Proximity Ligation Analysis of protein-protein interactions between MAPK13 and MAPKAPK3. HeLa cells were stained with anti-MAPK13 rabbit purified polyclonal 1:1200 and anti-MAPKAPK3 mouse monoclonal antibody 1:50. Each red dot represents the detection of protein-protein interaction complex, and nuclei were counterstained with DAPI (blue).
This gene encodes a member of the Ser/Thr protein kinase family. This kinase functions as a mitogen-activated protein kinase (MAP kinase)- activated protein kinase. MAP kinases are also known as extracellular signal-regulated kinases (ERKs), act as an integration point for multiple biochemical signals. This kinase was shown to be activated by growth inducers and stress stimulation of cells. In vitro studies demonstrated that ERK, p38 MAP kinase and Jun N-terminal kinase were all able to phosphorylate and activate this kinase, which suggested the role of this kinase as an integrative element of signaling in both mitogen and stress responses. This kinase was reported to interact with, phosphorylate and repress the activity of E47, which is a basic helix-loop-helix transcription factor known to be involved in the regulation of tissue-specific gene expression and cell differentiation. [provided by RefSeq