Interaction of a protein phosphatase with an Arabidopsis serine-threonine receptor kinase.
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.
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
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
Science
Date: Nov. 04, 1994
PubMed ID: 7973632
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