Nogo-B is a new physiological substrate for MAPKAP-K2

Simon Rousseau (Lead / Corresponding author), Mark Peggie, David G. Campbell, Angel R. Nebredaf, Philip Cohen

    Research output: Contribution to journalArticle

    24 Citations (Scopus)

    Abstract

    The neurite outgrowth inhibitor protein Nogo is one of 300 proteins that contain a reticulon homology domain, which is responsible for their association with the endoplasmic reticulum. Here we have found that the Nogo-B spliceform becomes phosphorylated at Ser107 in response to lipopolysaccharide in RAW264 macrophages or anisomycin in HeLa cells. The phosphorylation is prevented by SB 203580, an inhibitor of SAPK2a (stress-activated protein kinase 2a)/p38α and SAPK2b/p38β, and does not occur in embryonic fibroblasts generated from SAPK2a/p38α-deficient mice. Nogo-B is phosphorylated at Ser107 in vitro by MAPKAP-K2 [MAPK (mitogen-activated protein kinase)-activated protein kinase-2] or MAPKAP-K3, but not by other protein kinases that are known to be activated by SAPK2a/p38α. The anisomycin-induced phosphorylation of Ser107 in HeLa cells can be prevented by 'knockdown' of MAPKAP-K2 using siRNA (small interfering RNA). Taken together, our results identify Nogo-B as a new physiological substrate of MAPKAP-K2.

    Original languageEnglish
    Pages (from-to)433-440
    Number of pages8
    JournalBiochemical Journal
    Volume391
    Issue number2
    DOIs
    Publication statusPublished - 15 Oct 2005

    Keywords

    • MAPK (mitogen-activated protein kinase)-activated protein kinase-K2 (MAPKAP-K2)
    • Microtubule
    • Nogo (neurite outgrowth inhibitor protein)
    • p38 (p38 MAPK)

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