The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
TLS facilitates transport of mRNA encoding an actin-stabilizing protein to dendritic spines
Abstract
TLS (translocation in liposarcoma), an RNA-binding protein, was originally identified as a heterogeneous ribonuclear protein (hnRNP). Recently, we showed that TLS is localized in neuronal dendrites of mouse hippocampal neurons and is translocated to the spines, where local translation takes place, in an mGluR5 activation-dependent manner. However, the specific role of TLS has not been clarified. TLS-null neurons display abnormal spine morphology, suggesting that TLS-deficiency may impair activity-dependent actin reorganization in spines. To address this issue, we screened for mouse brain transcripts by their in vitro binding to TLS, and identified RNAs that associate with TLS, including mRNAs encoding actin-related proteins such as actin-stabilizing protein Nd1-L. Nd1-L transcripts were increased in the dendrites upon mGluR activation and significantly reduced in TLS-null dendrites. Overexpression of Nd1-L in mouse hippocampal neurons prevented damage to spine structure caused by actin destabilization. Our results demonstrate that TLS associates with mRNA encoding an actin-related protein and may be involved in actin reorganization in spines.
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Cites
Okamoto, K.-I., Nagai, T., Miyawaki, A., & Hayashi, Y. (2004) · Nature Neuroscience · doi:10.1038/nn1311 · Cited by 854
Actin-based plasticity in dendritic spines
Matus, A. (2000) · Science · doi:10.1126/science.290.5492.754 · Cited by 815
A Role of Actin Filament in Synaptic Transmission and Long-Term Potentiation
Kim, C.-H., & Lisman, J. E. (1999) · The Journal of Neuroscience · doi:10.1523/jneurosci.19-11-04314.1999 · Cited by 386
Krucker, T., Siggins, G. R., & Halpain, S. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.100139797 · Cited by 374
TLS (FUS) binds RNA in vivo and engages in nucleo-cytoplasmic shuttling
Zinszner, H., Sok, J., Immanuel, D., Yin, Y., & Ron, D. (1997) · Journal of Cell Science · doi:10.1242/jcs.110.15.1741 · Cited by 350
Hicks, G. G., Singh, N., Nashabi, A., Mai, S., Bozek, G., Klewes, L., Arapovic, D., White, E. K., Koury, M. J., Oltz, E. M., et al. (2000) · Nature Genetics · doi:10.1038/72842 · Cited by 299
Cited by
TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration
Lagier-Tourenne, C., Polymenidou, M., & Cleveland, D. W. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq137 · Cited by 1,021
ALS‐associated fused in sarcoma (FUS) mutations disrupt Transportin‐mediated nuclear import
Dormann, D., Rodde, R., Edbauer, D., Bentmann, E., Fischer, I., Hruscha, A., Than, M. E., Mackenzie, I. R. A., Capell, A., Schmid, B., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.143 · Cited by 836
A new subtype of frontotemporal lobar degeneration with FUS pathology
Neumann, M., Rademakers, R., Roeber, S., Baker, M., Kretzschmar, H. A., & Mackenzie, I. R. A. (2009) · Brain · doi:10.1093/brain/awp214 · Cited by 722
Dendritic mRNA: transport, translation and function
Bramham, C. R., & Wells, D. G. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2150 · Cited by 579
Protein aggregation in amyotrophic lateral sclerosis
Blokhuis, A. M., Groen, E. J. N., Koppers, M., van den Berg, L. H., & Pasterkamp, R. J. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1125-6 · Cited by 579
Metadata
- Authors
- Fujii, R., & Takumi, T.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2005-12-15
- Volume
- 118
- Issue
- 24
- Pages
- 5755-5765
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2085717785
- Cited by
- 247
- References
- 6
- FWCI
- 1.36
- Type
- journal article
- Language
- en
- Open access
- closed
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