The TET enzymes

The TET enzymes During the past decade, we have learnt that the most common DNA modification, 5-methylcytosine (5mC), playing crucial roles in development and disease, is not stable but can be actively reversed to its unmodified form via enzymatic catalysis involving the TET enzymes. These ground-breaking discoveries have been achieved thanks to technological advances in the detection of the oxidized forms of 5mC and to the boldness of individual scientists. The TET enzymes require molecular oxygen for their catalysis, making them important targets for hypoxia research. They also require special cofactors which enable additional levels of regulation. Moreover, mutations and other genetic alterations in TETs are found, especially in myeloid malignances. This review focuses on the kinetic and inhibitory properties of the TET enzymes and the role of TETs in cellular differentiation and transformation and in cancer. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Cellular and Molecular Life Sciences Springer Journals

The TET enzymes

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Publisher
Springer International Publishing
Copyright
Copyright © 2017 by Springer International Publishing AG, part of Springer Nature
Subject
Life Sciences; Cell Biology; Biomedicine, general; Life Sciences, general; Biochemistry, general
ISSN
1420-682X
eISSN
1420-9071
D.O.I.
10.1007/s00018-017-2721-8
Publisher site
See Article on Publisher Site

Abstract

During the past decade, we have learnt that the most common DNA modification, 5-methylcytosine (5mC), playing crucial roles in development and disease, is not stable but can be actively reversed to its unmodified form via enzymatic catalysis involving the TET enzymes. These ground-breaking discoveries have been achieved thanks to technological advances in the detection of the oxidized forms of 5mC and to the boldness of individual scientists. The TET enzymes require molecular oxygen for their catalysis, making them important targets for hypoxia research. They also require special cofactors which enable additional levels of regulation. Moreover, mutations and other genetic alterations in TETs are found, especially in myeloid malignances. This review focuses on the kinetic and inhibitory properties of the TET enzymes and the role of TETs in cellular differentiation and transformation and in cancer.

Journal

Cellular and Molecular Life Sciences – Springer Journals

Published: Nov 28, 2017

References

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  • TET1 suppresses cancer invasion by activating the tissue inhibitors of metalloproteinases
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  • Loss of 5-hydroxymethylcytosine is linked to gene body hypermethylation in kidney cancer
    Chen, K; Zhang, J; Guo, Z; Ma, Q; Xu, Z; Zhou, Y; Xu, Z; Li, Z; Liu, Y; Ye, X; Li, X; Yuan, B; Ke, Y; He, C; Zhou, L; Liu, J; Ci, W
  • Loss of the epigenetic mark, 5-hydroxymethylcytosine, correlates with small cell/nevoid subpopulations and assists in microstaging of human melanoma
    Lee, JJ; Cook, M; Mihm, MC; Xu, S; Zhan, Q; Wang, TJ; Murphy, GF; Lian, CG
  • Epigenetic silencing of TET2 and TET3 induces an EMT-like process in melanoma
    Gong, F; Guo, Y; Niu, Y; Jin, J; Zhang, X; Shi, X; Zhang, L; Li, R; Chen, L; Ma, RZ
  • Combined loss of Tet1 and Tet2 promotes B cell, but not myeloid malignancies, in mice
    Zhao, Z; Chen, L; Dawlaty, MM; Pan, F; Weeks, O; Zhou, Y; Cao, Z; Shi, H; Wang, J; Lin, L; Chen, S; Yuan, W; Qin, Z; Ni, H; Nimer, SD; Yang, FC; Jaenisch, R; Jin, P; Xu, M
  • Fumarate is an epigenetic modifier that elicits epithelial-to-mesenchymal transition
    Sciacovelli, M; Gonçalves, E; Johnson, TI; Zecchini, VR; Costa, Ana; Henriques, Sofia; Gaude, E; Drubbel, AV; Theobald, SJ; Abbo, SR; Tran, MGB; Rajeeve, V; Cardaci, S; Foster, S; Yun, H; Cutillas, P; Warren, A; Gnanapragasam, V; Gottlieb, E; Franze, K; Huntly, B; Maher, ER; Maxwell, PH; Saez-Rodriguez, J; Frezza, C
  • 5-Hydroxymethylcytosine expression in proliferative nodules arising within congenital nevi allows differentiation from malignant melanoma
    Pavlova, O; Fraitag, S; Hohl, D
  • TET family proteins and 5-hydroxymethylcytosine in esophageal squamous cell carcinoma
    Murata, A; Baba, Y; Ishimoto, T; Miyake, K; Kosumi, K; Harada, K; Kurashige, J; Iwagami, S; Sakamoto, Y; Miyamoto, Y; Yoshida, N; Yamamoto, M; Oda, S; Watanabe, M; Nakao, M; Baba, H
  • Decreased 5-Hydroxymethylcytosine (5-hmC) predicts poor prognosis in early-stage laryngeal squamous cell carcinoma
    Zhang, Y; Wu, K; Shao, Y; Sui, F; Yang, Q; Shi, B; Hou, P; Ji, M
  • Adult T cell leukemia aggressivenness correlates with loss of both 5-hydroxymethylcytosine and TET2 expression
    Marçais, A; Waast, L; Bruneau, J; Hanssens, K; Asnafi, V; Gaulard, P; Suarez, F; Dubreuil, P; Gessain, A; Hermine, O; Pique, C
  • Impact of TET2 mutations on response rate to azacitidine in myelodysplastic syndromes and low blast count acute myeloid leukemias
    Itzykson, R; Kosmider, O; Cluzeau, T; Mansat-De Mas, V; Dreyfus, F; Beyne-Rauzy, O; Quesnel, B; Vey, N; Gelsi-Boyer, V; Raynaud, S; Preudhomme, C; Ades, L; Fenaux, P; Fontenay, M
  • TET2 mutations predict response to hypomethylating agents in myelodysplastic syndrome patients
    Bejar, R; Lord, A; Stevenson, K; Bar-Natan, M; Perez-Ladaga, A; Zaneveld, J; Wang, H; Caughey, B; Stojanov, P; Getz, G; Garcia-Manero, G; Kantarjian, H; Chen, R; Stone, RM; Neuberg, D; Steensma, DP; Ebert, BL
  • Inhibition of hypoxia-inducible factor (HIF) hydroxylases by citric acid cycle intermediates: possible links between cell metabolism and stabilization of HIF
    Koivunen, P; Hirsila, M; Remes, AM; Hassinen, IE; Kivirikko, KI; Myllyharju, J
  • The length of peptide substrates has a marked effect on hydroxylation by the hypoxia-inducible factor prolyl 4-hydroxylases
    Koivunen, P; Hirsila, M; Kivirikko, KI; Myllyharju, J
  • Studies on the activity of the hypoxia-inducible-factor hydroxylases using an oxygen consumption assay
    Ehrismann, D; Flashman, E; Genn, DN; Mathioudakis, N; Hewitson, KS; Ratcliffe, PJ; Schofield, CJ
  • Characterization of the iron- and 2-oxoglutarate-binding sites of human prolyl 4-hydroxylase
    Myllyharju, J; Kivirikko, KI
  • Hydroxylation of (Pro-Pro-Gly)5 and (Pro-Pro-Gly)10 by prolyl hydroxylase. Evidence for an asymmetric active site in the enzyme
    Berg, RA; Kishida, Y; Sakakibara, S; Prockop, DJ
  • Catalytic properties of the asparaginyl hydroxylase (FIH) in the oxygen sensing pathway are distinct from those of its prolyl 4-hydroxylases
    Koivunen, P; Hirsila, M; Gunzler, V; Kivirikko, KI; Myllyharju, J
  • The activity of JmjC histone lysine demethylase KDM4A is highly sensitive to oxygen concentrations
    Hancock, RL; Masson, N; Dunne, K; Flashman, E; Kawamura, A
  • Studies on the catalytic domains of multiple JmjC oxygenases using peptide substrates
    Williams, ST; Walport, LJ; Hopkinson, RJ; Madden, SK; Chowdhury, R; Schofield, CJ; Kawamura, A
  • Repair of methylation damage in DNA and RNA by mammalian AlkB homologues
    Lee, DH; Jin, SG; Cai, S; Chen, Y; Pfeifer, GP; O’Connor, TR
  • The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for 2-oxoglutarate decarboxylation in a ligand reaction at the enzyme-bound ferrous ion
    Majamaa, K; Hanauske-Abel, HM; Gunzler, V; Kivirikko, KI
  • Mechanism of the prolyl hydroxylase reaction. 1. Role of co-substrates
    Tuderman, L; Myllyla, R; Kivirikko, KI
  • Inhibitor scaffolds for 2-oxoglutarate-dependent histone lysine demethylases
    Rose, NR; Ng, SS; Mecinovic, J; Lienard, BM; Bello, SH; Sun, Z; McDonough, MA; Oppermann, U; Schofield, CJ

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