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Development ePress online publication date 24 Sep 2003
doi: 10.1242/dev.00737

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Research article

GBP binds kinesin light chain and translocates during cortical rotation in Xenopus eggs


Carole Weaver, Gist H. Farr III, Weijun Pan, Brian A. Rowning, Jiyong Wang, Junhao Mao, Dianqing Wu, Lin Li, Carolyn A. Larabell, and David Kimelman*
* Author for correspondence (e-mail: kimelman{at}u.washington.edu)

In Xenopus, axis development is initiated by dorsally elevated levels of cytoplasmic {beta}-catenin, an intracellular factor regulated by GSK3 kinase activity. Upon fertilization, factors that increase {beta}-catenin stability are translocated to the prospective dorsal side of the embryo in a microtubule-dependent process. However, neither the identity of these factors nor the mechanism of their movement is understood. Here, we show that the GSK3 inhibitory protein GBP/Frat binds kinesin light chain (KLC), a component of the microtubule motor kinesin. Upon egg activation, GBP-GFP and KLC-GFP form particles and exhibit directed translocation. KLC, through a previously uncharacterized conserved domain, binds a region of GBP that is required for GBP translocation and for GSK3 binding, and competes with GSK3 for GBP. We propose a model in which conventional kinesin transports a GBP-containing complex to the future dorsal side, where GBP dissociates and contributes to the local stabilization of {beta}-catenin by binding and inhibiting GSK3.
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