The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

DBN1  -  drebrin 1

Homo sapiens

Synonyms: D0S117E, Developmentally-regulated brain protein, Drebrin
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of DBN1


Psychiatry related information on DBN1

  • Immunocytochemical study demonstrated that widespread drebrin immunoreactivity was observed in hippocampal formations of control human brains, while Alzheimer's disease (AD) brains showed remarkable reductions in this immunoreactivity [4].
  • Drebrin has been reported to be engaged in dendritic-cytoskeleton modulation at synapses, and such a novel NXF signaling system on neural gene promoter may be a molecular target of the adverse effects of Sim2 in the mental retardation of Down's syndrome [5].
  • Alzheimer disease, the most common cause of dementia in the elderly, was associated with an additional 81% decrease in levels of drebrin, a protein regulating postsynaptic plasticity [6].

High impact information on DBN1

  • Identification of a novel basic helix-loop-helix-PAS factor, NXF, reveals a Sim2 competitive, positive regulatory role in dendritic-cytoskeleton modulator drebrin gene expression [5].
  • Expression of two developmentally regulated brain-specific proteins is correlated with late outgrowth of the pyramidal tract [7].
  • Drebrin and mammalian Abp1 (mAbp1) are actin-binding proteins found previously to bind to Golgi membranes in an ARF1-dependent manner in vitro [8].
  • The mechanisms for selective recruitment of mAbp1 and drebrin to Golgi membranes indicate how actin-based structures are able to select specific actin-binding proteins and, thus, carry out multiple different functions within cells [8].
  • Despite sharing homology through two shared actin binding domains, drebrin and mAbp1 have different subcellular localization and bind to distinct actin structures on the Golgi apparatus [8].

Biological context of DBN1


Anatomical context of DBN1

  • By contrast, the podocytes of rodent glomeruli appear to contain significant drebrin concentrations only during early developmental stages [12].
  • Cell biological and biochemical characterization of drebrin complexes in mesangial cells and podocytes of renal glomeruli [12].
  • Drebrin, located in the dendritic spines of the neuron, plays a role in the synaptic plasticity together with actin filaments [1].
  • By double-label fluorescence microscopy we have found drebrin enriched in actin microfilament bundles associated with plaques of cell-cell contact sites representing adhering junctions [13].
  • The occurrence and the possible functions of drebrin in non-neuronal cells, notably epithelial cells, and the significance of the existence of two different actin-anchoring junctional plaques is discussed [13].

Associations of DBN1 with chemical compounds


Regulatory relationships of DBN1


Other interactions of DBN1

  • Interactions of drebrin and gephyrin with profilin [16].
  • Decreased drebrin could not simply be due to cell loss (F-actin) or neuronal loss (comparable neuron-specific enolase between groups) [1].
  • Furthermore, decreased moesin is the second F-actin bundling protein, besides drebrin, that is manifold reduced in fetal DS brain [17].
  • We conclude that at the time point of about 19 weeks of gestation (early second trimester) no neuronal loss can be detected but drebrin, a marker for dendritic spines and synaptosomal associated proteins alpha SNAP and SNAP 25 were significantly reduced indicating impaired synaptogenesis [18].
  • In both the CD1 control animals and the S100B animals, the immunoreactivity of drebrin increased with age, however there were no significant between group differences [19].

Analytical, diagnostic and therapeutic context of DBN1


  1. Drebrin, a dendritic spine protein, is manifold decreased in brains of patients with Alzheimer's disease and Down syndrome. Shim, K.S., Lubec, G. Neurosci. Lett. (2002) [Pubmed]
  2. Dynamics of the actin-binding protein drebrin in motile cells and definition of a juxtanuclear drebrin-enriched zone. Peitsch, W.K., Bulkescher, J., Spring, H., Hofmann, I., Goerdt, S., Franke, W.W. Exp. Cell Res. (2006) [Pubmed]
  3. Drebrin, an actin-binding, cell-type characteristic protein: induction and localization in epithelial skin tumors and cultured keratinocytes. Peitsch, W.K., Hofmann, I., Bulkescher, J., Hergt, M., Spring, H., Bleyl, U., Goerdt, S., Franke, W.W. J. Invest. Dermatol. (2005) [Pubmed]
  4. Disappearance of actin-binding protein, drebrin, from hippocampal synapses in Alzheimer's disease. Harigaya, Y., Shoji, M., Shirao, T., Hirai, S. J. Neurosci. Res. (1996) [Pubmed]
  5. Identification of a novel basic helix-loop-helix-PAS factor, NXF, reveals a Sim2 competitive, positive regulatory role in dendritic-cytoskeleton modulator drebrin gene expression. Ooe, N., Saito, K., Mikami, N., Nakatuka, I., Kaneko, H. Mol. Cell. Biol. (2004) [Pubmed]
  6. Loss of proteins regulating synaptic plasticity in normal aging of the human brain and in Alzheimer disease. Hatanpää, K., Isaacs, K.R., Shirao, T., Brady, D.R., Rapoport, S.I. J. Neuropathol. Exp. Neurol. (1999) [Pubmed]
  7. Expression of two developmentally regulated brain-specific proteins is correlated with late outgrowth of the pyramidal tract. Kalil, K., Perdew, M. J. Neurosci. (1988) [Pubmed]
  8. The Actin-depolymerizing Factor Homology and Charged/Helical Domains of Drebrin and mAbp1 Direct Membrane Binding and Localization via Distinct Interactions with Actin. Xu, W., Stamnes, M. J. Biol. Chem. (2006) [Pubmed]
  9. Drebrin particles: components in the ensemble of proteins regulating actin dynamics of lamellipodia and filopodia. Peitsch, W.K., Hofmann, I., Prätzel, S., Grund, C., Kuhn, C., Moll, I., Langbein, L., Franke, W.W. Eur. J. Cell Biol. (2001) [Pubmed]
  10. Molecular cloning of cDNA encoding human drebrin E and chromosomal mapping of its gene. Toda, M., Shirao, T., Minoshima, S., Shimizu, N., Toya, S., Uyemura, K. Biochem. Biophys. Res. Commun. (1993) [Pubmed]
  11. Drebrin expression is increased in spinal motoneurons of rats after axotomy. Kobayashi, S., Shirao, T., Sasaki, T. Neurosci. Lett. (2001) [Pubmed]
  12. Cell biological and biochemical characterization of drebrin complexes in mesangial cells and podocytes of renal glomeruli. Peitsch, W.K., Hofmann, I., Endlich, N., Prätzel, S., Kuhn, C., Spring, H., Gröne, H.J., Kriz, W., Franke, W.W. J. Am. Soc. Nephrol. (2003) [Pubmed]
  13. Drebrin is a widespread actin-associating protein enriched at junctional plaques, defining a specific microfilament anchorage system in polar epithelial cells. Peitsch, W.K., Grund, C., Kuhn, C., Schnölzer, M., Spring, H., Schmelz, M., Franke, W.W. Eur. J. Cell Biol. (1999) [Pubmed]
  14. Activation of N-methyl-D-aspartate receptor induces a shift of drebrin distribution: disappearance from dendritic spines and appearance in dendritic shafts. Sekino, Y., Tanaka, S., Hanamura, K., Yamazaki, H., Sasagawa, Y., Xue, Y., Hayashi, K., Shirao, T. Mol. Cell. Neurosci. (2006) [Pubmed]
  15. Actin-binding protein, drebrin, accumulates in submembranous regions in parallel with neuronal differentiation. Asada, H., Uyemura, K., Shirao, T. J. Neurosci. Res. (1994) [Pubmed]
  16. Interactions of drebrin and gephyrin with profilin. Mammoto, A., Sasaki, T., Asakura, T., Hotta, I., Imamura, H., Takahashi, K., Matsuura, Y., Shirao, T., Takai, Y. Biochem. Biophys. Res. Commun. (1998) [Pubmed]
  17. Manifold reduction of moesin in fetal Down syndrome brain. Lubec, B., Weitzdoerfer, R., Fountoulakis, M. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  18. Fetal life in Down syndrome starts with normal neuronal density but impaired dendritic spines and synaptosomal structure. Weitzdoerfer, R., Dierssen, M., Fountoulakis, M., Lubec, G. J. Neural Transm. Suppl. (2001) [Pubmed]
  19. Expression levels of cytoskeletal proteins indicate pathological aging of S100B transgenic mice: an immunohistochemical study of MAP-2, drebrin and GAP-43. Shapiro, L.A., Whitaker-Azmitia, P.M. Brain Res. (2004) [Pubmed]
WikiGenes - Universities