Interaction of the maize and Arabidopsis kinase interaction domains with a subset of receptor-like protein kinases: Implications for transmembrane signaling in plants

David M. Braun, Julie M. Stone, John C. Walker

Research output: Contribution to journalArticle

98 Citations (Scopus)

Abstract

The kinase interaction (KI) domain of kinase-associated protein phosphatase (KAPP) interacts with the phosphorylated form of an Arabidopsis thaliana receptor-like protein kinase (RLK). The KI domain may recruit KAPP into an RLK-initiated signaling complex. To examine additional roles that this domain may play in plant signal transduction, a search was conducted for other KI domain-containing proteins. One gene was isolated which encodes a KI domain, the maize homolog of KAPP. To test whether the maize KI domain associates with other maize proteins, it was used as a probe in a protein-protein interaction cloning strategy. A new maize RLK, KI domain interacting kinase 1 (KIK1), was identified by its interaction with the maize KI domain. The maize KI domain and the KIK1 kinase domain association required phosphorylation of the kinase. This work establishes that the KI domain phosphorylation-dependent signaling mechanism is present in both monocots and dicots, Additionally, it was determined that both the maize and Arabidopsis KI domains interact with several but not all of the active RLKs assayed. These multiple associations imply that KAPP may function in a number of RLK-initiated signaling pathways.

Original languageEnglish (US)
Pages (from-to)83-95
Number of pages13
JournalPlant Journal
Volume12
Issue number1
DOIs
StatePublished - Jan 1 1997

Fingerprint

Arabidopsis
protein kinases
Protein Kinases
Zea mays
phosphotransferases (kinases)
Phosphotransferases
receptors
corn
Phosphoprotein Phosphatases
proteins
phosphorylation
Phosphorylation
Protein Interaction Domains and Motifs
Proteins
protein-protein interactions
Magnoliopsida
Liliopsida

ASJC Scopus subject areas

  • Genetics
  • Plant Science
  • Cell Biology

Cite this

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title = "Interaction of the maize and Arabidopsis kinase interaction domains with a subset of receptor-like protein kinases: Implications for transmembrane signaling in plants",
abstract = "The kinase interaction (KI) domain of kinase-associated protein phosphatase (KAPP) interacts with the phosphorylated form of an Arabidopsis thaliana receptor-like protein kinase (RLK). The KI domain may recruit KAPP into an RLK-initiated signaling complex. To examine additional roles that this domain may play in plant signal transduction, a search was conducted for other KI domain-containing proteins. One gene was isolated which encodes a KI domain, the maize homolog of KAPP. To test whether the maize KI domain associates with other maize proteins, it was used as a probe in a protein-protein interaction cloning strategy. A new maize RLK, KI domain interacting kinase 1 (KIK1), was identified by its interaction with the maize KI domain. The maize KI domain and the KIK1 kinase domain association required phosphorylation of the kinase. This work establishes that the KI domain phosphorylation-dependent signaling mechanism is present in both monocots and dicots, Additionally, it was determined that both the maize and Arabidopsis KI domains interact with several but not all of the active RLKs assayed. These multiple associations imply that KAPP may function in a number of RLK-initiated signaling pathways.",
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