How to probe motor-domains of kinesins?

In the past, molecular motor proteins like kinesins have been investigated with macromolecular approaches. Recent research on kinesins has been focused on resolving how kinesin is regulated by intramolecular dynamics.

Kinesin - cargo

Schematic diagram of kinesin indicating the position of Loop 5, neck, and cover neck relative to the motor domain, coiled-coil, and cargo. Note they are in close proximity to each other and hence interact during the mechanochemical transduction of energy to movement and direction.

Kinesins are motor proteins which move along microtubules in cells. This movement is driven by ATP hydrolysis, meaning kinesins exhibit ATPase activity. Thus kinesins are crucial for basic cellular function such as meiosis, mitosis, and transport of cargo in cells. Usually kinesins move from the cell centre to the periphery of the cell (anterograde transport). Dynein on the other hand moves along microtubules in the opposite direction allowing retrograde transport towards the cell centre.

Two main technical approaches are currently used to measure kinesin based dynamic mechanisms:

1. Total internal reflection fluorescence (TIRF) microscopy to observe single kinesin motors and

2. Sub-domain swapping from one motor to another.

What’s new for your motor protein research?

Cytoskeleton Inc. has compiled recent findings in this emerging research field in their September 2014 newsletter, exploring how motor protein research can be driven forward thanks to a wide variety of motor protein related products.

#1 Kinesin motor domains

#2 Kinesin motor activity assays

#3 Microtubules and tubulin

#4 Dynein

  • Dynein (cytoplasmic) – (on enquiry)

Download your copy of the e-newsletter “Probing Sub-domains of Kinesin, or leave any questions or comments below!

Written by Ali El Baya, PhD
Ali el Bayâ is the Sales Manager at tebu-bio for the North of Europe.