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Identification of the components of PRDM14 complex in ESCs

ABSTRACT: We investigated the N-terminal domain of PRDM14, which has no discernable functional domain, and its contribution to the maintenance of pluripotency. We performed a mass spectrometry analysis of the PRDM14-containing complex to disclose partner molecules that bind to the N-terminal domain of PRDM14.

ORGANISM(S): Mus Musculus (mouse)

SUBMITTER: Yoshiyuki Seki

PROVIDER: PXD020571 | JPOST Repository | Mon Aug 03 00:00:00 BST 2020

REPOSITORIES: jPOST

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			Action	DRS
	1_PRMD14_Full_L1_P01.raw	Raw
	1_PRMD14_Full_L1_P02.raw	Raw
	1_PRMD14_Full_L1_P03.raw	Raw
	1_PRMD14_Full_L1_P04.raw	Raw
	1_PRMD14_Full_L1_P05.raw	Raw

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Publications

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

Yamamoto Maiko M Suwa Yoshiaki Y Sugiyama Kohta K Okashita Naoki N Kawaguchi Masanori M Tani Naoki N Matsubara Kazumi K Nakamura Akira A Seki Yoshiyuki Y

Journal of cell science 20200814 15

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 PRD ...[more]

PMID: 32661086

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Pol II phosphorylation regulates a switch between transcriptional and splicing condensates

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