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FHOD1  -  formin homology 2 domain containing 1

Homo sapiens

Synonyms: FH1/FH2 domain-containing protein 1, FHOS, FHOS1, Formin homolog overexpressed in spleen 1, Formin homology 2 domain-containing protein 1
 
 
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Disease relevance of FHOD1

 

High impact information on FHOD1

 

Biological context of FHOD1

 

Anatomical context of FHOD1

 

Associations of FHOD1 with chemical compounds

  • These studies demonstrate that FHOD1 is a PKGI-interacting protein and substrate in VSMCs and show that cyclic GMP negatively regulates the FHOD1-PKGI interaction [3].
  • Moreover, FHOD1 overexpression did not alter integrin usage during adhesion or migration [1].
  • Overexpression of FHOS and FHOS78 resulted in enhanced insulin-stimulated glucose uptake in L6 cells to similar levels [9].
 

Co-localisations of FHOD1

 

Regulatory relationships of FHOD1

  • These data suggest that FHOS induces transcription from SREs by multiple pathways and that Rac1 may influence the course of some FHOS-induced signaling events [10].
  • Finally, using a run-on transcription assay we show that the C-terminal FHOD1 cleavage product has the ability to inhibit RNA polymerase I transcription when overexpressed in HeLa cells as shown by blockage of BrUTP incorporation [11].
  • These results define a role for endogenous FHOD1 in SH4 domain-induced blebbing and suggest that its activity is regulated by ROCK1 in a Src-dependent manner [12].
 

Other interactions of FHOD1

  • FHOD3 and FHOD1 showed 52.1% total-amino-acid identity [6].
  • The proline-rich FH1 domain of FHOD1 was sufficient to interact with the central portion of PRKCP1 and full-length cyclophilin B [5].
  • Intramolecular autoinhibitory interactions between the C terminus of FHOS and an N-terminal region partially overlapping the Rac1 interaction domain were also identified [10].
  • These findings suggest that FHOS mediates an interaction between GLUT4/IRAP-containing vesicles and the cytoskeleton and may participate in exocytosis and/or retention of this membrane compartment [9].
  • We show that formin homologue overexpressed in spleen (FHOS/FHOD1) binds the cytoplasmic domain of human CD21 through its C terminus [13].
 

Analytical, diagnostic and therapeutic context of FHOD1

  • Here, we report the detection of homotypic interactions of FHOD1 in the yeast two-hybrid system, by co-immunoprecipitation and co-localization in mammalian cells [14].
  • Immunofluorescence studies of human VSMC show that FHOD1 is cytoplasmic and is concentrated in the perinuclear region [3].
  • Using confocal microscopy, we further demonstrate that while full length FHOD1 is mostly cytoplasmic, the FHOD1 N-terminal cleavage product is diffusely localized throughout the cytoplasm and the nucleoplasm, whereas the C-terminal cleavage product is almost exclusively nuclear with some nucleolar localization [11].
  • Though widely expressed, FHOS RNA is most abundant in the littoral cell, a major constituent of the red pulp of human spleen believed to function in antigen filtration [13].

References

  1. The formin-homology-domain-containing protein FHOD1 enhances cell migration. Koka, S., Neudauer, C.L., Li, X., Lewis, R.E., McCarthy, J.B., Westendorf, J.J. J. Cell. Sci. (2003) [Pubmed]
  2. Biochemical characterization of the diaphanous autoregulatory interaction in the formin homology protein FHOD1. Schönichen, A., Alexander, M., Gasteier, J.E., Cuesta, F.E., Fackler, O.T., Geyer, M. J. Biol. Chem. (2006) [Pubmed]
  3. Formin homology domain protein (FHOD1) is a cyclic GMP-dependent protein kinase I-binding protein and substrate in vascular smooth muscle cells. Wang, Y., El-Zaru, M.R., Surks, H.K., Mendelsohn, M.E. J. Biol. Chem. (2004) [Pubmed]
  4. FHOD1 coordinates actin filament and microtubule alignment to mediate cell elongation. Gasteier, J.E., Schroeder, S., Muranyi, W., Madrid, R., Benichou, S., Fackler, O.T. Exp. Cell Res. (2005) [Pubmed]
  5. Identification of FHOD1-binding proteins and mechanisms of FHOD1-regulated actin dynamics. Westendorf, J.J., Koka, S. J. Cell. Biochem. (2004) [Pubmed]
  6. Identification and characterization of human FHOD3 gene in silico. Katoh, M., Katoh, M. Int. J. Mol. Med. (2004) [Pubmed]
  7. The mammalian formin FHOD1 interacts with the ERK MAP kinase pathway. Boehm, M.B., Milius, T.J., Zhou, Y., Westendorf, J.J., Koka, S. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  8. Activation of the Rac-binding partner FHOD1 induces actin stress fibers via a ROCK-dependent mechanism. Gasteier, J.E., Madrid, R., Krautkrämer, E., Schröder, S., Muranyi, W., Benichou, S., Fackler, O.T. J. Biol. Chem. (2003) [Pubmed]
  9. The Formin family protein, formin homolog overexpressed in spleen, interacts with the insulin-responsive aminopeptidase and profilin IIa. Tojo, H., Kaieda, I., Hattori, H., Katayama, N., Yoshimura, K., Kakimoto, S., Fujisawa, Y., Presman, E., Brooks, C.C., Pilch, P.F. Mol. Endocrinol. (2003) [Pubmed]
  10. The formin/diaphanous-related protein, FHOS, interacts with Rac1 and activates transcription from the serum response element. Westendorf, J.J. J. Biol. Chem. (2001) [Pubmed]
  11. Caspase-3 cleaves the formin-homology-domain-containing protein FHOD1 during apoptosis to generate a C-terminal fragment that is targeted to the nucleolus. M??nard, I., Gervais, F.G., Nicholson, D.W., Roy, S. Apoptosis (2006) [Pubmed]
  12. The Diaphanous-related Formin FHOD1 associates with ROCK1 and promotes Src-dependent plasma membrane blebbing. Hannemann, S., Madrid, R., Stastna, J., Kitzing, T., Gasteier, J., Schönichen, A., Bouchet, J., Jimenez, A., Geyer, M., Grosse, R., Benichou, S., Fackler, O.T. J. Biol. Chem. (2008) [Pubmed]
  13. EBV attachment stimulates FHOS/FHOD1 redistribution and co-aggregation with CD21: formin interactions with the cytoplasmic domain of human CD21. Gill, M.B., Roecklein-Canfield, J., Sage, D.R., Zambela-Soediono, M., Longtine, N., Uknis, M., Fingeroth, J.D. J. Cell. Sci. (2004) [Pubmed]
  14. Oligomerization of the diaphanous-related formin FHOD1 requires a coiled-coil motif critical for its cytoskeletal and transcriptional activities. Madrid, R., Gasteier, J.E., Bouchet, J., Schröder, S., Geyer, M., Benichou, S., Fackler, O.T. FEBS Lett. (2005) [Pubmed]
 
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