Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Fusion of Secretory Vesicles with the Plasma Membrane

Fusion of Secretory Vesicles with the Plasma Membrane

Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...

Microtubule Associated Motor Proteins

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...

The Movement of Organelles and Vesicles

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,...

Phosphoinositides and PIPs

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...

Pinching-off of Coated Vesicles

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 Vesicles

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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Chromatophores as tools for the study of organelle transport.

Methods in molecular biology (Clifton, N.J.)·2001

Same author

Dynein, dynactin, and kinesin II's interaction with microtubules is regulated during bidirectional organelle transport.

The Journal of cell biology·2000

Same author

Ordering microtubules.

BioEssays : news and reviews in molecular, cellular and developmental biology·1997

Same author

Microtubules and microtubule motors: mechanisms of regulation.

International review of cytology·1996

Same author

Regulation of kinesin-directed movements.

Trends in cell biology·1995

Same author

Cytoplasmic dynein is a vesicle protein.

The Journal of biological chemistry·1992

Search research articles

Related Experiment Video

Updated: Jul 22, 2026

Lipid Vesicle-mediated Affinity Chromatography using Magnetic Activated Cell Sorting (LIMACS): a Novel Method to Analyze Protein-lipid Interaction

Lipid Vesicle-mediated Affinity Chromatography using Magnetic Activated Cell Sorting (LIMACS): a Novel Method to Analyze Protein-lipid Interaction

Published on: April 26, 2011

Cytoplasmic dynein binds to phospholipid vesicles

M L Lacey¹, L T Haimo

¹Department of Biology, University of California, Riverside 92521-0121.

Cell Motility and the Cytoskeleton

|January 1, 1994

Summary

Cytoplasmic dynein, a motor protein, binds directly to cell membranes through electrostatic interactions with acidic phospholipids, not requiring receptor proteins for organelle transport.

Area of Science:

Cell Biology
Molecular Motors
Membrane Biophysics

Background:

Cytoplasmic dynein is essential for retrograde organelle transport along microtubules.
Dynein must interact with organelle membranes, but the mechanism is unclear.
Potential mechanisms include receptor proteins or direct phospholipid interaction.

Purpose of the Study:

To investigate the mechanism of cytoplasmic dynein binding to synaptic membranes.
To determine if receptor proteins are necessary for dynein-membrane attachment.
To elucidate the role of phospholipids in dynein-membrane interactions.

Main Methods:

Studied dynein binding to native and treated synaptic membranes.
Examined purified dynein binding to phospholipid liposomes.

More Related Videos

Reconstitution of Basic Mitotic Spindles in Spherical Emulsion Droplets

Reconstitution of Basic Mitotic Spindles in Spherical Emulsion Droplets

Published on: August 13, 2016

Visualizing Cytoskeleton-Dependent Trafficking of Lipid-Containing Organelles in Drosophila Embryos

Visualizing Cytoskeleton-Dependent Trafficking of Lipid-Containing Organelles in Drosophila Embryos

Published on: December 13, 2021

Related Experiment Videos

Last Updated: Jul 22, 2026

Lipid Vesicle-mediated Affinity Chromatography using Magnetic Activated Cell Sorting (LIMACS): a Novel Method to Analyze Protein-lipid Interaction

Lipid Vesicle-mediated Affinity Chromatography using Magnetic Activated Cell Sorting (LIMACS): a Novel Method to Analyze Protein-lipid Interaction

Published on: April 26, 2011

Reconstitution of Basic Mitotic Spindles in Spherical Emulsion Droplets

Reconstitution of Basic Mitotic Spindles in Spherical Emulsion Droplets

Published on: August 13, 2016

Visualizing Cytoskeleton-Dependent Trafficking of Lipid-Containing Organelles in Drosophila Embryos

Visualizing Cytoskeleton-Dependent Trafficking of Lipid-Containing Organelles in Drosophila Embryos

Published on: December 13, 2021

Assessed the effect of trypsin and NaCl on dynein-membrane interactions.

Main Results:

Cytoplasmic dynein-synaptic membrane binding does not require receptor proteins.
Binding is mediated by electrostatic interactions with acidic phospholipids.
Dynein binding to liposomes mimics binding to native membranes and depends on acidic phospholipids.

Conclusions:

Cytoplasmic dynein can directly bind to organelle membranes via acidic phospholipids.
Electrostatic interactions are a key mechanism for dynein-membrane attachment.
This interaction is crucial for retrograde organelle transport.