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.

Publication

A Novel GLP1 Receptor Interacting Protein ATP6ap2 Regulates Insulin Secretion in Pancreatic Beta Cells.

Dai FF, Bhattacharjee A, Liu Y, Batchuluun B, Zhang M, Wang XS, Huang X, Luu L, Zhu D, Gaisano H, Wheeler MB

GLP1 activates its receptor, GLP1R, to enhance insulin secretion. The activation and transduction of GLP1R requires complex interactions with a host of accessory proteins, most of which remain largely unknown. In this study, we used membrane-based split ubiquitin yeast two-hybrid assays to identify novel GLP1R interactors in both mouse and human islets. Among these, ATP6ap2 (ATPase H(+)-transporting lysosomal accessory protein ... [more]

J. Biol. Chem. Oct. 09, 2015; 290(41);25045-61 [Pubmed: 26272612]

Throughput

  • Low Throughput

Additional Notes

  • MYTH system (split-ubiquitin)

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
GLP1R G6PC2
Affinity Capture-MS
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.

High-BioGRID
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Curated By

  • BioGRID