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Mob-binding domain found in large tumor suppressor homolog 2 (LATS2) LATS2, also called kinase phosphorylated during mitosis protein, serine/threonine-protein kinase kpm, or Warts-like kinase, is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and for governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. LATS2 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. LATS proteins 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 LATS2 serine/threonine protein kinase. |
Jiyao W et al.(2023). "The conserved domain database in 2023.",