Saitohin 嵌套在 tau 基因内，与 tau 和 Abl 相互作用，其人类特异性等位基因影响 Abl 磷酸化。
Saitohin, which is nested within the tau gene, interacts with tau and Abl and its human-specific allele influences Abl phosphorylation.
机构信息
Department of Cell Biology, University of Massachusetts Medical School, Worcester, Massachusetts 01655, USA.
出版信息
J Cell Biochem. 2011 Nov;112(11):3482-8. doi: 10.1002/jcb.23279.
Abstract
Saitohin (STH) is a gene unique to humans and their closest relatives whose function is not yet known. STH contains a single polymorphism (Q7R); the Q allele is human-specific and confers susceptibility to several neurodegenerative diseases. In previous work, we discovered that STH interacts with Peroxiredoxin 6 (Prdx6), a unique member of that family which is bifunctional and whose levels increase in Pick's disease. In this study, we report that STH also interacts with tau and the non-receptor tyrosine kinase c-Abl (Abl). Furthermore, Abl phosphorylates STH on its single tyrosine residue and STH increases tyrosine phosphorylation by Abl. The effect of Saitohin on Abl-mediated phosphorylation appears to be allele-specific, providing evidence for a new cellular function for STH.
摘要
Saitohin（STH）是一种仅存在于人类及其近亲中的基因，其功能尚不清楚。STH 包含一个单一的多态性（Q7R）；Q 等位基因是人类特有的，易患多种神经退行性疾病。在之前的工作中，我们发现 STH 与过氧化物还原酶 6（Prdx6）相互作用，Prdx6 是该家族中唯一的具有双功能的成员，其水平在匹克氏病中增加。在这项研究中，我们报告 STH 还与 tau 和非受体酪氨酸激酶 c-Abl（Abl）相互作用。此外，Abl 在 STH 的单个酪氨酸残基上磷酸化 STH，而 STH 增加 Abl 的酪氨酸磷酸化。Saitohin 对 Abl 介导的磷酸化的影响似乎是等位基因特异性的，为 STH 的新细胞功能提供了证据。
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