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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.

Pubmed ID: 7973632

Authors

  • Stone JM
  • Collinge MA
  • Smith RD
  • Horn MA
  • Walker JC

Journal

Science (New York, N.Y.)

Publication Data

November 4, 1994

Associated Grants

None

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