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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 (show MAPRE3 ELISA Kits). This pathway is regulated proximally by cyclin-dependent kinase 5 (show CDK5 ELISA Kits) 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 (show GJA1 ELISA Kits)) (together with Cx30 (show GJB6 ELISA Kits)) 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 (show CXCR4 ELISA Kits) and the actin cytoskeleton, drebrin regulates T cell activation. CD4 (show CD4 ELISA Kits)(+) 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 (show CA2 ELISA Kits)+) 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.
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 (show GRIN2B ELISA Kits)-containing NMDARs at the plasma membrane, while NR2A (show GRIN2A ELISA Kits)-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 (show CCR6 ELISA Kits) expression is induced during myoblast differentiation, in a p38 MAP kinase (show MAPK14 ELISA Kits)- and MyoD (show MYOD1 ELISA Kits)- 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.
Drebrin reduces SMC (show DYM ELISA Kits) activation through its interaction with the actin cytoskeleton but independently of its interaction with Homer (show HOMER1 ELISA Kits) scaffolds to prevent neointima formation.
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 (show GRIN1 ELISA Kits) signaling
Dbn1 regulates systemic anaphylaxis and IgE/Fcgr1-induced degranulation in mast cells by regulating actin reorganization and actin dynamics.
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