Dyrk2-associated EDD-DDB1-VprBP E3 ligase inhibits telomerase by TERT degradation

Hae Yun Jung; Xin Wang; Sohee Jun; Jae Il Park

doi:10.1074/jbc.M112.416792

Dyrk2-associated EDD-DDB1-VprBP E3 ligase inhibits telomerase by TERT degradation

Hae Yun Jung, Xin Wang, Sohee Jun, Jae Il Park

Research output: Contribution to journal › Article › peer-review

56 Scopus citations

Abstract

Background: Telomerase is an essential enzyme for the immortalization of stem and cancer cells. Results: Dyrk2-associated E3 ligase targets telomerase reverse transcriptase, a catalytic subunit of telomerase. Conclusion: Dyrk2-E3 ligase is necessary to negatively regulate telomerase activity. Significance: Learning how telomerase is regulated is crucial for understanding telomerase regulatory mechanism in cancer and stem cells.

Original language	English (US)
Pages (from-to)	7252-7262
Number of pages	11
Journal	Journal of Biological Chemistry
Volume	288
Issue number	10
DOIs	https://doi.org/10.1074/jbc.M112.416792
State	Published - Mar 8 2013

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

MD Anderson CCSG core facilities

Advanced Technology Genomics Core

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10.1074/jbc.M112.416792

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title = "Dyrk2-associated EDD-DDB1-VprBP E3 ligase inhibits telomerase by TERT degradation",

abstract = "Background: Telomerase is an essential enzyme for the immortalization of stem and cancer cells. Results: Dyrk2-associated E3 ligase targets telomerase reverse transcriptase, a catalytic subunit of telomerase. Conclusion: Dyrk2-E3 ligase is necessary to negatively regulate telomerase activity. Significance: Learning how telomerase is regulated is crucial for understanding telomerase regulatory mechanism in cancer and stem cells.",

author = "Jung, {Hae Yun} and Xin Wang and Sohee Jun and Park, {Jae Il}",

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AU - Jung, Hae Yun

AU - Wang, Xin

AU - Jun, Sohee

AU - Park, Jae Il

PY - 2013/3/8

Y1 - 2013/3/8

N2 - Background: Telomerase is an essential enzyme for the immortalization of stem and cancer cells. Results: Dyrk2-associated E3 ligase targets telomerase reverse transcriptase, a catalytic subunit of telomerase. Conclusion: Dyrk2-E3 ligase is necessary to negatively regulate telomerase activity. Significance: Learning how telomerase is regulated is crucial for understanding telomerase regulatory mechanism in cancer and stem cells.

AB - Background: Telomerase is an essential enzyme for the immortalization of stem and cancer cells. Results: Dyrk2-associated E3 ligase targets telomerase reverse transcriptase, a catalytic subunit of telomerase. Conclusion: Dyrk2-E3 ligase is necessary to negatively regulate telomerase activity. Significance: Learning how telomerase is regulated is crucial for understanding telomerase regulatory mechanism in cancer and stem cells.

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Dyrk2-associated EDD-DDB1-VprBP E3 ligase inhibits telomerase by TERT degradation

Abstract

ASJC Scopus subject areas

MD Anderson CCSG core facilities

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