Songyang Zhou, Liu Dan
Verna and Marrs Mclean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.
Crit Rev Eukaryot Gene Expr. 2006;16(2):103-18. doi: 10.1615/critreveukargeneexpr.v16.i2.10.
Work in model organisms, such as mouse, yeast, Tetrahymena, ciliates, and plants, has led to a deeper understanding of telomere biology. Telomeres together with telomere-binding proteins have evolved to protect chromosomal ends and maintain chromosomal length and integrity. Over the last two decades, biochemical, molecular, cellular, and genetic studies have greatly enhanced our knowledge of the unique function and structure of telomeres and telomere-associated factors. In this review, we focus on the important advances, in terms of our knowledge and the methods used, in understanding mammalian telomere regulation by telomeric proteins. Recently, the 6 telomeric proteins (TRF1, TRF2, POT1, TIN2, RAP1, and TPP1) were found to form a high-order complex. This complex and its associated partners provide the basis for constructing an interaction map of telomere regulators in mammalian cells, which we named the Telomere Interactome. The Telomere Interactome incorporates the various telomere signaling pathways and represents the molecular machinery that regulates mammalian telomeres. The establishment of the Telomere Interactome will also enable the integration of the intricate circuitries that regulate telomeres with other cellular interactomes in vertebrates.
在诸如小鼠、酵母、四膜虫、纤毛虫和植物等模式生物中的研究，加深了我们对端粒生物学的理解。端粒与端粒结合蛋白共同进化，以保护染色体末端并维持染色体长度和完整性。在过去二十年中，生物化学、分子、细胞和遗传学研究极大地增进了我们对端粒及端粒相关因子独特功能和结构的认识。在本综述中，我们聚焦于在理解端粒蛋白对哺乳动物端粒调控方面，就我们的知识和所使用的方法而言取得的重要进展。最近，发现6种端粒蛋白（TRF1、TRF2、POT1、TIN2、RAP1和TPP1）形成一个高阶复合物。这个复合物及其相关伙伴为构建哺乳动物细胞中端粒调节因子的相互作用图谱提供了基础，我们将其命名为端粒相互作用组。端粒相互作用组整合了各种端粒信号通路，代表了调节哺乳动物端粒的分子机制。端粒相互作用组的建立还将使调节端粒的复杂回路与脊椎动物中的其他细胞相互作用组得以整合。
