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The H2B ubiquitin-protein ligase RNF40 is required for somatic cell reprogramming

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The H2B ubiquitin-protein ligase RNF40 is required for somatic cell reprogramming. / Xie, Wanhua; Miehe, Michaela; Laufer, Sandra; Johnsen, Steven A.

In: CELL DEATH DIS, Vol. 11, No. 4, 27.04.2020, p. 287.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Xie, W, Miehe, M, Laufer, S & Johnsen, SA 2020, 'The H2B ubiquitin-protein ligase RNF40 is required for somatic cell reprogramming', CELL DEATH DIS, vol. 11, no. 4, pp. 287. https://doi.org/10.1038/s41419-020-2482-4

APA

Xie, W., Miehe, M., Laufer, S., & Johnsen, S. A. (2020). The H2B ubiquitin-protein ligase RNF40 is required for somatic cell reprogramming. CELL DEATH DIS, 11(4), 287. https://doi.org/10.1038/s41419-020-2482-4

Vancouver

Xie W, Miehe M, Laufer S, Johnsen SA. The H2B ubiquitin-protein ligase RNF40 is required for somatic cell reprogramming. CELL DEATH DIS. 2020 Apr 27;11(4):287. https://doi.org/10.1038/s41419-020-2482-4

Bibtex

@article{fe23fa1d4fe5472eac5308015fc0bae5,
title = "The H2B ubiquitin-protein ligase RNF40 is required for somatic cell reprogramming",
abstract = "Direct reprogramming of somatic cells to induced pluripotent stem cells (iPSCs) requires a resetting of the epigenome in order to facilitate a cell fate transition. Previous studies have shown that epigenetic modifying enzymes play a central role in controlling induced pluripotency and the generation of iPSC. Here we show that RNF40, a histone H2B lysine 120 E3 ubiquitin-protein ligase, is specifically required for early reprogramming during induced pluripotency. Loss of RNF40-mediated H2B monoubiquitination (H2Bub1) impaired early gene activation in reprogramming. We further show that RNF40 contributes to tissue-specific gene suppression via indirect effects by controlling the expression of the polycomb repressive complex-2 histone methyltransferase component EZH2, as well as through more direct effects by promoting the resolution of H3K4me3/H3K27me3 bivalency on H2Bub1-occupied pluripotency genes. Thus, we identify RNF40 as a central epigenetic mediator of cell state transition with distinct functions in resetting somatic cell state to pluripotency.",
author = "Wanhua Xie and Michaela Miehe and Sandra Laufer and Johnsen, {Steven A}",
year = "2020",
month = apr,
day = "27",
doi = "10.1038/s41419-020-2482-4",
language = "English",
volume = "11",
pages = "287",
journal = "CELL DEATH DIS",
issn = "2041-4889",
publisher = "NATURE PUBLISHING GROUP",
number = "4",

}

RIS

TY - JOUR

T1 - The H2B ubiquitin-protein ligase RNF40 is required for somatic cell reprogramming

AU - Xie, Wanhua

AU - Miehe, Michaela

AU - Laufer, Sandra

AU - Johnsen, Steven A

PY - 2020/4/27

Y1 - 2020/4/27

N2 - Direct reprogramming of somatic cells to induced pluripotent stem cells (iPSCs) requires a resetting of the epigenome in order to facilitate a cell fate transition. Previous studies have shown that epigenetic modifying enzymes play a central role in controlling induced pluripotency and the generation of iPSC. Here we show that RNF40, a histone H2B lysine 120 E3 ubiquitin-protein ligase, is specifically required for early reprogramming during induced pluripotency. Loss of RNF40-mediated H2B monoubiquitination (H2Bub1) impaired early gene activation in reprogramming. We further show that RNF40 contributes to tissue-specific gene suppression via indirect effects by controlling the expression of the polycomb repressive complex-2 histone methyltransferase component EZH2, as well as through more direct effects by promoting the resolution of H3K4me3/H3K27me3 bivalency on H2Bub1-occupied pluripotency genes. Thus, we identify RNF40 as a central epigenetic mediator of cell state transition with distinct functions in resetting somatic cell state to pluripotency.

AB - Direct reprogramming of somatic cells to induced pluripotent stem cells (iPSCs) requires a resetting of the epigenome in order to facilitate a cell fate transition. Previous studies have shown that epigenetic modifying enzymes play a central role in controlling induced pluripotency and the generation of iPSC. Here we show that RNF40, a histone H2B lysine 120 E3 ubiquitin-protein ligase, is specifically required for early reprogramming during induced pluripotency. Loss of RNF40-mediated H2B monoubiquitination (H2Bub1) impaired early gene activation in reprogramming. We further show that RNF40 contributes to tissue-specific gene suppression via indirect effects by controlling the expression of the polycomb repressive complex-2 histone methyltransferase component EZH2, as well as through more direct effects by promoting the resolution of H3K4me3/H3K27me3 bivalency on H2Bub1-occupied pluripotency genes. Thus, we identify RNF40 as a central epigenetic mediator of cell state transition with distinct functions in resetting somatic cell state to pluripotency.

U2 - 10.1038/s41419-020-2482-4

DO - 10.1038/s41419-020-2482-4

M3 - SCORING: Journal article

C2 - 32341358

VL - 11

SP - 287

JO - CELL DEATH DIS

JF - CELL DEATH DIS

SN - 2041-4889

IS - 4

ER -