Stone J M, Collinge M A, Smith R D, Horn M A, Walker J C
Department of Biochemistry, University of Missouri-Columbia 65211.
Science. 1994 Nov 4;266(5186):793-5. doi: 10.1126/science.7973632.
A protein phosphatase was cloned that interacts with a serine-threonine receptor-like kinase, RLK5, from Arabidopsis thaliana. The phosphatase, designated KAPP (kinase-associated protein phosphatase), is composed of three domains: an amino-terminal signal anchor, a kinase interaction (KI) domain, and a type 2C protein phosphatase catalytic region. Association of RLK5 with the KI domain is dependent on phosphorylation of RLK5 and can be abolished by dephosphorylation. KAPP may function as a signaling component in a pathway involving RLK5.
从拟南芥中克隆出一种与丝氨酸 - 苏氨酸类受体激酶RLK5相互作用的蛋白磷酸酶。该磷酸酶被命名为KAPP（激酶相关蛋白磷酸酶），由三个结构域组成：一个氨基末端信号锚、一个激酶相互作用（KI）结构域和一个2C型蛋白磷酸酶催化区域。RLK5与KI结构域的结合依赖于RLK5的磷酸化，而去磷酸化可使其结合被消除。KAPP可能作为涉及RLK5的信号通路中的一个信号成分发挥作用。
