BAIT

RAPH1

ALS2CR18, ALS2CR9, LPD, PREL-2, PREL2, RMO1, RalGDS/AF-6
Ras association (RalGDS/AF-6) and pleckstrin homology domains 1
GO Process (0)
GO Function (1)
GO Component (0)

Gene Ontology Molecular Function

Homo sapiens
PREY

ENAH

ENA, MENA, NDPP1, RP11-496N12.7
enabled homolog (Drosophila)
GO Process (2)
GO Function (2)
GO Component (5)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Homo sapiens

Affinity Capture-Western

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.

Publication

Lamellipodin, an Ena/VASP ligand, is implicated in the regulation of lamellipodial dynamics.

Krause M, Leslie JD, Stewart M, Lafuente EM, Valderrama F, Jagannathan R, Strasser GA, Rubinson DA, Liu H, Way M, Yaffe MB, Boussiotis VA, Gertler FB

Lamellipodial protrusion is regulated by Ena/VASP proteins. We identified Lamellipodin (Lpd) as an Ena/VASP binding protein. Both proteins colocalize at the tips of lamellipodia and filopodia. Lpd is recruited to EPEC and Vaccinia, pathogens that exploit the actin cytoskeleton for their own motility. Lpd contains a PH domain that binds specifically to PI(3,4)P2, an asymmetrically localized signal in chemotactic cells. ... [more]

Dev. Cell Oct. 01, 2004; 7(4);571-83 [Pubmed: 15469845]

Throughput

  • Low Throughput

Curated By

  • BioGRID