Publication Date:
1994-11-04
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stone, J M -- Collinge, M A -- Smith, R D -- Horn, M A -- Walker, J C -- New York, N.Y. -- Science. 1994 Nov 4;266(5186):793-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Missouri-Columbia 65211.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973632" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Arabidopsis/*enzymology/genetics
;
*Arabidopsis Proteins
;
Blotting, Southern
;
Catalysis
;
Genes, Plant
;
Molecular Sequence Data
;
Phosphoprotein Phosphatases/chemistry/genetics/*metabolism
;
Phosphorylation
;
Protein-Serine-Threonine Kinases/*metabolism
;
Sequence Homology, Amino Acid
;
Signal Transduction
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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