Phosphorylation Regulates SIRT1 Function
作者： Tsutomu Sasaki , Bernhard Maier , Katarzyna D. Koclega , Maksymilian Chruszcz , Wendy Gluba
DOI: 10.1371/JOURNAL.PONE.0004020
关键词: Cell cycle 、 Cyclin-dependent kinase 、 Deacetylase activity 、 CDC2 Protein Kinase 、 Kinase 、 Cyclin-dependent kinase 1 、 Sirtuin 1 、 Molecular biology 、 Cell biology 、 Sirtuin 、 Biology 、 General Biochemistry, Genetics and Molecular Biology 、 General Agricultural and Biological Sciences 、 General Medicine
摘要: … SIRT1 on cell proliferation, we transfected Sirt1-deficient mouse cells with expression vectors for normal FLAG-SIRT1 (WT) or FLAG-SIRT1 … We found that the proliferation defects of Sirt1 …
harvard.edu
elsevier.com
paperity.org
researchgate.net 参考文章(46)
Erich A. Nigg, Mitotic kinases as regulators of cell division and its checkpoints Nature Reviews Molecular Cell Biology. ,vol. 2, pp. 21- 32 ,(2001) , 10.1038/35048096
J. Landry, A. Sutton, S. T. Tafrov, R. C. Heller, J. Stebbins, L. Pillus, R. Sternglanz, The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 97, pp. 5807- 5811 ,(2000) , 10.1073/PNAS.110148297
Heidi A. Tissenbaum, Leonard Guarente, Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans Nature. ,vol. 410, pp. 227- 230 ,(2001) , 10.1038/35065638
Ala Berdichevsky, Mohan Viswanathan, H. Robert Horvitz, Leonard Guarente, C. elegans SIR-2.1 Interacts with 14-3-3 Proteins to Activate DAF-16 and Extend Life Span Cell. ,vol. 125, pp. 1165- 1177 ,(2006) , 10.1016/J.CELL.2006.04.036
B. Rogina, S. L. Helfand, Sir2 mediates longevity in the fly through a pathway related to calorie restriction Proceedings of the National Academy of Sciences of the United States of America. ,vol. 101, pp. 15998- 16003 ,(2004) , 10.1073/PNAS.0404184101
Zhou Songyang, Steven Blechner, Nicole Hoagland, Merl F. Hoekstra, Helen Piwnica-Worms, Lewis C. Cantley, Use of an oriented peptide library to determine the optimal substrates of protein kinases Current Biology. ,vol. 4, pp. 973- 982 ,(1994) , 10.1016/S0960-9822(00)00221-9
Tarek Abbas, Sudhakar Jha, Nicholas E. Sherman, Anindya Dutta, Autocatalytic phosphorylation of CDK2 at the activating Thr160. Cell Cycle. ,vol. 6, pp. 843- 852 ,(2007) , 10.4161/CC.6.7.4000
Mary Kay H. Pflum, Jeffrey K. Tong, William S. Lane, Stuart L. Schreiber, Histone Deacetylase 1 Phosphorylation Promotes Enzymatic Activity and Complex Formation Journal of Biological Chemistry. ,vol. 276, pp. 47733- 47741 ,(2001) , 10.1074/JBC.M105590200
J. S. Smith, C. B. Brachmann, I. Celic, M. A. Kenna, S. Muhammad, V. J. Starai, J. L. Avalos, J. C. Escalante-Semerena, C. Grubmeyer, C. Wolberger, J. D. Boeke, A phylogenetically conserved NAD+-dependent protein deacetylase activity in the Sir2 protein family. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 97, pp. 6658- 6663 ,(2000) , 10.1073/PNAS.97.12.6658
William Humphrey, Andrew Dalke, Klaus Schulten, VMD: Visual molecular dynamics Journal of Molecular Graphics. ,vol. 14, pp. 33- 38 ,(1996) , 10.1016/0263-7855(96)00018-5