PEPR1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
BAK1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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.
Publication
Structural basis for recognition of an endogenous peptide by the plant receptor kinase PEPR1.
The endogenous peptides AtPep1-8 in Arabidopsis mature from the conserved C-terminal portions of their precursor proteins PROPEP1-8, respectively. The two homologous leucine-rich repeat-receptor kinases (LRR-RKs) PEPR1 and PEPR2 act as receptors of AtPeps. AtPep binding leads to stable association of PEPR1,2 with the shared receptor LRR-RK BAK1, eliciting immune responses similar to those induced by pathogens. Here we report a ... [more]
Throughput
- Low Throughput
Additional Notes
- AtPep1 induces PEPR1 LRR-BAK1 LRR heterodimerization. (LRR = Leucine-rich repeat)
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| BAK1 PEPR1 | 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