BAIT

CDC3

septin CDC3, L000000243, YLR314C
Component of the septin ring that is required for cytokinesis; septins are GTP-binding proteins that assemble with other septins into rod-like complexes that can associate with other rods to form filament polymers; septin rings at the mother-bud neck act as scaffolds for recruiting factors needed for cell division and as barriers to prevent diffusion of specific proteins between mother and daughter cells
Saccharomyces cerevisiae (S288c)
PREY

LNP1

YHR192W
Lunapark family member involved in ER network formation; localizes to ER junctions and this localization is regulated by the yeast atlastin ortholog Sey1p; interacts with the reticulon protein Rtn1p; induced in response to the DNA-damaging agent MMS
GO Process (1)
GO Function (0)
GO Component (2)

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)

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.

Publication

Coiled-Coil Networking Shapes Cell Molecular Machinery.

Wang Y, Zhang X, Zhang H, Lu Y, Huang H, Dong X, Chen J, Dong J, Yang X, Hang H, Jiang T

The highly abundant alpha-helical coiled-coil motif not only mediates crucial protein-protein interactions in the cell, but is also an attractive scaffold in synthetic biology and material science and a potential target for disease intervention. Therefore, a systematic understanding of the coiled-coil interactions at the organismal level would help unravel the full spectrum of the biological function of this interaction motif ... [more]

Mol. Biol. Cell Aug. 08, 2012; 0(0); [Pubmed: 22875988]

Throughput

  • High Throughput

Additional Notes

  • Interaction between cloned coiled-coil domains

Curated By

  • BioGRID