PREY

HA2

AHA2, F9N11.40, F9N11_40, H(+)-ATPase 2, P-TYPE H(+)-ATPASE ISOFORM 2, PLASMA MEMBRANE PROTON ATPASE 2, PMA2, AT4G30190
H(+)-ATPase 2
Arabidopsis thaliana (Columbia)

Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

Publication

RIN4 functions with plasma membrane H+-ATPases to regulate stomatal apertures during pathogen attack.

Liu J, Elmore JM, Fuglsang AT, Palmgren MG, Staskawicz BJ, Coaker G

Pathogen perception by the plant innate immune system is of central importance to plant survival and productivity. The Arabidopsis protein RIN4 is a negative regulator of plant immunity. In order to identify additional proteins involved in RIN4-mediated immune signal transduction, we purified components of the RIN4 protein complex. We identified six novel proteins that had not previously been implicated in ... [more]

PLoS Biol. Jun. 30, 2009; 7(6);e1000139 [Pubmed: 19564897]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
RIN4 HA2
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
-
RIN4 HA2
Two-hybrid
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.

Low-BioGRID
-

Curated By

  • BioGRID