Phosphorylation of LATS1 and 2 by p-STK4 (p-MST1)

Cytosolic LATS1 and LATS2 are phosphorylated by phospho-STK4 (p-MST1). LATS proteins are known to form complexes with MOB1 proteins and this reaction is annotated with LATS:MOB1 complexes as its substrate. Likewise, phosphorylated (active) STK4 (p-MST1) and SAV1 are known to form a complex and that complex is annotated as the catalyst of this reaction. Serine-909 and threonine-1079 have been identified as LATS1 residues phosphorylated by STK4 (MST1) kinase. The target residues of LATS2 have not been identified experimentally but are inferred to be serine-872 and threonine-1041 based on sequence similarity (Chan et al. 2005).

细胞质中的LATS1和LATS2蛋白由磷酸化型的STK4（p-MST1）进行磷酸化。已知LATS蛋白与MOB1蛋白形成复合物，该反应以LATS:MOB1复合物作为其底物进行标注。同样，磷酸化（活性）的STK4（p-MST1）与SAV1蛋白亦能形成复合物，该复合物被标注为该反应的催化剂。Serine-909和threonine-1079已被鉴定为LATS1蛋白由STK4（MST1）激酶磷酸化的残基。尽管LATS2蛋白的目标残基尚未通过实验确定，但基于序列相似性推断，其可能为serine-872和threonine-1041（Chan等，2005年）。