Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily.
High levels of expression in heart, brain, skeletal muscle and pancreas, lower levels observed in lung, liver and kidney.
Autophosphorylated. Phosphorylated at Thr-208 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Phosphorylation at Thr-208 by TAOK1 activates the kinase activity, leading to phosphorylation and detachment of MAPT/TAU from microtubules. Phosphorylation at Ser-212 by GSK3-beta (GSK3B) inhibits the kinase activity. Phosphorylation by CaMK1 promotes activity and is required to promote neurite outgrowth. Phosphorylation at Thr-596 by PRKCZ/aPKC in polarized epithelial cells inhibits the kinase activity and promotes binding to 14-3-3 protein YWHAZ, leading to relocation from cell membrane to cytoplasm.
Cell membrane. Cytoplasm. Cytoskeleton.
Microtubule affinity-regulating kinase 2 (MARK2), also known as EMK1 (ELKL motif kinase 1) or Par1b, is a 788 amino acid protein that is a member of the protein kinase superfamily, MARK subfamily. Highly expressed in heart, brain, skeletal muscle and pancreas, MARK2 is essential for the asymmetric development of membrane domains around polarized epithelial cells. Activation of MARK2 by phosphorylation on Thr 208 allows the protein to modulate the building of a columnar versus a hepatic epithelial cell. MARK2 contains one KA1 (kinase-associated) domain, one protein kinase domain and one UBA domain. MARK2 is expressed as 14 isoforms produced by alternative splicing events. Some of these isoforms may function in graft rejection.
Wei, Xianfu et al.
MARK2 enhances cisplatin resistance via PI3K/AKT/NF-κB signaling pathway in osteosarcoma cells. | American Journal of Translational Research