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Correction: Corrigendum: Reprogramming to pluripotency is an ancient trait of vertebrate Oct4 and Pou2 proteins

Natalia Tapia
Peter Reinhardt
Hans R. Schöler
Amendments and Corrections05 Feb 2013
Nature Communications

Volume: 4, P: 1
The emergence of Sox and POU transcription factors predates the origins of animal stem cells

The pluripotency program is maintained by transcription factors from the Sox and POU families. Here they identify SOX and POU factors from unicellular relatives of animals and show that unicellular SOX can replace SOX2 to induce pluripotency, whilst unicellular POU differs from OCT4.

Ya Gao
Daisylyn Senna Tan
Ralf Jauch
ResearchOpen Access14 Nov 2024
Nature Communications

Volume: 15, P: 1-16
Dissecting the role of distinct OCT4-SOX2 heterodimer configurations in pluripotency

Natalia Tapia
Caitlin MacCarthy
Hans R. Schöler
ResearchOpen Access28 Aug 2015
Scientific Reports

Volume: 5, P: 1-9
The ubiquitination landscape of the influenza A virus polymerase

Influenza A virus replication relies on host cell-derived ubiquitination of the viral polymerase. Here, Günl et al. show that site-specific ubiquitination of PB1-K578 is acquired during infection and facilitates spatiotemporal control of polymerase dimerization and NP binding.

Franziska Günl
Tim Krischuns
Linda Brunotte
ResearchOpen Access11 Feb 2023
Nature Communications

Volume: 14, P: 1-19
Reprogramming to pluripotency is an ancient trait of vertebrate Oct4 and Pou2 proteins

The mammalian transcription factors Oct4 and Pou2 are implicated in germ cell pluripotency induction and maintenance. Tapia and colleagues find that axolotl Pou2 and Oct4 reprogram mouse and human fibroblasts to a pluripotent state, suggesting ancestral Oct4 and Pou2 gene function is evolutionarily conserved.

Natalia Tapia
Peter Reinhardt
Hans R. Schöler
Research11 Dec 2012
Nature Communications

Volume: 3, P: 1-12
A unique Oct4 interface is crucial for reprogramming to pluripotency

Oct4 cannot be replaced by other members of the same family of transcription factors to induce reprogramming. By comparing the structure of the POU family domain of Oct4 complexed to DNA with that of others, Schöler and colleagues identify an α-helix that is exposed on the surface of Oct4 and provides an interaction platform to recruit epigenetic modifiers to Oct4 targets. Mutations abolishing this helix suppress the reprogramming properties of Oct4.

Daniel Esch
Juha Vahokoski
Hans R. Schöler
Research03 Feb 2013
Nature Cell Biology

Volume: 15, P: 295-301

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Correction: Corrigendum: Reprogramming to pluripotency is an ancient trait of vertebrate Oct4 and Pou2 proteins

The emergence of Sox and POU transcription factors predates the origins of animal stem cells

Dissecting the role of distinct OCT4-SOX2 heterodimer configurations in pluripotency

The ubiquitination landscape of the influenza A virus polymerase

Reprogramming to pluripotency is an ancient trait of vertebrate Oct4 and Pou2 proteins

A unique Oct4 interface is crucial for reprogramming to pluripotency

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