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An expanded Oct4 interaction network: implications for stem cell biology, development, and disease.

Cell stem cell | Apr 2, 2010

The transcription factor Oct4 is key in embryonic stem cell identity and reprogramming. Insight into its partners should illuminate how the pluripotent state is established and regulated. Here, we identify a considerably expanded set of Oct4-binding proteins in mouse embryonic stem cells. We find that Oct4 associates with a varied set of proteins including regulators of gene expression and modulators of Oct4 function. Half of its partners are transcriptionally regulated by Oct4 itself or other stem cell transcription factors, whereas one-third display a significant change in expression upon cell differentiation. The majority of Oct4-associated proteins studied to date show an early lethal phenotype when mutated. A fraction of the human orthologs is associated with inherited developmental disorders or causative of cancer. The Oct4 interactome provides a resource for dissecting mechanisms of Oct4 function, enlightening the basis of pluripotency and development, and identifying potential additional reprogramming factors.

Pubmed ID: 20362542 RIS Download

Mesh terms: Animals | Cell Differentiation | Chromosomes, Artificial, Bacterial | Disease | Embryonic Stem Cells | Gene Dosage | Gene Expression Regulation, Developmental | Gene Transfer Techniques | Humans | Mice | Models, Biological | Mutation | Neoplasms | Octamer Transcription Factor-3 | Phenotype | Protein Binding | Recombinant Fusion Proteins | Transcription, Genetic

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Associated grants

  • Agency: Medical Research Council, Id: MC_U105185859
  • Agency: Wellcome Trust, Id:

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Centralized, standards compliant, public data repository for proteomics data, including protein and peptide identifications, post-translational modifications and supporting spectral evidence. Originally it was developed to provide a common data exchange format and repository to support proteomics literature publications. This remit has grown with PRIDE, with the hope that PRIDE will provide a reference set of tissue-based identifications for use by the community. The future development of PRIDE has become closely linked to HUPO PSI. PRIDE encourages and welcomes direct user submissions of protein and peptide identification data to be published in peer-reviewed publications. Users may Browse public datasets, use PRIDE BioMart for custom queries, or download the data directly from the FTP site. PRIDE has been developed through a collaboration of the EMBL-EBI, Ghent University in Belgium, and the University of Manchester.


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