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Cited by 231

The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.

O-GlcNAcylation regulates EZH2 protein stability and function

Open access
Chu, Chi-Shuen, Lo, Pei-Wen, Yeh, Yi-Hsien, Hsu, Pang-Hung, Peng, Shih-Huan, Teng, Yu-Ching, Kang, Ming-Lun, Wong, Chi-Huey, Juan, Li-Jung·2014·Proceedings of the National Academy of Sciences

Abstract

Significance: The present study identifies a cross-talk of two important posttranslational modifications, revealing that enhancer of zeste homolog 2 (EZH2) O-GlcNAcylation (GlcNac, N -acetylglucosamine) at serine 75 is required for EZH2 protein stability and therefore facilitates the histone H3 trimethylation at K27 to form H3K27me3. The finding is significant because both O-linked GlcNAc transferase-mediated O-GlcNAcylation and EZH2-mediated H3K27me3 formation play a pivotal role in development, and their up-regulation is believed to participate in tumor malignancy. The identification of O-linked GlcNAc transferase association with the polycomb repressive complex 2 (PRC2) further provides a new approach to regulate PRC2 function.

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Metadata

Authors
Chu, C.-S., Lo, P.-W., Yeh, Y.-H., Hsu, P.-H., Peng, S.-H., Teng, Y.-C., Kang, M.-L., Wong, C.-H., & Juan, L.-J.
Venue
Proceedings of the National Academy of Sciences
Published
2014-01-13
Volume
111
Issue
4
Pages
1355-1360
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2050575492
Cited by
231
References
6
FWCI
8.03
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: O-GlcNAcylation regulates EZH2 protein stability and function. https://app.cochat.ai/papers/10.1073/pnas.1323226111
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Chu, C.-S., Lo, P.-W., Yeh, Y.-H., Hsu, P.-H., Peng, S.-H., Teng, Y.-C., Kang, M.-L., Wong, C.-H., & Juan, L.-J. (2014). O-GlcNAcylation regulates EZH2 protein stability and function. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1323226111

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