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.
Department of Biochemistry, University of Missouri-Columbia 65211.
J M
JM
Stone
M A
MA
Collinge
R D
RD
Smith
M A
MA
Horn
J C
JC
Walker
D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000201:enzymology* / Q000235:genetics; D029681:Arabidopsis Proteins; D015139:Blotting, Southern; D002384:Catalysis; D017343:Genes, Plant; D008969:Molecular Sequence Data; D010749:Phosphoprotein Phosphatases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction
D029681:Arabidopsis Proteins; C089427:RLK5 protein, Arabidopsis; D017346:Protein Serine-Threonine Kinases; C090240:KAPP protein, Arabidopsis; D010749:Phosphoprotein Phosphatases