BAIT

BOI1

BOB1, GIN7, L000000191, L000000703, YBL085W
Protein implicated in polar growth; functionally redundant with Boi2p; interacts with bud-emergence protein Bem1p; contains an SH3 (src homology 3) domain and a PH (pleckstrin homology) domain; relocalizes from bud neck to cytoplasm upon DNA replication stress; BOI1 has a paralog, BOI2, that arose from the whole genome duplication
GO Process (2)
GO Function (1)
GO Component (6)
Saccharomyces cerevisiae (S288c)
PREY

SEC3

PSL1, L000001829, L000001520, YER008C
Subunit of the exocyst complex; the exocyst mediates polarized targeting and tethering of post-Golgi secretory vesicles to sites of exocytosis prior to SNARE-mediated fusion; PtdIns[4,5]P2-binding protein that localizes to exocytic sites in a Rho1p-dependent, actin-independent manner, targeting and anchoring the exocyst to the plasma membrane with Exo70p; direct GTP Rho1p effector; required for ER inheritance; relocalizes away from bud neck upon DNA replication stress
Saccharomyces cerevisiae (S288c)

Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

The cell polarity proteins Boi1p and Boi2p stimulate vesicle fusion at the plasma membrane of yeast cells.

Kustermann J, Wu Y, Rieger L, Dedden D, Phan T, Walther P, Duenkler A, Johnsson N

Eukaryotic cells can direct secretion to defined regions of their plasma membrane. These regions are distinguished by an elaborate architecture of proteins and lipids that are specialized to capture and fuse post-Golgi vesicles. Here, we show that the proteins Boi1p and Boi2p are important elements of this area of active exocytosis at the tip of growing yeast cells. Cells lacking ... [more]

J. Cell. Sci. Sep. 15, 2017; 130(18);2996-3008 [Pubmed: 28751498]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
SEC3 BOI1
Negative Genetic
Negative Genetic

Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores.

High-0.1877BioGRID
374258
BOI1 SEC3
PCA
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.

Low-BioGRID
2446937
BOI1 SEC3
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.

High-BioGRID
-

Curated By

  • BioGRID