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KMID : 0613820190290030369
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Journal of Life Science
2019 Volume.29 No. 3 p.369 ~ p.375
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The Carboxyl-terminal Tail of a Heterotrimeric Kinesin 2 Motor Subunit Directly Binds to β2-tubulin
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Jeong Young-Joo
Park Sung-Woo
Kim Sang-Jin
Lee Won-Hee
Kim Moo-Seong
Urm Sang-Hwa
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Abstract
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Microtubules form through the polymerization of α- and β-tubulin, and tubulin transport plays an important role in de?ning the rate of microtubule growth inside cellular appendages, such as the cilia and ?agella. Heterotrimeric kinesin 2 is a molecular motor member of the kinesin superfamily (KIF) that moves along the microtubules to transport multiple cargoes. It consists of two motor subunits (KIF3A and KIF3B) and a kinesin-associated protein 3 (KAP3), forming a heterotrimeric complex. Heterotrimeric kinesin 2 interacts with many different binding proteins through the cargo-binding domains of the KIF3s, but these binding proteins have not yet been specified. To identify these proteins for KIF3A, we performed yeast two-hybrid (Y2H) screening and found a specific interaction with β2- tubulin (Tubb2), a microtubule component. Tubb2 was found to bind to the cargo-binding domain of KIF3A but did not interact with KIF3B, KIF5B, or kinesin light chain 1 in the Y2H assay. The carboxyl-terminal region of Tubb2 is essential for interaction with KIF3A. Other Tubb isoforms, including Tubb1, Tubb3, Tubb4, and Tubb5, also interacted with KIF3A in the Y2H screening. However, α1-tubulin (Tuba1) did not interact with KIF3A. In addition, an antibody to KIF3A specifically co-immunoprecipitated the KIF3B and KAP3 associated with Tubb2 from mouse brain extracts. In combination, these results suggest that a heterotrimeric kinesin 2 motor protein is capable of binding to tubulin and may transport it in cells.
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KEYWORD
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Binding protein, kinesin, microtubule, transport, tubulin
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