Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Select your origin of interest
Human DBN1 Protein expressed in Wheat germ - ABIN1351156
Park, Yamada, Kojo, Sato, Onozuka, Yamamoto: Drebrin (developmentally regulated brain protein) is associated with axo-somatic synapses and neuronal gap junctions in rat mesencephalic trigeminal nucleus. in Neuroscience letters 2009
Drebrin may regulate activities of epigenetic reader ZMYND8 via its cytoplasmic sequestration.
Inhibition of cortactin or dynamin-2 abrogated the increased virus entry observed in DBN1-deficient cells, suggesting that DBN1 suppresses dynamin-mediated endocytosis via interaction with cortactin.
Lack of drebrin leads to the dysfunction of cell-cell communication, resulting in aberrant migration of metastatic cancer cells, aberrant synaptic function in dementia, and rupture of endothelial integrity.
One candidate pathway coupling actin filaments to microtubules consists of the actin filament-binding protein drebrin and the microtubule-binding +TIP protein EB3. This pathway is regulated proximally by cyclin-dependent kinase 5 phosphorylation of drebrin but the upstream elements in the pathway have yet to be identified.
These observations indicate that drebrin loss in dendritic spines occurs at the prodromal stage of Alzheimer's disease (AD), before the density and morphology of dendritic spines change. Quantitation of drebrin may be a possible tool for diagnosing the prodromal stage of AD, before dementia development in AD.
Taking into account that connexin-43 (Cx43) (together with Cx30) is heavily expressed in astrocytes and that drebrin supports cell-cell contacts, the understanding of details of how brain cells live and die reveals molecular pathology involved in neurodegeneration, Alzheimer's disease (AD), other cognitive disorders, and aging
further studies on drebrin and its binding proteins will be of great importance to elucidate the pathologies of various diseases and may contribute to their medical treatment and diagnostics development.
through its interaction with CXCR4 and the actin cytoskeleton, drebrin regulates T cell activation. CD4(+) T cells are one of the main targets for the human immunodeficiency virus (HIV)-1.
Our work has shown that the immunosuppressant compound BTP2, which blocks Ca(2+) influx into cells, interacts with the actin-reorganizing protein, drebrin. Here we review the role of drebrin in the regulation of calcium signaling, with a focus on immune cells.
Upregulation of drebrin was noted in several types of cancers, e.g., basal cell carcinomas for which it may serve as marker, liver metastases of colon carcinomas, and bladder cancer, suggesting that it is involved in regulating actin dynamics during tumor development, progression, and metastasis.
drebrin has to be added to the list of actin-binding proteins regulating actin dynamics of mesangial cell processes and foot processes of podocytes. It will be important to determine its role in hereditary and acquired glomerulopathies.
these results contribute to the current understanding of cell-cell junction regulation, introducing a new function of drebrin as a stabilizer of endothelial integrity.
Cancer cell motility and invasion are crucial elements in the metastatic cascade and involve dramatic changes in cellular morphology that are associated with dynamic remodelling of the cytoskeleton. Interestingly, it now appears that drebrin could deliver this role during cancer development.
Drebrin reduces SMC activation through its interaction with the actin cytoskeleton but independently of its interaction with Homer scaffolds to prevent neointima formation.
Exploring the relationship between drebrin and cognitive function may provide insight into the early prevention of cognitive impairment and in the diagnosis and treatment of Alzheimer's disease.
Drebrin is critical for progranulin-dependent activation of the Akt and MAPK pathways and modulates motility, invasion and anchorage-independent growth in bladder neoplasms.
The study compared the proteome profiles of the human colon adenocarcinoma cell line HCT-116 with its metastatic derivative E1. DBN1 was found to be overexpressed in E1 as compared to HCT-116 cells.
In basal cell carcinoma tissues, intense and homogeneous drebrin expression was observed mainly at tumor cell-cell boundaries. In contrast, drebrin was stained only weakly and non-homogeneously in trichoblastoma and trichoepthelioma tissue samples.
Rab8a and Drebrin E act as key proteins in the regulation of apical trafficking in intestinal epithelial cells.
drebrin has a role in HIV infection by modulating viral entry, mainly through the control of actin cytoskeleton polymerization in response to HIV-1
Functional perturbations of drebrin demonstrate that proximal leading process microtubule-actomyosin coupling steers the direction of centrosome and somal migration, as well as the switch from tangential to radial migration.
Hippocampal Drebrin protein expression levels in adult APP/PS1 mice decline with age. Behavioral data demonstrated that cognitive and probe activities decline with age. A correlation analysis showed that the expression level of the Drebrin protein significantly correlatives with behavioral performance in Alzheimer's disease mice.
In subventricular zone of Dbn1-null mice number of neuroblasts and cell proliferation decreased, although cell death remained unchanged.
Drebrin A is highly enriched in dendritic spines, but its effects on actin morphology, dynamics, and interplay with other actin regulators are yet to be clarified. Here we review recent advances in understanding drebrin effects on actin morphology and dynamics.
Drebrin A can be found co-clustering with NR2B-containing NMDARs at the plasma membrane, while NR2A-containing NMDARs co-traffic into the spine cytoplasm but do not co-cluster at the plasma membrane.
these findings suggest that during cell migration drebrin is involved in retraction processes but not in lamellipodia formation. The novel, sizable juxtanuclear drebrin-enriched zone remains to be characterized in detail with respect to its molecular assembly and functions.
bn1 expression is induced during myoblast differentiation, in a p38 MAP kinase- and MyoD- dependent manner. RNAi-mediated depletion of drebrin, or treatment with a chemical drebrin inhibitor, resulted in a similar phenotype in myoblasts: defective differentiation, with low levels of early and late differentiation markers and inefficient production of myofibers.
Study determines the specific roles of drebrin in the regulation of the axonal cytoskeleton, and provides evidence that drebrin contributes to the coordination of the actin and microtubule cytoskeleton during the initial stages of axon branching.
Data suggest further studies to elucidate the effect of drebrin (Dbn) on the development and progression of Alzheimer's disease (AD).
Study demonstrated that isoform conversion of drebrin is critical, and that drebrin A is indispensable for adult hippocampal synaptic plasticity and hippocampus-dependent fear learning; the phenotype of drebrin A knockout mice suggests functional differences between drebrin A and drebrin E
These findings provide unprecedented experimental support for a role of drebrin in the regulation of memory-related synaptic plasticity and neurotransmitter receptor signaling
Dbn1 regulates systemic anaphylaxis and IgE/Fcgr1-induced degranulation in mast cells by regulating actin reorganization and actin dynamics.
SAHA likely inhibits ADDL-induced drebrin loss from dendritic spines by stabilizing drebrin in these structures, rather than by increasing drebrin clusters or dendritic protrusions
These results suggest that Cdk5-p35 regulates neuronal migration through phosphorylation of drebrin in growth cone processes.
Double knockout Psen1Psen2 leads to a decrease in immunoreactivity for drebrin A at both synaptic and nonsynaptic areas of CA1 hippocampus.
The density of drebrin-positive glutamatergic synapses formed on GABAergic neurons is lower than those on glutamatergic neurons.
These results suggest that the actin-binding domain of drebrin is centered on actin subdomain 2 and may adopt a folded conformation upon binding to F-actin.
Drebrin A plays an indispensable role in some processes of generating fear learning and memory.
The protein encoded by this gene is a cytoplasmic actin-binding protein thought to play a role in the process of neuronal growth. It is a member of the drebrin family of proteins that are developmentally regulated in the brain. A decrease in the amount of this protein in the brain has been implicated as a possible contributing factor in the pathogenesis of memory disturbance in Alzheimer's disease. At least two alternative splice variants encoding different protein isoforms have been described for this gene.
developmentally-regulated brain protein
, drebrin E
, drebrin E2
, drebrin A
, developmentally regulated brain protein
, drebrin 1