Abstract
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.
Original language | English (US) |
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Pages (from-to) | 793-795 |
Number of pages | 3 |
Journal | Science |
Volume | 266 |
Issue number | 5186 |
DOIs | |
State | Published - 1994 |
Externally published | Yes |
ASJC Scopus subject areas
- General