Why a heterotrimer? Elucidating the evolutionary persistence of kinesin-2 through the characterization of its mechanochemical cycle.

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Authors
Albracht, Clay D.
Issue Date
2015-05
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Electronic thesis
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ENG
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Biology
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Abstract
The kinesin family of motor proteins relies heavily on the homodimeric architecture for the assembly of motor proteins; however, heterotrimeric KIF3AB has been shown to be as processive as kinesin-1 while having different mechanochemical properties. This leads to the question: "Why is KIF3AB a heterotrimer?" The non-redundant cellular functions could hint at the advantages required from the motor proteins. Different subsets of microtubules are present in cilia, and the functional differences between the motor head allows for two different motor heads that could associate differently with these microtubules. Our data supports these differences in association by indicating that KIF3AB has a bias for the KIF3A motor domain. Phosphate release kinetics confirms that the initial association and release of phosphate occurs from the KIF3A motor domain. Finally, the specificity for binding the scaffold protein, kinesin associated protein (KAP) could be the reason for the heterotrimer. The associated tails of the KIF3A and KIF3B polypeptide could be required for binding to KAP subsequently providing the scaffold for intraflagellar transport.
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May 2015
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Rensselaer Polytechnic Institute, Troy, NY
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