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Nucleophosmin Interacts with PIN2/TERF1-interacting Telomerase Inhibitor 1 (PinX1) and Attenuates the PinX1 Inhibition on Telomerase Activity
Telomerase activation and telomere maintenance are critical for cellular immortalization and transformation. PIN2/TERF1-interacting telomerase inhibitor 1 (PinX1) is a telomerase regulator and the aberrant expression of PinX1 causes telomere shortening. Identifying PinX1-interacting proteins is impo...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5334639/ https://www.ncbi.nlm.nih.gov/pubmed/28255170 http://dx.doi.org/10.1038/srep43650 |
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author | Cheung, Derek Hang-Cheong Ho, Sai-Tim Lau, Kwok-Fai Jin, Rui Wang, Ya-Nan Kung, Hsiang-Fu Huang, Jun-Jian Shaw, Pang-Chui |
author_facet | Cheung, Derek Hang-Cheong Ho, Sai-Tim Lau, Kwok-Fai Jin, Rui Wang, Ya-Nan Kung, Hsiang-Fu Huang, Jun-Jian Shaw, Pang-Chui |
author_sort | Cheung, Derek Hang-Cheong |
collection | PubMed |
description | Telomerase activation and telomere maintenance are critical for cellular immortalization and transformation. PIN2/TERF1-interacting telomerase inhibitor 1 (PinX1) is a telomerase regulator and the aberrant expression of PinX1 causes telomere shortening. Identifying PinX1-interacting proteins is important for understanding telomere maintenance. We found that PinX1 directly interacts with nucleophosmin (NPM), a protein that has been shown to positively correlate with telomerase activity. We further showed that PinX1 acts as a linker in the association between NPM and hTERT, the catalytic subunit of telomerase. Additionally, the recruitment of NPM by PinX1 to the telomerase complex could partially attenuate the PinX1-mediated inhibition on telomerase activity. Taken together, our data reveal a novel mechanism that regulates telomerase activation through the interaction between NPM, PinX1 and the telomerase complex. |
format | Online Article Text |
id | pubmed-5334639 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-53346392017-03-06 Nucleophosmin Interacts with PIN2/TERF1-interacting Telomerase Inhibitor 1 (PinX1) and Attenuates the PinX1 Inhibition on Telomerase Activity Cheung, Derek Hang-Cheong Ho, Sai-Tim Lau, Kwok-Fai Jin, Rui Wang, Ya-Nan Kung, Hsiang-Fu Huang, Jun-Jian Shaw, Pang-Chui Sci Rep Article Telomerase activation and telomere maintenance are critical for cellular immortalization and transformation. PIN2/TERF1-interacting telomerase inhibitor 1 (PinX1) is a telomerase regulator and the aberrant expression of PinX1 causes telomere shortening. Identifying PinX1-interacting proteins is important for understanding telomere maintenance. We found that PinX1 directly interacts with nucleophosmin (NPM), a protein that has been shown to positively correlate with telomerase activity. We further showed that PinX1 acts as a linker in the association between NPM and hTERT, the catalytic subunit of telomerase. Additionally, the recruitment of NPM by PinX1 to the telomerase complex could partially attenuate the PinX1-mediated inhibition on telomerase activity. Taken together, our data reveal a novel mechanism that regulates telomerase activation through the interaction between NPM, PinX1 and the telomerase complex. Nature Publishing Group 2017-03-03 /pmc/articles/PMC5334639/ /pubmed/28255170 http://dx.doi.org/10.1038/srep43650 Text en Copyright © 2017, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Cheung, Derek Hang-Cheong Ho, Sai-Tim Lau, Kwok-Fai Jin, Rui Wang, Ya-Nan Kung, Hsiang-Fu Huang, Jun-Jian Shaw, Pang-Chui Nucleophosmin Interacts with PIN2/TERF1-interacting Telomerase Inhibitor 1 (PinX1) and Attenuates the PinX1 Inhibition on Telomerase Activity |
title | Nucleophosmin Interacts with PIN2/TERF1-interacting Telomerase Inhibitor 1 (PinX1) and Attenuates the PinX1 Inhibition on Telomerase Activity |
title_full | Nucleophosmin Interacts with PIN2/TERF1-interacting Telomerase Inhibitor 1 (PinX1) and Attenuates the PinX1 Inhibition on Telomerase Activity |
title_fullStr | Nucleophosmin Interacts with PIN2/TERF1-interacting Telomerase Inhibitor 1 (PinX1) and Attenuates the PinX1 Inhibition on Telomerase Activity |
title_full_unstemmed | Nucleophosmin Interacts with PIN2/TERF1-interacting Telomerase Inhibitor 1 (PinX1) and Attenuates the PinX1 Inhibition on Telomerase Activity |
title_short | Nucleophosmin Interacts with PIN2/TERF1-interacting Telomerase Inhibitor 1 (PinX1) and Attenuates the PinX1 Inhibition on Telomerase Activity |
title_sort | nucleophosmin interacts with pin2/terf1-interacting telomerase inhibitor 1 (pinx1) and attenuates the pinx1 inhibition on telomerase activity |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5334639/ https://www.ncbi.nlm.nih.gov/pubmed/28255170 http://dx.doi.org/10.1038/srep43650 |
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