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Mol. Cell. Biol., Sep 1995, 5188-5195, Vol 15, No. 9
Copyright © 1995, American Society for Microbiology

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

N Alexandrova, J Niklinski, V Bliskovsky, GA Otterson, M Blake, FJ Kaye and M Zajac-Kaye
Laboratory of Biological Chemistry, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.

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.


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