The PRDM14-CtBP1/2-PRC2 complex regulates transcriptional repression during the transition from primed to naïve pluripotency.


Journal

Journal of cell science
ISSN: 1477-9137
Titre abrégé: J Cell Sci
Pays: England
ID NLM: 0052457

Informations de publication

Date de publication:
14 08 2020
Historique:
received: 27 11 2019
accepted: 25 06 2020
pubmed: 15 7 2020
medline: 22 6 2021
entrez: 15 7 2020
Statut: epublish

Résumé

The pluripotency-associated transcriptional network is regulated by a core circuitry of transcription factors. The PR domain-containing protein PRDM14 maintains pluripotency by activating and repressing transcription in a target gene-dependent manner. However, the mechanisms underlying dichotomic switching of PRDM14-mediated transcriptional control remain elusive. Here, we identified C-terminal binding protein 1 and 2 (CtBP1 and CtBP2; generically referred to as CtBP1/2) as components of the PRDM14-mediated repressive complex. CtBP1/2 binding to PRDM14 depends on CBFA2T2, a core component of the PRDM14 complex. The loss of

Identifiants

pubmed: 32661086
pii: jcs.240176
doi: 10.1242/jcs.240176
pii:
doi:

Substances chimiques

Co-Repressor Proteins 0
DNA-Binding Proteins 0
PRDM14 protein, human 0
RNA-Binding Proteins 0
Transcription Factors 0
Alcohol Oxidoreductases EC 1.1.-
CTBP2 protein, human EC 1.1.-
Polycomb Repressive Complex 2 EC 2.1.1.43

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Informations de copyright

© 2020. Published by The Company of Biologists Ltd.

Déclaration de conflit d'intérêts

Competing interestsThe authors declare no competing or financial interests.

Auteurs

Maiko Yamamoto (M)

Department of Biomedical Chemistry, School of Science and Technology, Kwansei Gakuin University, 2-1 Gakuen, Sanda, Hyogo 669-1337, Japan.

Yoshiaki Suwa (Y)

Department of Biomedical Chemistry, School of Science and Technology, Kwansei Gakuin University, 2-1 Gakuen, Sanda, Hyogo 669-1337, Japan.

Kohta Sugiyama (K)

Department of Biomedical Chemistry, School of Science and Technology, Kwansei Gakuin University, 2-1 Gakuen, Sanda, Hyogo 669-1337, Japan.

Naoki Okashita (N)

Department of Biomedical Chemistry, School of Science and Technology, Kwansei Gakuin University, 2-1 Gakuen, Sanda, Hyogo 669-1337, Japan.

Masanori Kawaguchi (M)

Department of Biomedical Chemistry, School of Science and Technology, Kwansei Gakuin University, 2-1 Gakuen, Sanda, Hyogo 669-1337, Japan.

Naoki Tani (N)

Liaison Laboratory Research Promotion Center, Institute of Molecular Embryology and Genetics, Kumamoto University, 2-2-1 Honjo, Chuo-ku, Kumamoto 860-0811, Japan.

Kazumi Matsubara (K)

Department of Biomedical Chemistry, School of Science and Technology, Kwansei Gakuin University, 2-1 Gakuen, Sanda, Hyogo 669-1337, Japan.

Akira Nakamura (A)

Department of Germline Development, Institute of Molecular Embryology and Genetics, Kumamoto University, 2-2-1 Honjo, Chuo-ku, Kumamoto 860-0811, Japan.

Yoshiyuki Seki (Y)

Department of Biomedical Chemistry, School of Science and Technology, Kwansei Gakuin University, 2-1 Gakuen, Sanda, Hyogo 669-1337, Japan yseki@kwansei.ac.jp.

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Classifications MeSH