Synonyms
Historical Background
Murine and human MK5 cDNAs were initially isolated in 1998 in two independent screens for proteins with sequence homology to MK2 (New et al. 1998; Ni et al. 1998). The novel 54-kDa kinase ubiquitously expressed in all tissues displayed 45% amino acid identity to MK2. Both groups showed that MK5 could be phosphorylated and activated in vitro by the p38 MAP kinase, as detected by 32P incorporation into a substrate peptide (KKRPQRATSNVFS) or Hsp25 (HSPB1). New et al. named this kinase as p38-regulated and activated kinase or PRAK to emphasize its integration into the p38 pathway. More recently, MK5 has also been shown to interact with the atypical MAP kinases, ERK3 (MAPK6) and ERK4 (MAPK4), and these kinases are also involved in the phosphorylation and activation of MK5 (Schumacher et al. 2004; Seternes et al. 2004; Aberg et al. 2006; Kant et al. 2006). An MK5 gene does not appear to be present in either C. elegans or Drosophila...
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Menon, M.B., Kotlyarov, A. (2018). MAP Kinase-Activated Protein Kinase 5 (MK5). In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, Cham. https://doi.org/10.1007/978-3-319-67199-4_321
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DOI: https://doi.org/10.1007/978-3-319-67199-4_321
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