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    Expanding the substantial interactome of NEMO using protein microarrays.

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    Authors
    Fenner, Beau J
    Scannell, Michael
    Prehn, Jochen H M
    Affiliation
    Centre for Human Proteomics and Department of Physiology and Medical Physics, Royal College of Surgeons in Ireland, Dublin, Ireland.
    Issue Date
    2010
    
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    Citation
    Expanding the substantial interactome of NEMO using protein microarrays. 2010, 5 (1):e8799 PLoS ONE
    Journal
    PloS one
    URI
    http://hdl.handle.net/10147/93877
    DOI
    10.1371/journal.pone.0008799
    PubMed ID
    20098747
    Abstract
    Signal transduction by the NF-kappaB pathway is a key regulator of a host of cellular responses to extracellular and intracellular messages. The NEMO adaptor protein lies at the top of this pathway and serves as a molecular conduit, connecting signals transmitted from upstream sensors to the downstream NF-kappaB transcription factor and subsequent gene activation. The position of NEMO within this pathway makes it an attractive target from which to search for new proteins that link NF-kappaB signaling to additional pathways and upstream effectors. In this work, we have used protein microarrays to identify novel NEMO interactors. A total of 112 protein interactors were identified, with the most statistically significant hit being the canonical NEMO interactor IKKbeta, with IKKalpha also being identified. Of the novel interactors, more than 30% were kinases, while at least 25% were involved in signal transduction. Binding of NEMO to several interactors, including CALB1, CDK2, SAG, SENP2 and SYT1, was confirmed using GST pulldown assays and coimmunoprecipitation, validating the initial screening approach. Overexpression of CALB1, CDK2 and SAG was found to stimulate transcriptional activation by NF-kappaB, while SYT1 overexpression repressed TNFalpha-dependent NF-kappaB transcriptional activation in human embryonic kidney cells. Corresponding with this finding, RNA silencing of CDK2, SAG and SENP2 reduced NF-kappaB transcriptional activation, supporting a positive role for these proteins in the NF-kappaB pathway. The identification of a host of new NEMO interactors opens up new research opportunities to improve understanding of this essential cell signaling pathway.
    Language
    en
    ISSN
    1932-6203
    ae974a485f413a2113503eed53cd6c53
    10.1371/journal.pone.0008799
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