Present addresses: Children's Hospital Los Angeles, 4650 Sunset Blvd, Los Angeles, CA 90027, USA (Y.O.); Institute of Cell Biology and Neuroscience ‘Prof E. De Robertis’, Department of Histology and Cell Biology, School of Medicine, University of Buenos Aires, Buenos Aires, Argentina 1121 (F.C.); Korea Research Institute of Bioscience and Biotechnology, Daejon 305-333, South Korea (C.-S.L.); Department of Neurology, Georg-August-University Göttingen, 37075 Göttingen, Germany (C.N.); Department of Neurology, Northwestern University Medical School, Chicago, IL 60611, USA (J.Y.W.).
Transient decrease in F-actin may be necessary for translocation of proteins into dendritic spines
Article first published online: 5 DEC 2005
European Journal of Neuroscience
Volume 22, Issue 12, pages 2995–3005, December 2005
How to Cite
Ouyang, Y., Wong, M., Capani, F., Rensing, N., Lee, C.-S., Liu, Q., Neusch, C., Martone, M. E., Wu, J. Y., Yamada, K., Ellisman, M. H. and Choi, D. W. (2005), Transient decrease in F-actin may be necessary for translocation of proteins into dendritic spines. European Journal of Neuroscience, 22: 2995–3005. doi: 10.1111/j.1460-9568.2005.04521.x
- Issue published online: 5 DEC 2005
- Article first published online: 5 DEC 2005
- Received 31 January 2005, revised 25 October 2005, accepted 29 October 2005
- dendritic spine;
- information storage;
- protein translocation;
- synaptic specificity
It remains poorly understood as to how newly synthesized proteins that are required to act at specific synapses are translocated into only selected subsets of potentiated dendritic spines. Here, we report that F-actin, a major component of the skeletal structure of dendritic spines, may contribute to the regulation of synaptic specificity of protein translocation. We found that the stabilization of F-actin blocked the translocation of GFP-CaMKII and inhibited the diffusion of 3-kDa dextran into spines (in 2–3 weeks cultures). Neuronal activation in hippocampal slices and cultured neurons led to an increase in the activation (decrease in the phosphorylation) of the actin depolymerization factor, cofilin, and a decrease in F-actin. Furthermore, the induction of long-term potentiation by tetanic stimulation induced local transient depolymerization of F-actin both in vivo and in hippocampal slices (8–10 weeks), and this local F-actin depolymerization was blocked by APV, a N-methyl-d-aspartate (NMDA) receptor antagonist. These results suggest that F-actin may play a role in synaptic specificity by allowing protein translocation into only potentiated spines, gated through its depolymerization, which is probably triggered by the activation of NMDA receptors.