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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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The N-terminal domain of c-Myc associates with alpha-tubulin and microtubules in vivo and in vitro.

The polymerization of alpha- and beta-tubulin into microtubules results in a complex network of microfibrils that have important structural and functional roles in all eukaryotic cells. In addition, microtubules can interact with a diverse family of polypeptides which are believed to directly promote the assembly of microtubules and to modulate their functional activity. We have demonstrated that the c-Myc oncoprotein interacts in vivo and in vitro with alpha-tubulin and with polymerized microtubules and have defined the binding site to the N-terminal region within the transactivation domain of c-Myc. In addition, we have shown that c-Myc colocalizes with microtubules and remains tightly bound to the microtubule network after detergent extraction of intact cells. These findings suggest a potential role for Myc-tubulin interaction in vivo.[1]

References

  1. The N-terminal domain of c-Myc associates with alpha-tubulin and microtubules in vivo and in vitro. Alexandrova, N., Niklinski, J., Bliskovsky, V., Otterson, G.A., Blake, M., Kaye, F.J., Zajac-Kaye, M. Mol. Cell. Biol. (1995) [Pubmed]
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