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

Julie M. Stone, Margaret A. Collinge, Robert D. Smith, Mark A. Horn, John C. Walker

Research output: Contribution to journalArticle

212 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)793-795
Number of pages3
JournalScience
Volume266
Issue number5186
DOIs
Publication statusPublished - Jan 1 1994

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