The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
Histone deacetylase SIRT1 modulates neuronal differentiation by its nuclear translocation
Open accessAbstract
Neural precursor cells (NPCs) differentiate into neurons, astrocytes, and oligodendrocytes in response to intrinsic and extrinsic changes. Notch signals maintain undifferentiated NPCs, but the mechanisms underlying the neuronal differentiation are largely unknown. We show that SIRT1, an NAD + -dependent histone deacetylase, modulates neuronal differentiation. SIRT1 was found in the cytoplasm of embryonic and adult NPCs and was transiently localized in the nucleus in response to differentiation stimulus. SIRT1 started to translocate into the nucleus within 10 min after the transfer of NPCs into differentiation conditions, stayed in the nucleus, and then gradually retranslocated to the cytoplasm after several hours. The number of neurospheres that generated Tuj1 + neurons was significantly decreased by pharmacological inhibitors of SIRT1, dominant-negative SIRT1 and SIRT1-siRNA , whereas overexpression of SIRT1, but not that of cytoplasm-localized mutant SIRT1, enhanced neuronal differentiation and decreased Hes1 expression. Expression of SIRT1-siRNA impaired neuronal differentiation and migration of NPCs into the cortical plate in the embryonic brain. Nuclear receptor corepressor (N-CoR), which has been reported to bind SIRT1, promoted neuronal differentiation and synergistically increased the number of Tuj1 + neurons with SIRT1, and both bound the Hes1 promoter region in differentiating NPCs. Hes1 transactivation by Notch1 was inhibited by SIRT1 and/or N-CoR. Our study indicated that SIRT1 is a player of repressing Notch1-Hes1 signaling pathway, and its transient translocation into the nucleus may have a role in the differentiation of NPCs.
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Cites
Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
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Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1
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Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-γ
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Haigis, M. C., & Guarente, L. P. (2006) · Genes & Development · doi:10.1101/gad.1467506 · Cited by 1,295
Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice
Cheng, H.-L., Mostoslavsky, R., Saito, S., Manis, J. P., Gu, Y., Patel, P., Bronson, R., Appella, E., Alt, F. W., & Chua, K. F. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1934713100 · Cited by 1,095
Mechanisms of Asymmetric Stem Cell Division
Knoblich, J. A. (2008) · Cell · doi:10.1016/j.cell.2008.02.007 · Cited by 1,015
Notch signalling in vertebrate neural development
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Nucleocytoplasmic Shuttling of the NAD+-dependent Histone Deacetylase SIRT1
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Self-citationHsieh, J., Nakashima, K., Kuwabara, T., Mejia, E., & Gage, F. H. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407643101 · Cited by 719
Cited by
Mammalian Sirtuins: Biological Insights and Disease Relevance
Haigis, M. C., & Sinclair, D. A. (2010) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev.pathol.4.110807.092250 · Cited by 2,085
Acetylation of Tau Inhibits Its Degradation and Contributes to Tauopathy
Min, S.-W., Cho, S.-H., Zhou, Y., Schroeder, S., Haroutunian, V., Seeley, W. W., Huang, E. J., Shen, Y., Masliah, E., Mukherjee, C., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.08.044 · Cited by 949
SIRT1 Is Essential for Normal Cognitive Function and Synaptic Plasticity
Michan, S., Li, Y., Chou, M. M.-H., Parrella, E., Ge, H., Long, J. M., Allard, J. S., Lewis, K., Miller, M., Xu, W., et al. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.0027-10.2010 · Cited by 541
Redox regulation of SIRT1 in inflammation and cellular senescence
Hwang, J.-W., Yao, H., Caito, S., Sundar, I. K., & Rahman, I. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.03.015 · Cited by 503
Tanno, M., Kuno, A., Yano, T., Miura, T., Hisahara, S., Ishikawa, S., Shimamoto, K., & Horio, Y. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.090266 · Cited by 358
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Metadata
- Authors
- Hisahara, S., Chiba, S., Matsumoto, H., Tanno, M., Yagi, H., Shimohama, S., Sato, M., & Horio, Y.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2008-10-07
- Volume
- 105
- Issue
- 40
- Pages
- 15599-15604
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1989164058
- Cited by
- 279
- References
- 33
- FWCI
- 4.36
- Type
- journal article
- Language
- en
- Open access
- green
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