THE N-TERMINAL DOMAIN OF C-MYC ASSOCIATES WITH ALPHA-TUBULIN AND MICROTUBULES IN-VIVO AND IN-VITRO

Citation
N. Alexandrova et al., THE N-TERMINAL DOMAIN OF C-MYC ASSOCIATES WITH ALPHA-TUBULIN AND MICROTUBULES IN-VIVO AND IN-VITRO, Molecular and cellular biology, 15(9), 1995, pp. 5188-5195
Citations number
36
Categorie Soggetti
Biology
ISSN journal
02707306
Volume
15
Issue
9
Year of publication
1995
Pages
5188 - 5195
Database
ISI
SICI code
0270-7306(1995)15:9<5188:TNDOCA>2.0.ZU;2-G
Abstract
The polymerization of alpha- and beta-tubulin into microtubules result s in a complex network of microfibrils that have important structural and functional roles in all eukaryotic cells, In addition, microtubule s fan interact with a diverse family of polypeptides which are believe d to directly promote the assembly of microtubules and to modulate the ir functional activity, We have demonstrated that the c-Myc oncoprotei n interacts in vivo and in vitro with alpha-tubulin and with polymeriz ed microtubules and have defined the binding site to the N-terminal re gion within the transactivation domain of c-Myc. In addition, we have shown that c-Myc colocalizes with microtubules and remains tightly bou nd to the microtubule network after detergent extraction of intact cel ls, These findings suggest a potential role for Myc-tubulin interactio n in vivo.