PKA phosphorylates MAPKAPK5

Stable Identifier
Reaction [transition]
Homo sapiens
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MAPKAPK5 is phosphorylated at serine 115 by the catalytic subunit of PKA, which translocates into the nucleus in response to elevated cellular cAMP levels. Phosphorylation at serine 115 promotes the cytoplasmic relocalization of MAPKAPK5 and is required for HSBP1-dependent rearrangements of F-actin in response to PKA (Gerits et al, 2007; Kostenko et al, 2011a; Kostenko et al, 2009; reviewed in Kostenko et al, 2011b)
Literature References
PubMed ID Title Journal Year
20849292 Cross-talk between protein kinase A and the MAPK-activated protein kinases RSK1 and MK5

Dumitriu, G, Kostenko, S, Moens, U, Gerits, N, Shiryaev, A

J. Recept. Signal Transduct. Res. 2011
20734105 Serine residue 115 of MAPK-activated protein kinase MK5 is crucial for its PKA-regulated nuclear export and biological function

Dumitriu, G, Klenow, H, Kostenko, S, Moens, U, Johannessen, M, Gerits, N, Shiryaev, A

Cell. Mol. Life Sci. 2011
17947239 Modulation of F-actin rearrangement by the cyclic AMP/cAMP-dependent protein kinase (PKA) pathway is mediated by MAPK-activated protein kinase 5 and requires PKA-induced nuclear export of MK5

Kostenko, S, Mikalsen, T, Moens, U, Johannessen, M, Gerits, N, Shiryaev, A

J. Biol. Chem. 2007
19166925 PKA-induced F-actin rearrangement requires phosphorylation of Hsp27 by the MAPKAP kinase MK5

Kostenko, S, Moens, U, Johannessen, M

Cell. Signal. 2009
Catalyst Activity

cAMP-dependent protein kinase activity of Protein Kinase A, catalytic subunits [nucleoplasm]

Orthologous Events
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