Mitogen-activated protein kinase 15 (MAPK15)

Mitogen-activated protein kinase 15 (MAPK15) is a member of the MAP kinase family, commonly referred to as ERK7 or ERK8, and defined by atypical structural and functional properties. MAPK15 is found across many species and is involved in multiple cell-signaling pathways related to autophagy, ciliogenesis, and protein trafficking. It regulates both basal and starvation-induced autophagy by interacting with ATG8 family proteins (LC3B, GABARAP, GABARAPL1), stimulating autophagosome formation, protein degradation, and influencing genome stability via interaction with PCNA. MAPK15's activity connects stress responses such as nutrient deprivation and oxidative damage to critical processes maintaining cellular viability and integrity. Pathophysiologically, loss of MAPK15 function or expression correlates with increased cell motility and reduced carcinogenic resistance, suggesting roles in cancer progression, and it is also considered a potential therapeutic target for ciliopathies and malignancies linked to genomic instability[1][2][3].

Other names

Mitogen-activated protein kinase 15MAPK15ERK7ERK8MAP kinase 15ERK-7ERK-8extracellular signal-regulated kinase 7extracellular signal-regulated kinase 8MAPK 15

Most described mechanisms are based on kinase-mediated phosphorylation affecting autophagy, regulation of PCNA (DNA replication), and response to nutrient depletion and oxidative stress[2][3].