Drebrin at Junctional Plaques.
Adhesion, segregation, and cellular plasticity are regulated by actin filaments anchored at the plaques of adherens junctions, sites of mechanical stabilization, and interfaces of multiple signaling networks. Drebrins were originally identified in neuronal cells, but the isoform drebrin E was also detected at adherens junctions of a wide range of non-neuronal cells, including polarized epithelia, endothelia, and fibroblasts. Here the protein is enriched at actin filament bundles associated with junctional plaques. Polarized epithelial cells contain two types of actin-associated complexes, one comprising drebrin but not vinculin and the other involving vinculin, but not drebrin. At gap junctions drebrin interacts with connexin 43, stabilizes this protein at membranes, and links it to the actin cytoskeleton. In vivo drebrin is widespread in diverse non-neuronal tissues of epithelial, endothelial, and smooth muscle origin, but not ubiquitous. In intestinal cells it is involved in cell compaction, linking of actin filaments to microtubules and formation and stabilization of the terminal web. 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.
['Ludwig-Peitsch|Wiebke K|WK|']
D008841:Actin Cytoskeleton D022005:Adherens Junctions D000818:Animals D014408:Biomarkers, Tumor D018031:Connexin 43 D006801:Humans D008870:Microtubules D009369:Neoplasms D009479:Neuropeptides D060066:Protein Interaction Maps D016596:Vinculin
Drebrin Actin Adherens junction Vinculin Connexin 43 Microtubule Basal cell carcinoma