Journal
JOURNAL OF CELLULAR PHYSIOLOGY
Volume 232, Issue 8, Pages 2083-2093Publisher
WILEY
DOI: 10.1002/jcp.25607
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Funding
- National Research Foundation of Korea (NRF) [2015R1A2A2A01003080, 2014M3C7A1064545]
- Korea Health Industry Development Institute (KHIDI) [HI14C0093]
- Yonsei University Research Fund [2014-12-0134]
- Yonsei University Future-leading Research Initiative [2015-22-0055]
- National Research Foundation of Korea [2015R1A2A2A01003080, 2014M3C7A1064545] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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Human telomerase reverse transcriptase (hTERT) is the catalytic subunit of telomerase, an RNA-dependent DNA polymerase that elongates telomeric DNA. hTERT displays several extra-telomeric functions that are independent of its telomere-regulatory function, including tumor progression, and neuronal cell death regulation. In this study, we evaluated these additional hTERT non-telomeric functions. We determined that hTERT interacts with several 19S and 20S proteasome subunits. The 19S regulatory particle and 20S core particle are part of 26S proteasome complex, which plays a central role in ubiquitin-dependent proteolysis. In addition, hTERT positively regulated 26S proteasome activity independent of its enzymatic activity. Moreover, hTERT enhanced subunit interactions, which may underlie hTERT's ability of hTERT to stimulate the 26S proteasome. Furthermore, hTERT displayed cytoprotective effect against ER stress via the activation of 26S proteasome in acute myeloid leukemia cells. Our data suggest that hTERT acts as a novel chaperone to promote 26S proteasome assembly and maintenance. J. Cell. Physiol. 232: 2083-2093, 2017. (c) 2016 Wiley Periodicals, Inc.
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