QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

HOME  |   SEARCH  |   ARCHIVE  |   SUBSCRIBE  |   CONTACT  |   HELP

The Journal of Neuroscience, March 7, 2007, 27(10):2606-2616; doi:10.1523/JNEUROSCI.4181-06.2007

This Article Full Text Full Text (PDF) Submit an eLetter Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Web of Science (16) Citing Articles via Google Scholar Google Scholar Articles by Li, W. Articles by Liang, F. Search for Related Content PubMed PubMed Citation Articles by Li, W. Articles by Liang, F.

 Previous Article  |  Next Article 

Development/Plasticity/Repair
Sirtuin 2, a Mammalian Homolog of Yeast Silent Information Regulator-2 Longevity Regulator, Is an Oligodendroglial Protein That Decelerates Cell Differentiation through Deacetylating -Tubulin

Wenbo Li, Bin Zhang, Junhong Tang, Qiong Cao, Yajun Wu, Chun Wu, Jing Guo, Eng-Ang Ling, and Fengyi Liang

Department of Anatomy, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117597

Correspondence should be addressed to Dr. Fengyi Liang, Department of Anatomy, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117597. Email: antlfy{at}nus.edu.sg

Silent information regulator-2 (SIR2) proteins regulate lifespan of diverse organisms, but their distribution and roles in the CNS remain unclear. Here, we show that sirtuin 2 (SIRT2), a mammalian SIR2 homolog, is an oligodendroglial cytoplasmic protein and localized to the outer and juxtanodal loops in the myelin sheath. Among cytoplasmic proteins of OLN-93 oligodendrocytes, -tubulin was the main substrate of SIRT2 deacetylase. In cultured primary oligodendrocyte precursors (OLPs), SIRT2 emergence accompanied elevated -tubulin acetylation and OLP differentiation into the prematurity stage. Small interfering RNA knockdown of SIRT2 increased the -tubulin acetylation, myelin basic protein expression, and cell arbor complexity of OLPs. SIRT2 overexpression had the opposite effects, and counteracted the cell arborization-promoting effect of overexpressed juxtanodin. SIRT2 mutation concomitantly reduced its deacetylase activity and its impeding effect on OLP arborization. These results demonstrated a counterbalancing role of SIRT2 against a facilitatory effect of tubulin acetylation on oligodendroglial differentiation. Selective SIRT2 availability to oligodendroglia may have important implications for myelinogenesis, myelin–axon interaction, and brain aging.

Key words: sirtuin 2; tubulin acetylation/deacetylation; oligodendrocyte differentiation; myelination; RNA interference; cytoskeleton

---

Received Sept. 25, 2006; revised Dec. 27, 2006; accepted Jan. 31, 2007.

Correspondence should be addressed to Dr. Fengyi Liang, Department of Anatomy, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117597. Email: antlfy{at}nus.edu.sg

This article has been cited by other articles:

				R. Pescini Gobert, L. Joubert, M.-L. Curchod, C. Salvat, I. Foucault, C. Jorand-Lebrun, M. Lamarine, H. Peixoto, C. Vignaud, C. Fremaux, et al. Convergent Functional Genomics of Oligodendrocyte Differentiation Identifies Multiple Autoinhibitory Signaling Circuits Mol. Cell. Biol., March 15, 2009; 29(6): 1538 - 1553. [Abstract] [Full Text] [PDF]

				I. A. Meijer, A. A. Simoes-Lopes, S. Laurent, T. Katz, J. St-Onge, D. J. Verlaan, N. Dupre, M. Thibault, J. Mathurin, J.-P. Bouchard, et al. A Novel Duplication Confirms the Involvement of 5q23.2 in Autosomal Dominant Leukodystrophy Arch Neurol, November 1, 2008; 65(11): 1496 - 1501. [Abstract] [Full Text] [PDF]

				N. Ohkawa, S. Sugisaki, E. Tokunaga, K. Fujitani, T. Hayasaka, M. Setou, and K. Inokuchi N-acetyltransferase ARD1-NAT1 regulates neuronal dendritic development. Genes Cells, November 1, 2008; 13(11): 1171 - 1183. [Abstract] [Full Text] [PDF]

				R. Pandithage, R. Lilischkis, K. Harting, A. Wolf, B. Jedamzik, J. Luscher-Firzlaff, J. Vervoorts, E. Lasonder, E. Kremmer, B. Knoll, et al. The regulation of SIRT2 function by cyclin-dependent kinases affects cell motility J. Cell Biol., March 5, 2008; 180(5): 915 - 929. [Abstract] [Full Text] [PDF]

				H. B. Werner, K. Kuhlmann, S. Shen, M. Uecker, A. Schardt, K. Dimova, F. Orfaniotou, A. Dhaunchak, B. G. Brinkmann, W. Mobius, et al. Proteolipid Protein Is Required for Transport of Sirtuin 2 into CNS Myelin J. Neurosci., July 18, 2007; 27(29): 7717 - 7730. [Abstract] [Full Text] [PDF]

Home  |   Search  |   Archive  |   Subscribe  |   Contact  |   Help