BAIT

BNI1

PPF3, SHE5, formin BNI1, L000000190, YNL271C
Formin; polarisome component; nucleates the formation of linear actin filaments, involved in cell processes such as budding and mitotic spindle orientation which require the formation of polarized actin cables, functionally redundant with BNR1
Saccharomyces cerevisiae (S288c)
PREY

SEC5

L000001831, YDR166C
Essential 107kDa subunit of the exocyst complex; the exocyst mediates polarized targeting and tethering of post-Golgi secretory vesicles to active sites of exocytosis at the plasma membrane prior to SNARE-mediated fusion; involved in assembly of the exocyst complex; required with Sec3p for ER inheritance where it promotes anchoring of the cortical ER at the bud tip
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

The cell polarity proteins Boi1 and Boi2 direct an actin nucleation complex to sites of exocytosis in Saccharomyces cerevisiae.

Glomb O, Wu Y, Rieger L, Ruethnick D, Mulaw MA, Johnsson N

Owing to the local enrichment of factors that influence its dynamics and organization, the actin cytoskeleton displays different shapes and functions within the same cell. In yeast cells, post-Golgi vesicles ride on long actin cables to the bud tip. The proteins Boi1 and Boi2 (Boi1/2) participate in tethering and docking these vesicles to the plasma membrane. Here, we show in ... [more]

J. Cell. Sci. Feb. 13, 2020; 133(3); [Pubmed: 31964708]

Throughput

  • Low Throughput

Additional Notes

  • split-ubiquitin

Curated By

  • BioGRID