distinct subunit compositions.