Molecular Signaling Laboratory, Department of Immunology, Central Clinical School, Monash University, Melbourne, Victoria 3004, Australia.
Front Biosci (Landmark Ed). 2011 Jan 1;16(1):187-207. doi: 10.2741/3683.
Telomeres are the termini of linear chromosomes. They are composed of DNA and DNA-binding proteins critical for maintaining chromosome integrity and cellular function. Telomere binding proteins regulate the structure and function of telomeres through the formation of different complexes with telomeric DNA. Double- and single-stranded telomeric DNA binding protein complexes have shared and unique functions that regulate telomere homeostasis. Recent studies have shown that telomerase interacts with several telomere-binding protein complexes including shelterin, CST, DNA-dependent protein kinase (DNA-PK) and MRN. The present review describes the recognised telomere-binding protein complexes, sub-complex exchanges and inter-complex molecular interactions. It also discusses the evidence suggesting that telomerase reverse transcriptase (TERT) switches between different complexes. Studies of the telomere protein inter-complex interactions and the switching of components between complexes provide insight into their fundamental roles of programming telomere length and configuration, and thus cell proliferative potential.
端粒是线性染色体的末端。它们由 DNA 和 DNA 结合蛋白组成，对于维持染色体的完整性和细胞功能至关重要。端粒结合蛋白通过与端粒 DNA 形成不同的复合物来调节端粒的结构和功能。双链和单链端粒 DNA 结合蛋白复合物具有共享和独特的功能，可调节端粒的动态平衡。最近的研究表明，端粒酶与几种端粒结合蛋白复合物相互作用，包括庇护素、CST、DNA 依赖性蛋白激酶（DNA-PK）和 MRN。本综述描述了公认的端粒结合蛋白复合物、亚复合物交换和复合物间的分子相互作用。它还讨论了表明端粒酶逆转录酶 (TERT) 在不同复合物之间切换的证据。研究端粒蛋白复合物间的相互作用以及复合物间成分的切换，为深入了解其调节端粒长度和构象以及细胞增殖潜能的基本功能提供了线索。
