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  • MARCKS as a negative regulator of lipopolysaccharide signaling
    Manček Keber, Mateja ...
    Myristoylated alanine-rich C kinase substrate (MARCKS) is an intrinsically unfolded protein with a conserved cationic effector domain, which mediates thecross-talk between several signal transduction ... pathways. Transcription of MARCKS is increased by stimulation with bacterial LPS.We determined that MARCKS and MARCKS-related protein specifically bind to LPS and that the addition of the MARCKS effector peptide inhibited LPS-induced production of TNF-a in mononuclear cells. The LPS binding site within the effector domain ofMARCKS was narrowed down to a heptapeptide that binds to LPS in an extended conformation as determined by nuclear magnetic resonance spectroscopy. After LPS stimulation, MARCKS moved from the plasma membrane to FYVE-positive endosomes, where it colocalized with LPS. MARCKS-deficient mouse embryonic fibroblasts (MEFs) responded to LPS with increased IL-6 production compared with the matched wild-type MEFs. Similarly, small interfering RNA knockdown ofMARCKS also increased LPS signaling, whereas overexpression of MARCKS inhibited LPS signaling. TLR4 signaling was enhanced by the ablation of MARCKS, which had no effect on stimulation by TLR2, TLR3, and TLR5 agonists. These findings demonstrate that MARCKS contributes to the negative regulation of the cellular response to LPS
    Vir: The journal of immunology. - ISSN 0022-1767 (Vol. 188, no. 8, 2012, str. 3893-3902)
    Vrsta gradiva - članek, sestavni del
    Leto - 2012
    Jezik - angleški
    COBISS.SI-ID - 4930586

    Povezava(-e):

    http://www.jimmunol.org/content/early/2012/03/16/jimmunol.1003605.abstract
    DOI

vir: The journal of immunology. - ISSN 0022-1767 (Vol. 188, no. 8, 2012, str. 3893-3902)
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