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A protein interaction network for pluripotency of embryonic stem cells

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  • Jianlong Wang

    (Children’s Hospital and Dana Farber Cancer Institute, Harvard Medical School, Harvard Stem Cell Institute)

  • Sridhar Rao

    (Children’s Hospital and Dana Farber Cancer Institute, Harvard Medical School, Harvard Stem Cell Institute)

  • Jianlin Chu

    (Children’s Hospital and Dana Farber Cancer Institute, Harvard Medical School, Harvard Stem Cell Institute)

  • Xiaohua Shen

    (Children’s Hospital and Dana Farber Cancer Institute, Harvard Medical School, Harvard Stem Cell Institute)

  • Dana N. Levasseur

    (Children’s Hospital and Dana Farber Cancer Institute, Harvard Medical School, Harvard Stem Cell Institute)

  • Thorold W. Theunissen

    (Children’s Hospital and Dana Farber Cancer Institute, Harvard Medical School, Harvard Stem Cell Institute)

  • Stuart H. Orkin

    (Children’s Hospital and Dana Farber Cancer Institute, Harvard Medical School, Harvard Stem Cell Institute
    Howard Hughes Medical Institute)

Abstract

Embryonic stem (ES) cells are pluripotent1,2 and of therapeutic potential in regenerative medicine3,4. Understanding pluripotency at the molecular level should illuminate fundamental properties of stem cells and the process of cellular reprogramming. Through cell fusion the embryonic cell phenotype can be imposed on somatic cells, a process promoted by the homeodomain protein Nanog5, which is central to the maintenance of ES cell pluripotency6,7. Nanog is thought to function in concert with other factors such as Oct4 (ref. 8) and Sox2 (ref. 9) to establish ES cell identity. Here we explore the protein network in which Nanog operates in mouse ES cells. Using affinity purification of Nanog under native conditions followed by mass spectrometry, we have identified physically associated proteins. In an iterative fashion we also identified partners of several Nanog-associated proteins (including Oct4), validated the functional relevance of selected newly identified components and constructed a protein interaction network. The network is highly enriched for nuclear factors that are individually critical for maintenance of the ES cell state and co-regulated on differentiation. The network is linked to multiple co-repressor pathways and is composed of numerous proteins whose encoding genes are putative direct transcriptional targets of its members. This tight protein network seems to function as a cellular module dedicated to pluripotency.

Suggested Citation

  • Jianlong Wang & Sridhar Rao & Jianlin Chu & Xiaohua Shen & Dana N. Levasseur & Thorold W. Theunissen & Stuart H. Orkin, 2006. "A protein interaction network for pluripotency of embryonic stem cells," Nature, Nature, vol. 444(7117), pages 364-368, November.
    • Handle: RePEc:nat:nature:v:444:y:2006:i:7117:d:10.1038_nature05284
    DOI: 10.1038/nature05284
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    Cited by:

    1. Amin R Mazloom & Ruth Dannenfelser & Neil R Clark & Arsen V Grigoryan & Kathryn M Linder & Timothy J Cardozo & Julia C Bond & Aislyn D W Boran & Ravi Iyengar & Anna Malovannaya & Rainer B Lanz & Avi M, 2011. "Recovering Protein-Protein and Domain-Domain Interactions from Aggregation of IP-MS Proteomics of Coregulator Complexes," PLOS Computational Biology, Public Library of Science, vol. 7(12), pages 1-10, December.
    2. Xinru Zhang & Bohao Fang & Yi-Fei Huang, 2023. "Transcription factor binding sites are frequently under accelerated evolution in primates," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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