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Novel heterotrimeric kinesin-related protein purified from sea urchin eggs

Nature volume 366, pages 268–270 (1993)Cite this article

Abstract

KINESIN heavy chain and kinesin-related polypeptides (KRPs) comprise a family of motor proteins with diverse intracellular transport functions1–7. Using pan-kinesin peptide antibodies that react with these proteins8,9, we haven previously purified from sea urchin eggs a trimeric microtubule-binding and bundling protein, KRP(85/95) (ref. 8) comprising subunits of Mr115,000 (115K), 95K and 85K. We report here that kinesin-related genes encode the 85K and 95K subunits, and that the protein can be immunoprecipitated from cytosol as a trimeric complex using an 85K monoclonal antibody. We also find that purified KRP(85/95) directs movements towards the 'plus' ends of microtubules. To our knowledge, this protein is the first kinesin-related motor to be purified from its natural host cell in a native multimeric state.

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Authors and Affiliations

  1. Section of Molecular and Cellular Biology, Division of Biological Sciences, University of California, Davis, California, 95616, USA

    D. G. Cole, S. W. Chinn, K. P. Wedaman, K. Hall, T. Vuong  & J. M. Scholey

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  1. D. G. Cole
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  2. S. W. Chinn
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  3. K. P. Wedaman
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  6. J. M. Scholey
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Cole, D., Chinn, S., Wedaman, K. et al. Novel heterotrimeric kinesin-related protein purified from sea urchin eggs. Nature 366, 268–270 (1993). https://doi.org/10.1038/366268a0

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