BAIT

TOPP4

type one serine/threonine protein phosphatase 4, AT2G39840
serine/threonine-protein phosphatase PP1 isozyme 4
GO Process (1)
GO Function (1)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Arabidopsis thaliana (Columbia)
PREY

AT4G40100

T5J17.2, T5J17_2
PP1 regulatory subunit2-like protein1
GO Process (2)
GO Function (0)
GO Component (1)

Gene Ontology Biological Process

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

Identification of a Regulatory Subunit of Protein Phosphatase 1 Which Mediates Blue Light Signaling for Stomatal Opening.

Takemiya A, Yamauchi S, Yano T, Ariyoshi C, Shimazaki KI

Protein phosphatase 1 (PP1) is a eukaryotic Ser/Thr protein phosphatase comprised of a catalytic subunit (PP1c) and a regulatory subunit that modulates catalytic activity, subcellular localization, and substrate specificity. PP1c positively regulates stomatal opening through blue light signaling between phototropins and the plasma membrane H(+)-ATPase in guard cells. However, the regulatory subunit functioning in this process is unknown. We identified ... [more]

Unknown May. 13, 2012; 0(0); [Pubmed: 22585556]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
TOPP4 AT4G40100
Reconstituted Complex
Reconstituted Complex

An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.

Low-BioGRID
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Curated By

  • BioGRID