BAIT

AT5G59010

K19M22.7, K19M22_7
brassinosteroid-signaling kinase 5
GO Process (0)
GO Function (0)
GO Component (2)

Gene Ontology Cellular Component

Arabidopsis thaliana (Columbia)
PREY

BSK1

BR-signaling kinase 1, F23E12.210, F23E12_210, AT4G35230
BR-signaling kinase 1
GO Process (2)
GO Function (2)
GO Component (4)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Arabidopsis thaliana (Columbia)

Two-hybrid

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

BSKs are partially redundant positive regulators of brassinosteroid signaling in Arabidopsis.

Sreeramulu S, Mostizky Y, Sunitha S, Shani E, Nahum H, Salomon D, Ben Hayun L, Gruetter C, Rauh D, Ori N, Sessa G

Arabidopsis thaliana Brassinosteroid Signaling Kinases (BSKs) constitute a receptor-like cytoplasmic kinase subfamily (RLCK-XII) of 12 members. Previous analysis demonstrated a positive role for BSK1 and BSK3 in the initial steps of brassinosteroid (BR) signal transduction. To investigate the function of BSKs in plant growth and BR signaling, we characterized T-DNA insertion lines within 8 BSK genes (BSK1 to BSK8) and ... [more]

Plant J. Mar. 15, 2013; 0(0); [Pubmed: 23496207]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
BSK1 AT5G59010
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.

Low-BioGRID
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Curated By

  • BioGRID