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Mob-binding domain found in nuclear Dbf2-related kinase 1 (NDR1) and similar proteins NDR1, also called serine/threonine-protein kinase 38 (STK38), plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersensitive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR1 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 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 NDR1 serine/threonine protein kinase. |
Jiyao W et al.(2023). "The conserved domain database in 2023.",