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Science 4 November 1994:
Vol. 266. no. 5186, pp. 793 - 795
DOI: 10.1126/science.7973632
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Articles

Science, Vol 266, Issue 5186, 793-795
Copyright © 1994 by American Association for the Advancement of Science

articles

Interaction of a protein phosphatase with an Arabidopsis serine-threonine receptor kinase

JM Stone, MA Collinge, RD Smith, MA Horn, and JC Walker

Department of Biochemistry, University of Missouri-Columbia 65211.

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.


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