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Interactions of enolase isoforms with tubulin and microtubules during myogenesis

机译:烯醇化酶同工型与微管蛋白和微管在成肌过程中的相互作用

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摘要

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 αα enolase isoform, expressed at high level, exhibited extensive co-localization with microtubules, the muscle-specific ββ isoform, expressed at low level, did not. During differentiation, the level of β subunit increased significantly; the α and β enolase immunoreactivities were detected both in cytosol and along the microtubules. We identified tubulin from muscle extract as an interacting protein for immobilized ββ enolase. ELISA and surface plasmon resonance measurements demonstrated the direct binding of enolase isoforms to tubulin with an apparent KD 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.
机译:烯醇化酶是一种糖酵解酶,在高等脊椎动物中表现为细胞类型的特异性同工型。在本文中,我们首次证明了烯醇化酶同工型在肌肉卫星细胞分化过程中与微管相互作用。在未分化的成肌细胞中,高表达的泛在αα烯醇酶同工型与微管表现出广泛的共定位,而低水平表达的肌肉特异性ββ同工型则没有。在分化过程中,β亚基的水平显着增加。在细胞质和微管中均检测到α和β烯醇酶的免疫反应性。我们从肌肉提取物中鉴定出微管蛋白是固定化ββ烯醇酶的相互作用蛋白。 ELISA和表面等离子体共振测量表明,烯醇化酶同工型与微管蛋白直接结合,其表观KD低于微摩尔范围,并且表明存在0.8 mM的2-磷酸甘油酸酯消除了相互作用。我们的数据显示,在成肌分化的各个阶段,微管由不同的烯醇酶同工型修饰,而烯醇酶同工型受双方伴侣的丰度控制。我们建议烯醇酶与微管的结合可能有助于调节已知在从成肌细胞向肌管转变期间发生的细胞骨架丝的动力。

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