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

Reconstituted Complex

An interaction is detected between purified proteins in vitro.

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

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
VASP RAPH1
Proximity Label-MS
Proximity Label-MS

An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods.

High20.02BioGRID
3010387

Curated By

  • BioGRID