Search results for MAPK14

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Reaction (4 results from a total of 4)

Identifier: R-HSA-9662823
Species: Homo sapiens
Compartment: cytosol, plasma membrane
The phosphorylation of disintegrin and metalloproteinase domain-containing protein 17 (ADAM17) by PLK2 and MAPKs has been determined by direct and indirect experiments (Müllberg et al. 1993, Schwarz et al. 2014, Fan and Derynck 1999; Gechtman et al. 1999; Díaz-Rodríguez et al. 2002; Fan, Turck, and Derynck 2003 & Xu and Derynck 2010). Specifically, the phosphorylation at residues Thr735 (Díaz-Rodríguez et al. 2002 & Xu and Derynck 2010) and Ser819 is required for ectodomains shedding.
Identifier: R-HSA-9626880
Species: Homo sapiens
Compartment: cytosol
In resting cells, the neutrophil cytosolic factor 1 (NCF1, also known as p47phox), NCF2 (p67phox), and NCF4 (p40phox) are located in the cytosol where they associate in a trimer complex with a 1:1:1 stoichiometry through specific domains (Groemping Y & Rittinger K 2005; El-Benna J et al. 2005; Park JW et al. 1994; Lapouge K et al. 2002; El-Benna J et al. 2016). However, NCF1 may also exist separately from the trimer (El-Benna J et al. 2016). In the resting state, two SH3 domains of NCF1 (p47phox) bind the auto‐inhibitory region (AIR; amino acids 292‐340) to keep NCF1 in a closed auto‐inhibited state, preventing its binding to p22phox and therefore NOX2 activation (Groemping Y et al. 2003; Yuzawa S et al. 2004; El-Benna J et al. 2016). Priming of neutrophils by several agents such as GM‐CSF, TNFα, PAF, LPS and CL097, a TLR7/8 agonist, induces partial phosphorylation of NCF1 (Makni-Maalej K et al. 2015; Dang PM et al. 1999; Dewas C et al. 2003; DeLeo FR et al. 1998). Mass spectrometry analysis of NCF1 identified Ser345 as the phosphorylated site in human neutrophils primed by TNFα and GM‐CSF (Dang PMC et al. 2006). Site‐directed mutagenesis of Ser345 and use of a competitive inhibitory peptide containing the Ser345 sequence have demonstrated that this step is critical for the priming of ROS production in human neutrophils (Dang PMC et al. 2006). Further, inhibitors of the p38 MAPK abrogated TNF-alpha- and TLR8 agonist-induced phosphorylation of Ser345 (Dang PMC et al. 2006; Makni-Maalej K et al. 2015).
Identifier: R-HSA-3238999
Species: Homo sapiens
Compartment: nucleoplasm
MAPKAPK5 (PRAK) forms a complex with MAPK14 (p38 alpha) or MAPK11 (p38 beta) irrespective of the phosphorylation status and kinase activity of MAPKAPK5, MAPK14 and MAPK11 (New et al. 2003). Phosphorylation of p38 alpha and p38 beta by MKK3 or MKK6 (Raingeaud et al. 1996), however, is required for the subsequent activation of MAPKAPK5 by p38 MAPK (New et al. 1998, Sun et al. 2007).
Identifier: R-HSA-3239019
Species: Homo sapiens
Compartment: nucleoplasm
MAPK14 (p38 alpha) and MAPK11 (p38 beta) phosphorylate MAPKAPK5 (PRAK) on threonine residue 182, located in the conserved LMTP site in the T-loop of the kinase domain. Phosphorylation of T182 is necessary for the MAPKAPK5 catalytic activity (New et al. 1998).
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