Abstract
Telomerase reverse transcriptase (TERT) is a catalytic subunit of telomerase. Telomerase complex plays a key role in cancer formation by telomere dependent or independent mechanisms. Telomere maintenance mechanisms include complex TERT changes such as gene amplifications, TERT structural variants, TERT promoter germline and somatic mutations, TERT epigenetic changes, and alternative lengthening of telomere. All of them are cancer specific at tissue histotype and at single cell level. TERT expression is regulated in tumors via multiple genetic and epigenetic alterations which affect telomerase activity. Telomerase activity via TERT expression has an impact on telomere length and can be a useful marker in diagnosis and prognosis of various cancers and a new therapy approach. In this review we want to highlight the main roles of TERT in different mechanisms of cancer development and regulation.
Highlights
In most human cancers, telomerase is reactivated during carcinogenesis by expression of the catalytic subunit telomerase reverse transcriptase (TERT)
MD and KB-K contributed to the conception and design of the review, drafted, and finalized the manuscript
BW contributed to the conception and design of the review and its draft version
Summary
Telomerase is reactivated during carcinogenesis by expression of the catalytic subunit telomerase reverse transcriptase (TERT). TERT plays a key role in cancer formation, ensuring chromosomal stability by maintaining telomere length, and allowing cells to avert senescence. It constitutes a limiting factor for formation of the telomerase complex in cancer cells [1]. TERT is one of two major components of the larger telomerase complex, which extends telomeres by adding specific short repetitive DNA sequences. These tandem repeats are bound by the shelterin complex, which is composed of six proteins: telomere repeat factor 1 and 2 (TRF1, TRF2), protection of telomeres 1 (POT1), TRF1-interacting nuclear protein 2 (TIN2), tripeptidyl peptidase I (TPP1), and repressor/activator protein 1 (RAP1) (Figure 1) [2].
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