中文摘要：

Telomeres，线性真核细胞的染色体的结束，是双人脚踏车 DNA 重复并且由各种各样的 telomeric 蛋白质盖住。这些核蛋白建筑群保护 telomeres 免受 DNA 的伤害损坏反应(DDR ) ，再结合，和端对端的熔化，保证染色体稳定性。人的 telosome/shelterin 建筑群是学习最好的联系 telomere 的蛋白质建筑群之一，由六核心 telomeric 蛋白质 TRF1， TRF2， TIN2， RAP1， POT1，和 TPP1 组成。TPP1，也已知的同样肾上腺皮质的发育异常蛋白质相当或相同的事物(ACD ) ，是 TEBP- 的一个通常认为的哺乳动物的相当或相同的事物并且属于 oligonucleotide 绑定(OB )-fold-containing 蛋白质家庭。三功能的域在 TPP1， N 终端 OB 褶层， POT1 有约束力的招募域(RD ) ，和 carboxyl 终端交往 TIN2 域(TID ) 以内被识别了。TPP1 能与 POT1 和 TIN2 交往维持 telomere 结构，并且调停为 telomere 延伸的 telomerase 招募。这些特征显示了 TPP1 玩在 telomere 的一个必要角色维护。这里，我们将考察重要调查结果加亮 TPP1 的功能的意义，与它和另外的 telosome 部件和 telomerase 的相互作用的一个焦点。我们将也在疾病治疗讨论潜在的含意。

英文摘要：

Telomeres, the ends of linear eukaryotic chromosomes, are tandem DNA repeats and capped by various telomeric proteins. These nucleoprotein complexes protect telomeres from DNA damage response （DDR）, recombination, and end-to-end fusions, ensuring genome stability. The human telosome/shelterin complex is one of the best-studied telomere-associated protein complexes, made up of six core telomeric proteins TRF1, TRF2, TIN2, RAPI, POT1, and TPPI. TPP1, also known as adrenocortical dysplasia protein homolog （ACD）, is a putative mammalian homolog of TEBP-β and belongs to the oligonucleotide binding （OB）-fold-containing protein family. Three functional domains have been identified within TPP1, the N-terminal OB fold, the POT1 binding recruitment domain （RD）, and the carboxyl-terminal TIN2-interacting domain （TID）. TPP1 can interact with both POT1 and TIN2 to maintain telomere structure, and mediate telomerase recruitment for telomere elongation. These features have indicated TPP1 play an essential role in telomere maintenance. Here, we will review important findings that highlight the functional significance of TPP1, with a focus on its interaction with other telosome components and the telomerase. We will also discuss potential implications in disease therapies.