Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.

Publication

Abiotic Stress-Inducible Receptor-Like Kinases Negatively Control ABA Signaling in Arabidopsis.

Tanaka H, Osakabe Y, Katsura S, Mizuno S, Maruyama K, Kusakabe K, Mizoi J, Shinozaki K, Yamaguchi-Shinozaki K

Membrane-anchored receptor-like protein kinases (RLKs) recognize extracellular signals at the cell surface and activate the downstream signaling pathway by phosphorylating specific target proteins. We analyzed a receptor-like cytosolic kinase (RLCK), ARCK1, whose expression was induced by abiotic stress. ARCK1 belongs to the cysteine-rich repeat (CRR)-RLK subfamily and encodes a cytosolic protein kinase. The arck1 mutant showed higher sensitivity than the ... [more]

Unknown Jan. 07, 2012; 0(0); [Pubmed: 22225700]

Throughput

Low Throughput

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
AT4G11890 CRK39	PCA PCA A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay.	Tanaka H (2012)	Low	-	BioGRID	-

Curated By

BioGRID

Interaction Summary

AT4G11890

Gene Ontology Biological Process

Gene Ontology Molecular Function

kinase activity [ISS]

CRK39