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Updated: Sep 13, 2026

Identification of Post-translational Modifications of Plant Protein Complexes
Published on: February 22, 2014
Interaction of a protein phosphatase with an Arabidopsis serine-threonine receptor kinase
J M Stone1, M A Collinge, R D Smith
1Department of Biochemistry, University of Missouri-Columbia 65211.
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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