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)

Curated By

BioGRID

Interaction Summary

GLP1R

Gene Ontology Biological Process

Gene Ontology Molecular Function

transmembrane signaling receptor activity [TAS]

Gene Ontology Cellular Component

VAMP3