RT Journal Article
SR Electronic
T1 Interaction of a protein phosphatase with an Arabidopsis serine-threonine receptor kinase
JF Science
JO Science
FD American Association for the Advancement of Science
SP 793
OP 795
DO 10.1126/science.7973632
VO 266
IS 5186
A1 Stone, JM
A1 Collinge, MA
A1 Smith, RD
A1 Horn, MA
A1 Walker, JC
YR 1994
UL http://science.sciencemag.org/content/266/5186/793.abstract
AB 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.