BAIT

IST1

YNL265C
Protein with positive role in the multivesicular body sorting pathway; functions and forms a complex with Did2p; recruitment to endosomes is mediated by the Vps2p-Vps24p subcomplex of ESCRT-III; also interacts with Vps4p
GO Process (1)
GO Function (0)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

IST1

YNL265C
Protein with positive role in the multivesicular body sorting pathway; functions and forms a complex with Did2p; recruitment to endosomes is mediated by the Vps2p-Vps24p subcomplex of ESCRT-III; also interacts with Vps4p
GO Process (1)
GO Function (0)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)

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

An in vivo map of the yeast protein interactome.

Tarassov K, Messier V, Landry CR, Radinovic S, Serna Molina MM, Shames I, Malitskaya Y, Vogel J, Bussey H, Michnick SW

Protein interactions regulate the systems-level behavior of cells; thus, deciphering the structure and dynamics of protein interaction networks in their cellular context is a central goal in biology. We have performed a genome-wide in vivo screen for protein-protein interactions in Saccharomyces cerevisiae by means of a protein-fragment complementation assay (PCA). We identified 2770 interactions among 1124 endogenously expressed proteins. Comparison ... [more]

Science Jun. 13, 2008; 320(5882);1465-70 [Pubmed: 18467557]

Throughput

  • High Throughput

Curated By

  • BioGRID