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Interaction of a protein phosphatase with an Arabidopsis serine-threonine receptor kinase.

Authors:
Stone JM, Collinge MA, Smith RD, Horn MA, Walker JC
Affiliation:
Journal:
Science (New York, N.Y.)

Abstract

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.

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