c-Myc的N端结构域在体内和体外均与α-微管蛋白及微管相关联。
The N-terminal domain of c-Myc associates with alpha-tubulin and microtubules in vivo and in vitro.
作者信息
Alexandrova N, Niklinski J, Bliskovsky V, Otterson G A, Blake M, Kaye F J, Zajac-Kaye M
机构信息
Laboratory of Biological Chemistry, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.
出版信息
Mol Cell Biol. 1995 Sep;15(9):5188-95. doi: 10.1128/MCB.15.9.5188.
Abstract
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.
摘要
α-微管蛋白和β-微管蛋白聚合成微管，形成了一个复杂的微纤维网络，该网络在所有真核细胞中都具有重要的结构和功能作用。此外，微管可与多种多肽相互作用，这些多肽被认为可直接促进微管的组装并调节其功能活性。我们已经证明，c-Myc癌蛋白在体内和体外均能与α-微管蛋白以及聚合的微管相互作用，并确定了其与c-Myc反式激活域内N端区域的结合位点。此外，我们还表明，c-Myc与微管共定位，并且在完整细胞经去污剂提取后仍与微管网络紧密结合。这些发现提示了Myc-微管蛋白相互作用在体内可能具有的作用。
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