Deocaris Custer C, Yamasaki Kazuhiko, Kaul Sunil C, Wadhwa Renu
National Institute of Advanced Industrial Science & Technology (AIST), Tsukuba, Japan.
Ann N Y Acad Sci. 2006 May;1067:220-3. doi: 10.1196/annals.1354.027.
Chaperone functions mediated by the heat-shock protein (HSP) family constitute a fundamental mechanism that governs the life span of organisms. Here we investigated the chaperone activities of the mitochondrial HSP70 protein, mortalin, which is a heat-uninducible stress protein involved in immortalization and tumorigenesis. There are two mortalin alleles, mot-1 and mot-2, in mouse, encoding two distinct proteins. Whereas an overexpression of mot-1-induced senescence in NIH 3T3 cells, overexpression of mot-2 promoted their malignant properties. Here, we provide evidence that mot-1 possesses very low chaperone activity as compared to mot-2. A "lazy lid" hypothesis is proposed for their differential aging phenotypes.
热休克蛋白（HSP）家族介导的伴侣功能构成了一种控制生物体寿命的基本机制。在此，我们研究了线粒体HSP70蛋白mortalin的伴侣活性，它是一种与永生化和肿瘤发生有关的热非诱导应激蛋白。小鼠中有两个mortalin等位基因，mot-1和mot-2，编码两种不同的蛋白质。在NIH 3T3细胞中，mot-1的过表达诱导衰老，而mot-2的过表达则促进其恶性特性。在此，我们提供证据表明，与mot-2相比，mot-1的伴侣活性非常低。针对它们不同的衰老表型，我们提出了“懒惰盖子”假说。
