Patel Trupti Nv, Vasan Richa, Gupta Divanshu, Patel Jay, Trivedi Manjari
Department of Medical Biotechnology, Vellore Institute of Technology, Vellore, Tamilnadu, India E-mail :
Asian Pac J Cancer Prev. 2015;16(8):3085-90. doi: 10.7314/apjcp.2015.16.8.3085.
The telomeric end structures of the DNA are known to contain tandem repeats of TTAGGG sequence bound with specialised protein complex called the "shelterin complex". It comprises six proteins, namely TRF1, TRF2, TIN2, POT1, TPP1 and RAP1. All of these assemble together to form a complex with double strand and single strand DNA repeats at the telomere. Such an association contributes to telomere stability and its protection from undesirable DNA damage control-specific responses. However, any alteration in the structure and function of any of these proteins may lead to undesirable DNA damage responses and thus cellular senescence and death. In our review, we throw light on how mutations in the proteins belonging to the shelterin complex may lead to various malfunctions and ultimately have a role in tumorigenesis and cancer progression.
已知DNA的端粒末端结构包含与名为“端粒保护蛋白复合体”的特殊蛋白质复合体结合的TTAGGG序列串联重复。它由六种蛋白质组成,即TRF1、TRF2、TIN2、POT1、TPP1和RAP1。所有这些蛋白质共同组装形成一个复合体,该复合体在端粒处具有双链和单链DNA重复序列。这种结合有助于端粒稳定性及其免受不良DNA损伤控制特异性反应的影响。然而,这些蛋白质中任何一种的结构和功能发生改变都可能导致不良的DNA损伤反应,进而导致细胞衰老和死亡。在我们的综述中,我们阐明了属于端粒保护蛋白复合体的蛋白质中的突变如何可能导致各种功能障碍,并最终在肿瘤发生和癌症进展中发挥作用。