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Actin‐Binding protein, drebrin, accumulates in submembranous regions in parallel with neuronal differentiation
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AbstractDrebrins are developmentally regulated actin‐binding proteins. In this study, we analyzed subcellular distribution of drebrin E in neuroblastoma cells (SHSY5Y) in culture, especially in terms of its relationship to actin filaments. In undifferentiated cells, drebrin E was scattered as flocculus small dots along the stress fibers and also accumulated at adhesion plaques. In parallel with the neuronal differentiation following retinoic acid treatment, drebrin E was accumulated, accompanying filamentous (F) actin, in the submembranous cortical cytoplasm. Similar submembranous localization of drebrins was observed in primary cultured neurons. In the presence of drebrin E F‐actin was more stable against cytochalasin D than F‐actin lacking drebrin E. These results suggest that drebrin E plays a role in neuronal morphological differentiation by changing its subcellular localization with stabilized F‐actin. © 1994 Wiley‐Liss, Inc.
Title: Actin‐Binding protein, drebrin, accumulates in submembranous regions in parallel with neuronal differentiation
Description:
AbstractDrebrins are developmentally regulated actin‐binding proteins.
In this study, we analyzed subcellular distribution of drebrin E in neuroblastoma cells (SHSY5Y) in culture, especially in terms of its relationship to actin filaments.
In undifferentiated cells, drebrin E was scattered as flocculus small dots along the stress fibers and also accumulated at adhesion plaques.
In parallel with the neuronal differentiation following retinoic acid treatment, drebrin E was accumulated, accompanying filamentous (F) actin, in the submembranous cortical cytoplasm.
Similar submembranous localization of drebrins was observed in primary cultured neurons.
In the presence of drebrin E F‐actin was more stable against cytochalasin D than F‐actin lacking drebrin E.
These results suggest that drebrin E plays a role in neuronal morphological differentiation by changing its subcellular localization with stabilized F‐actin.
© 1994 Wiley‐Liss, Inc.
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