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.
Alexandrova
N
N
Laboratory of Biological Chemistry, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.
Niklinski
J
J
Bliskovsky
V
V
Otterson
G A
GA
Blake
M
M
Kaye
F J
FJ
Zajac-Kaye
M
M
D001483:Base Sequence; D001665:Binding Sites; D002451:Cell Compartmentation; D004252:DNA Mutational Analysis; D005455:Fluorescent Antibody Technique; D006801:Humans; D008870:Microtubules / Q000378:metabolism*; D008969:Molecular Sequence Data; D011485:Protein Binding; D016271:Proto-Oncogene Proteins c-myc / Q000378:metabolism*; D017384:Sequence Deletion; D014404:Tubulin / Q000378:metabolism*; D014407:Tumor Cells, Cultured
D016271:Proto-Oncogene Proteins c-myc; D014404:Tubulin