Microtubule-associated serine/threonine-protein kinase 2 (MAST2, also known as MAST205) belongs to the MAST family, which is characterised by containing a serine/threonine kinase domain and a PDZ (postsynaptic density protein-95/discs large/zona occludens-1) domain []. MAST2 regulates lipopolysaccharide-induced IL-12 synthesis in macrophages by forming a complex with TRAF6, resulting in the inhibition of TRAF6 NF-kappa-B activation [, ]. It localises in the DAPC/UAPC, which is found within the postsynaptic region of the neuromuscular junction (NMJ) and central synapses []. It also functions in spermatid maturation in mammals [].
MAST (Microtubule-Associated Serine/Threonine) kinases are characterised by containing a serine/threonine kinase domain and a PDZ (postsynaptic density protein-95/discs large/zona occludens-1) domain []. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN []. MAST1 links the dystrophin/utrophin network with microtubule filaments via the syntrophins []. MAST1 localises in the DAPC/UAPC, which is found within the postsynaptic region of the neuromuscular junction (NMJ) and central synapses []. The splice variant of its C-terminal affects its subcellular localisation within neurons []. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3 [].
