Open Access
PLoS ONE, volume 13, issue 2, pages e0193182
Hexokinase 2 is a molecular bridge linking telomerase and autophagy
Roh Jae Il
1
,
Kim Yujin
1
,
Oh Jahyun
1
,
Kim Yunmi
1
,
Lee JeeHyun
1
,
Lee Jaehoon
1
,
Chun Kyung-Hee
2
,
LEE Han-Woong
1
1
Department of Biochemistry, College of Life Science and Biotechnology and Yonsei Laboratory Animal Research Center, Yonsei University, Seoul, Republic of Korea
|
2
Department of Biochemistry & Molecular Biology, Yonsei University College of Medicine, Seoul, Republic of Korea
|
Publication type: Journal Article
Publication date: 2018-02-20
PubMed ID:
29462198
Multidisciplinary
Abstract
Autophagy is systematically regulated by upstream factors and nutrients. Recent studies reported that telomerase and hexokinase 2 [HK2) regulate autophagy through mTOR and that telomerase has the capacity to bind to the HK2 promoter. However, the molecular linkage among telomerase, HK2, and autophagy is not fully understood. Here, we show that HK2 connects telomerase to autophagy. HK2 inhibition in HepG2 cells suppressed TERT-induced autophagy activation and further enhancement by glucose deprivation. The HK2 downstream factor mTOR was responsible for the TERT-induced autophagy activation under glucose deprivation, implying that TERT promotes autophagy through an HK2-mTOR pathway. TERC played a role similar to that of TERT, and simultaneous expression of TERT and TERC synergistically enhanced HK2 expression and autophagy. At the gene level, TERT bound to the HK2 promoter at a specific region harboring the telomerase-responsive sequence ‘TTGGG.’ Mutagenesis of TERC and the TERT-responsive element in the HK2 promoter revealed that TERC is required for the binding of TERT to the HK2 promoter. We demonstrate the existence of a telomerase-HK2-mTOR-autophagy axis and suggest that inhibition of the interaction between telomerase and the HK2 promoter diminishes glucose starvation-induced autophagy.
Citations by journals
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Journal of Cell Science
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1 publication, 3.85%
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Citations by publishers
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4
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4 publications, 15.38%
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Elsevier
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2 publications, 7.69%
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Wiley
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2 publications, 7.69%
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Bentham Science
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1 publication, 3.85%
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Mary Ann Liebert
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1 publication, 3.85%
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Tech Science Press
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Tech Science Press, 1, 3.85%
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1 publication, 3.85%
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Public Library of Science (PLoS)
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1 publication, 3.85%
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KeAi Communications Co.
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1 publication, 3.85%
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Hindawi Limited
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Hindawi Limited
1 publication, 3.85%
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- We do not take into account publications that without a DOI.
- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.
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Roh J. I. et al. Hexokinase 2 is a molecular bridge linking telomerase and autophagy // PLoS ONE. 2018. Vol. 13. No. 2. p. e0193182.
GOST all authors (up to 50)
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Roh J. I., Kim Y., Oh J., Kim Y., Lee J., Lee J., Chun K., LEE H. Hexokinase 2 is a molecular bridge linking telomerase and autophagy // PLoS ONE. 2018. Vol. 13. No. 2. p. e0193182.
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TY - JOUR
DO - 10.1371/journal.pone.0193182
UR - https://doi.org/10.1371%2Fjournal.pone.0193182
TI - Hexokinase 2 is a molecular bridge linking telomerase and autophagy
T2 - PLoS ONE
AU - Roh, Jae Il
AU - Kim, Yujin
AU - Oh, Jahyun
AU - Kim, Yunmi
AU - Lee, JeeHyun
AU - Lee, Jaehoon
AU - Chun, Kyung-Hee
AU - LEE, Han-Woong
PY - 2018
DA - 2018/02/20 00:00:00
PB - Public Library of Science (PLoS)
SP - e0193182
IS - 2
VL - 13
PMID - 29462198
SN - 1932-6203
ER -
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@article{2018_Roh,
author = {Jae Il Roh and Yujin Kim and Jahyun Oh and Yunmi Kim and JeeHyun Lee and Jaehoon Lee and Kyung-Hee Chun and Han-Woong LEE},
title = {Hexokinase 2 is a molecular bridge linking telomerase and autophagy},
journal = {PLoS ONE},
year = {2018},
volume = {13},
publisher = {Public Library of Science (PLoS)},
month = {feb},
url = {https://doi.org/10.1371%2Fjournal.pone.0193182},
number = {2},
pages = {e0193182},
doi = {10.1371/journal.pone.0193182}
}
Cite this
MLA
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Roh, Jae Il, et al. “Hexokinase 2 is a molecular bridge linking telomerase and autophagy.” PLoS ONE, vol. 13, no. 2, Feb. 2018, p. e0193182. https://doi.org/10.1371%2Fjournal.pone.0193182.