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The direct activation of MIK, a germinal center kinase (GCK)-like kinase, by MARK, a maize atypical receptor kinase, suggests a new mechanism for signaling through kinase-dead receptors

AuthorsLlompart, Blanca; Castells, Enric; Río, Adolfo; Roca, Ramón; Ferrando, Adolfo; Stiefel, Virginia; Puigdomènech, Pere ; Casacuberta, Josep M.
Issue Date28-Nov-2003
PublisherAmerican Society for Biochemistry and Molecular Biology
CitationJournal of Biological Chemistry
AbstractSignaling by receptor protein kinases (RPKs) involves their dimerization and transphosphorylation. However, atypical RPKs with kinase-defective domains have been described recently. Some of them are essential for proper signaling in animal systems, although the precise mechanism involved is unknown in most cases. Here we describe the cloning and characterization of an atypical plant receptor kinase from maize, MARK, which does not phosphorylate in vitro. A yeast two-hybrid approach has allowed us to identify a new germinal center kinase (GCK)-related protein, MIK, that interacts with MARK. Interestingly, the interaction of the intracellular domain of MARK with the regulator domain of MIK strongly induces MIK kinase activity. As some GCK-related proteins connect cell-surface receptors to the intracellular MAPK cascades, the activation of MIK by direct interaction with MARK could illustrate a new mechanism for signaling through atypical RPKs.
Description7 pages, 8 figures.-- PMID: 12966093[PubMed].
Publisher version (URL)http://dx.doi.org/10.1074/jbc.M307482200
Appears in Collections:(IQAC) Artículos
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