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Mol Cells. 2015 Sep;38(9):814-20. doi: 10.14348/molcells.2015.0144. Epub 2015 Jul 21.

Increased Stability of Nucleolar PinX1 in the Presence of TERT.

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Department of Bioscience and Biotechnology, Konkuk University, Seoul 143-701, Korea.
Department of Obstetrics and Gynecology, Hanyang University College of Medicine, Seoul 133-791, Korea.
Institute of Medical Science, Hanyang University College of Medicine, Seoul 133-791, Korea.


PinX1, a nucleolar protein of 328 amino acids, inhibits telomerase activity, which leads to the shortening of telomeres. The C-terminal region of PinX1 is responsible for its nucleolar localization and binding with TERT, a catalytic component of telomerase. A fraction of TERT localizes to the nucleolus, but the role of TERT in the nucleolus is largely unknown. Here, we report a functional connection between PinX1 and TERT regarding PinX1 stability. The C-terminal of PinX1(205-328), a nucleolar fragment, was much more stable than the N-terminal of PinX1(1-204), a nuclear fragment. Interestingly, PinX1 was less stable in TERT-depleted cells and more stable in TERT-myc expressing cells. Stability assays for PinX1 truncation forms showed that both PinX1(1-328) and PinX1(205-328), nucleolar forms, were more rapidly degraded in TERT-depleted cells, while they were more stably maintained in TERT-overexpressing cells, compared to each of the controls. However, PinX1(1-204) was degraded regardless of the TERT status. These results reveal that the stability of PinX1 is maintained in nucleolus in the presence of TERT and suggest a role of TERT in the regulation of PinX1 steady-state levels.


PinX1; TERT; nucleolus; protein stability

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