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首页> 外文期刊>Cellular Signalling >Regulation of C1-Ten protein tyrosine phosphatase by p62/SQSTM1-mediated sequestration and degradation
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Regulation of C1-Ten protein tyrosine phosphatase by p62/SQSTM1-mediated sequestration and degradation

机译：p62 / SQSTM1介导的螯合和降解对C1-Ten蛋白酪氨酸磷酸酶的调节

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摘要

C1-Ten is a member of the tensin family of focal adhesion molecules but recent studies suggest it plays a more active role in many biological processes because of its potential association with diabetes and cancers. However, relatively little is known about the regulation of C1-Ten, such as changes in its protein level or cellular localization. The cellular localization of C1-Ten is unique because it is expressed in cytoplasmic puncta but nothing is known about these puncta. Here, we show that p62 sequestrates C1-Ten into puncta, making C1-Ten diffuse into the cytoplasm upon p62 depletion. More importantly, p62-mediated C1-Ten sequestration promoted C1-Ten ubiquitination and proteasomal degradation. p62-mediated protein reduction was specific to C1-Ten, and not other tensins such as tensin1 and tensin3. Thus, our results link cellular localization of C1-Ten to an off-switch site for C1-Ten. Additionally, p62 expression increased but C1-Ten protein decreased during muscle differentiation, supporting a role for p62 as a physiological regulator of C1-Ten.
机译：C1-Ten是粘着斑张力蛋白家族的成员，但最近的研究表明，由于其与糖尿病和癌症的潜在联系，它在许多生物过程中起着更加积极的作用。但是，对C1-Ten的调控（例如其蛋白质水平的变化或细胞定位）的了解相对较少。 C1-Ten在细胞中的定位是独特的，因为它在细胞质点中表达，但对这些点却一无所知。在这里，我们显示p62会将C1-Ten螯合成点状，使p1-耗尽时C1-Ten扩散到细胞质中。更重要的是，p62介导的C1-Ten螯合促进了C1-Ten泛素化和蛋白酶体降解。 p62介导的蛋白质还原是C1-Ten特有的，而不是其他张力蛋白，例如tensin1和tensin3。因此，我们的结果将C1-Ten的细胞定位链接到C1-Ten的非开关位点。此外，在肌肉分化过程中，p62表达增加，但C1-Ten蛋白减少，支持了p62作为C1-Ten的生理调节剂的作用。

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