BAIT

FHOD1

FHOS
formin homology 2 domain containing 1
GO Process (2)
GO Function (2)
GO Component (4)
Homo sapiens

Co-localization

Interaction inferred from two proteins that co-localize in the cell by indirect immunofluorescence only when in addition, if one gene is deleted, the other protein becomes mis-localized. Also includes co-dependent association of proteins with promoter DNA in chromatin immunoprecipitation experiments.

Publication

The human formin FHOD1 contains a bipartite structure of FH3 and GTPase-binding domains required for activation.

Schulte A, Stolp B, Schoenichen A, Pylypenko O, Rak A, Fackler OT, Geyer M

Formins induce the nucleation and polymerization of unbranched actin filaments. They share three homology domains required for profilin binding, actin polymerization, and regulation. Diaphanous-related formins (DRFs) are activated by GTPases of the Rho/Rac family, whose interaction with the N-terminal formin domain is thought to displace a C-terminal Diaphanous-autoregulatory domain (DAD). We have determined the structure of the N-terminal domains of ... [more]

Structure Sep. 10, 2008; 16(9);1313-23 [Pubmed: 18786395]

Throughput

  • Low Throughput

Additional Notes

  • Source of RAC2 not clear

Curated By

  • BioGRID