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

Science (New York, N.Y.) | Nov 4, 1994

http://www.ncbi.nlm.nih.gov/pubmed/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.

Pubmed ID: 7973632 RIS Download

Mesh terms: Amino Acid Sequence | Arabidopsis | Arabidopsis Proteins | Blotting, Southern | Catalysis | Genes, Plant | Molecular Sequence Data | Phosphoprotein Phosphatases | Phosphorylation | Protein-Serine-Threonine Kinases | Sequence Homology, Amino Acid | Signal Transduction

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