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Related Experiment Video

Updated: Jul 22, 2026

Identification of Kinesin-1 Cargos Using Fluorescence Microscopy

Identification of Kinesin-1 Cargos Using Fluorescence Microscopy

Published on: February 14, 2016

Regulation of kinesin-directed movements.

¹Dept of Biology, University of California, Riverside, CA 92521, USA.

Trends in Cell Biology

|April 1, 1995

Summary

Cellular organelle movement relies on kinesin and dynein motors. Phosphorylation of kinesin may regulate its interaction with microtubules and organelles, controlling transport direction and timing.

Area of Science:

Cell Biology
Molecular Motors
Cytoskeletal Dynamics

Background:

Bidirectional organelle transport is crucial for cellular function.
This transport is mediated by microtubule-based motors, primarily kinesin and cytoplasmic dynein.
Cellular control over organelle movement implies regulation of these motor proteins' activity.

Purpose of the Study:

To investigate the potential role of protein phosphorylation in regulating kinesin motor activity.
To explore how phosphorylation might modulate kinesin's interaction with microtubules and organelles.

Main Methods:

Review of recent studies on kinesin, kinesin-like proteins, and associated proteins.
Analysis of phosphorylation patterns in relation to motor protein function.

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Motility of Single Molecules and Clusters of Bi-Directional Kinesin-5 Cin8 Purified from S. cerevisiae Cells

Motility of Single Molecules and Clusters of Bi-Directional Kinesin-5 Cin8 Purified from S. cerevisiae Cells

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Related Experiment Videos

Last Updated: Jul 22, 2026

Identification of Kinesin-1 Cargos Using Fluorescence Microscopy

Identification of Kinesin-1 Cargos Using Fluorescence Microscopy

Published on: February 14, 2016

Assembling Molecular Shuttles Powered by Reversibly Attached Kinesins

Assembling Molecular Shuttles Powered by Reversibly Attached Kinesins

Published on: January 26, 2019

Motility of Single Molecules and Clusters of Bi-Directional Kinesin-5 Cin8 Purified from S. cerevisiae Cells

Motility of Single Molecules and Clusters of Bi-Directional Kinesin-5 Cin8 Purified from S. cerevisiae Cells

Published on: February 2, 2022

Main Results:

Kinesin, kinesin-like proteins, and associated proteins are subject to phosphorylation.
Phosphorylation state changes are suggested to potentially alter kinesin's interaction capabilities.

Conclusions:

Phosphorylation is a likely regulatory mechanism for kinesin-driven organelle transport.
Modulation of kinesin activity via phosphorylation could control the direction and timing of organelle movements.