Less is more: how protein degradation regulates muscle development.

Less is more: how protein degradation regulates muscle development.
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少即是多:蛋白质降解如何调节肌肉发育

DOI:
10.1007/2789_2008_101
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发表时间:
2009
期刊:
Ernst Schering Foundation symposium proceedings
影响因子:
--
通讯作者:
Hoppe T.
Hoppe T.
中科院分区:
--
文献类型:
--
作者:
Hoppe T.

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在肌肉发育过程中肌节结构的组织涉及受调节的多步组装途径。肌球蛋白组装因子α-45在整个肌肉粗丝形成过程中既作为分子伴侣又作为肌球蛋白的Hsp 90共伴侣发挥作用。因此,突变inunc-45导致瘫痪的蠕虫,在横纹体壁肌肉中严重的肌原纤维紊乱。我们的数据表明,功能性肌肉的形成inCaelobditis elegansis链接到泛素依赖的β-45营业额,调节E3酶UFD-2和CHN-1与泛素选择性伴侣CDC-48(也称为p97在人类)的合作。已知编码p97的基因中的错义突变会引起显性的迟发性遗传性包涵体肌病。值得注意的是,我们确定了CDC-48/p97在肌纤维分化和维持过程中的保守作用,这似乎对理解病理条件下肌肉形成和维持的缺陷具有重要意义。
The organization of sarcomeric structures during muscle development involves regulated multistep assembly pathways. The myosin assembly factor UNC-45 functions both as a molecular chaperone and as an Hsp90 co-chaperone for myosin throughout muscle thick-filament formation. Consequently, mutations inunc-45result in paralyzed worms with severe myofibril disorganization in striated body wall muscles. Our data suggest that functional muscle formation inCaenorhabditis elegansis linked to ubiquitin-dependent UNC-45 turnover, regulated by the E3 enzymes UFD-2 and CHN-1 in cooperation with the ubiquitin-selective chaperone CDC-48 (also known as p97 in human). Missense mutations in the gene encoding p97 are known to cause a dominant, late-onset hereditary inclusion body myopathy. Remarkably, we identified a conserved role of CDC-48/p97 in the process of myofiber differentiation and maintenance, which appears to have important implications for understanding defects in muscle formation and maintenance during pathological conditions.
酵母多聚泛素化因子 Ufd2p 的人类同源物在细胞凋亡过程中被 caspase 6 和颗粒酶 B 切割。
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影响因子: --
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