Mob-binding domain found in the nuclear Dbf2-related kinase (NDR) subfamily
NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also includes Drosophila melanogaster tricorner, which is a serine/threonine-protein kinase that plays an important role in controlling cell structure and proliferation of a variety of polarized outgrowths including epidermal hairs, bristles, arista laterals, and dendrites. It affects cellular morphogenesis by regulating the expression of target genes that encode cytoskeleton-interacting proteins and not via the direct modification of the cytoskeleton. It maintains the integrity of epidermal hairs and is an essential component of the signaling pathway regulating dendritic branching of sensory neurons. The NDR subfamily belongs to the NDR/LATS family of kinases that bind to highly conserved Mob (Mps One binder) coactivators, forming regulatory complexes that control a diverse set of in vivo effector proteins, and are essential and evolutionarily conserved components of "Hippo" signaling pathways. Mob association creates a novel binding pocket that participates in the formation of the active state of NDR/LATS kinases. NDR-like kinases contain a regulatory domain located N-terminal to the serine/threonine kinase domain (called the N-terminal regulatory (NTR) domain) and an insert within the catalytic domain that contains an auto-inhibitory sequence. This model corresponds to the NTR or Mob-binding domain of NDR-like serine/threonine protein kinases.
Jiyao W et al.(2023). "The conserved domain database in 2023.",