Authors:

Olivia Scheil

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About Paper:

Cells utilize intracellular trafficking to move necessary materials to their subcellular location. Kinesins are essential motor proteins that transport cargoes along the microtubule cytoskeleton. Kinesins carry out intracellular trafficking by binding the microtubule lattice and hydrolyzing ATP through their motor domains. This process imposes mechanical stress upon microtubules and uses cellular energy. To mitigate these impacts, kinesins can utilize a mechanism of self-regulation called autoinhibition, which prevents the motor domain from binding to microtubules. However, a less-understood regulation mechanism involves KIFBP (kinesin family binding protein), which has been shown to inhibit the binding of some kinesins to microtubules. Whether KIFBP inhibits all kinesins remains unknown. To investigate this, we developed a microscopy-based assay that determines which kinesins are impacted by KIFBP. Using the kinesin motors kinesin-3 KIF1A (positive control) and kinesin-1 KIF5C (negative control), we determined assay conditions effective in elucidating KIFBP activity. We then applied our assay to determine the effects of KIFBP on additional members of the kinesin-3 family. Our analysis indicates a statistically-significant reduction in microtubule binding of the kinesin-3 proteins KIF13B and KIF16B. These results suggest that KIFBP may be a general regulator of kinesin-3 motor proteins which play critical roles in intracellular trafficking in neuronal cells. We are continuing with this assay to investigate the potential relationship of KIFBP with other kinesins.

Source:

Chicago Area Undergraduate Research Symposium

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Co-authors:

Olivia Scheil