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    Methods Mol Biol. 2009;517:169-90.

    Analysis of ubiquitin degradation and phosphorylation of proteins.

    Gray P.

    Source

    Division of Pediatric Infectious Diseases, University of California Los Angeles, Los Angeles, CA 90048, USA. grayp@cshs.org

    Abstract

    Both ubiquitination and phosphorylation are crucial mediators involved in controlling the functions of numerous proteins belonging to the Toll-like receptor (TLR) signaling pathways. Altering the aforementioned post-translational events can be detrimental to the host survival. Therefore, the importance of these modifications cannot be overestimated. This chapter describes techniques used to examine if a protein is ubiquitinated and/or phosphorylated. In addition, a method is provided to identify the modified amino acids. We have previously shown using these techniques that the protein MyD88 adapter-like (Mal) is phosphorylated and ubiquitinated following activation of the TLR2 and TLR4 signaling pathways. Both post-translational modifications are essential for the activation and degradation of Mal, and thus are crucial steps, in regulating these TLR signaling cascades and consequently the innate immune response.

    PMID:
    19378034
    [PubMed - indexed for MEDLINE]

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