Interactions of enolase isoforms with tubulin and microtubules during myogenesis
Interactions of enolase isoforms with tubulin and microtubules during myogenesis
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DOI：
10.1016/j.bbagen.2007.01.015
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发表时间：
2007-06-01
影响因子：
3
通讯作者：
Ovadi, J.
中科院分区：
文献类型：
--
作者：
Keller, A.;Peltzer, J.;Ovadi, J.
烯醇化酶是一种糖酵解酶，在高等脊椎动物中表达为细胞类型特异性同工型。在此，我们首次证明了在肌肉卫星细胞分化过程中烯醇化酶亚型与微管相互作用。而在未分化的成肌细胞中，普遍存在的act烯醇化酶亚型，高水平表达，表现出广泛的共定位与微管，肌肉特异性亚型，低水平表达，没有。在分化过程中，亚基水平显着增加;在胞浆和沿着微管中均检测到α和烯醇化酶免疫反应。我们从肌肉提取物中鉴定出微管蛋白作为固定化β-烯醇化酶的相互作用蛋白。ELISA和表面等离子体共振测量表明，直接结合的烯醇化酶亚型微管蛋白的表观K-D低于微摩尔范围，并表明，存在0.8 mM的2-磷酸甘油废除的相互作用。我们的数据表明，在成肌分化的不同阶段，微管被不同的烯醇化酶亚型修饰，这是由双方的丰度控制的。我们认为，结合的烯醇化酶微管可能有助于调节的动态的细胞骨架丝发生在从成肌细胞到肌管的过渡。(c)2007 Elsevier B. V.保留所有权利。
Enolase is a glycolytic enzyme, expressed as cell-type specific isoforms in higher vertebrates. Herein we demonstrated for the first time that enolase isoforms interact with microtubules during muscle satellite cell differentiation. While in undifferentiated myoblasts the ubiquitous act enolase isoform, expressed at high level, exhibited extensive co-localization with microtubules, the muscle-specific isoform, expressed at low level, did not. During differentiation, the level of subunit increased significantly; the a and enolase immunoreactivities were detected both in cytosol and along the microtubules. We identified tubulin from muscle extract as an interacting protein for immobilized beta beta enolase. ELISA and surface plasmon resonance measurements demonstrated the direct binding of enolase isoforms to tubulin with an apparent K-D below the micromolar range, and indicated that the presence of 0.8 mM 2-phosphoglycerate abolished the interaction. Our data showed that, at various stages of myogenic differentiation, microtubules were decorated by different enolase isoforms, which was controled by the abundance of both partners. We suggest that the binding of enolase to microtubules could contribute to the regulation of the dynamism of the cytoskeletal filaments known to occur during the transition from myoblast to myotubes. (c) 2007 Elsevier B.V. All rights reserved.