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Mob-binding domain found in the NDR/LATS family serine/threonine protein kinases The nuclear Dbf2-related (NDR)/large tumor suppressor (LATS) family includes NDR, LATS, CBK1, and Sid2p. They are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. NDR/LATS kinases 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. These 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/LATS family serine/threonine protein kinases. |
Jiyao W et al.(2023). "The conserved domain database in 2023.",