The Groucho-associated Phosphatase PPM1B Displaces Pax Transactivation Domain Interacting Protein (PTIP) to Switch the Transcription Factor Pax2 from a Transcriptional Activator to a Repressor, Journal of Biological Chemistry, vol.122, issue.11, pp.7185-7194, 2015. ,
DOI : 10.1042/BJ20121113
Phosphorylation of p38 in HL60 Cells, Bioscience, Biotechnology, and Biochemistry, vol.74, issue.3, pp.548-552, 2010. ,
DOI : 10.1271/bbb.90735
Translation elongation factor EF-Tu is a target for Stp, a serine-threonine phosphatase involved in virulence of Listeria monocytogenes, Molecular Microbiology, vol.20, issue.Part 3, pp.383-396, 2005. ,
DOI : 10.1128/jb.174.3.947-952.1992
The Sir2 Family of Protein Deacetylases, Annual Review of Biochemistry, vol.73, issue.1, 2004. ,
DOI : 10.1146/annurev.biochem.73.011303.073651
, Annu. Rev. Biochem, vol.73, pp.417-435
Metabolic control of primed human pluripotent stem cell fate and function by the miR-200c???SIRT2 axis, Nature Cell Biology, vol.19, issue.5, pp.445-456, 2017. ,
DOI : 10.1016/j.stem.2009.05.005
Ppm1b negatively regulates necroptosis through dephosphorylating Rip3, Nature Cell Biology, vol.332, issue.4, pp.434-444, 2015. ,
DOI : 10.1128/IAI.73.6.3219-3227.2005
URL : http://europepmc.org/articles/pmc4523090?pdf=render
, , 2007.
, Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry, Proc. Natl. Acad
, , pp.2193-2198
Illuminating the landscape of host-pathogen interactions with the bacterium Listeria monocytogenes, Proc. Natl. Acad. Sci. USA, pp.19484-19491, 2011. ,
DOI : 10.1016/j.smim.2010.02.002
MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification, Nature Biotechnology, vol.7, issue.12, pp.1367-1372, 2008. ,
DOI : 10.1038/nprot.2007.261
Andromeda: A Peptide Search Engine Integrated into the MaxQuant Environment, Journal of Proteome Research, vol.10, issue.4, pp.1794-1805, 2011. ,
DOI : 10.1021/pr101065j
, , 2012.
, SIRT2 as a therapeutic target for age-related disorders, Front. Pharmacol, vol.3, p.82
A Role for SIRT2-Dependent Histone H3K18 Deacetylation in Bacterial Infection, Science, vol.13, issue.8, 2013. ,
DOI : 10.1038/nprot.2011.355
URL : https://hal.archives-ouvertes.fr/pasteur-00853764
Regulation of Sirtuin Function by Posttranslational Modifications, Frontiers in Pharmacology, vol.3, p.29, 2012. ,
DOI : 10.3389/fphar.2012.00029
URL : https://www.frontiersin.org/articles/10.3389/fphar.2012.00029/pdf
Emerging Role of Sirtuin 2 in the Regulation of Mammalian Metabolism, Trends in Pharmacological Sciences, vol.36, issue.11, pp.756-768, 2015. ,
DOI : 10.1016/j.tips.2015.08.001
PhosphoSitePlus, 2014: mutations, PTMs and recalibrations, Nucleic Acids Research, vol.22, issue.D1, pp.512-520, 2015. ,
DOI : 10.1093/bioinformatics/btl151
URL : https://academic.oup.com/nar/article-pdf/43/D1/D512/17437800/gku1267.pdf
Prognostic significance of sirtuin 2 protein nuclear localization in glioma: An immunohistochemical study, Oncology Reports, vol.28, issue.3, pp.923-930, 2012. ,
DOI : 10.3892/or.2012.1872
SIRT2, a tubulin deacetylase, acts to block the entry to chromosome condensation in response to mitotic stress, Oncogene, vol.37, issue.7, pp.945-957, 2007. ,
DOI : 10.1038/ng1538
Sirtuins in Epigenetic Regulation, Chemical Reviews, vol.115, issue.6, pp.2350-2375, 2015. ,
DOI : 10.1021/cr500457h
Mutational analysis of the domain structure of mouse protein phosphatase 2C??, Biochemical Journal, vol.332, issue.1, pp.243-250, 1998. ,
DOI : 10.1042/bj3320243
Role of Type 2C Protein Phosphatases in Growth Regulation and in Cellular Stress Signaling, Critical Reviews in Biochemistry and Molecular Biology, vol.6, issue.6, pp.437-461, 2007. ,
DOI : 10.1074/jbc.M203969200
PPM1A Regulates Antiviral Signaling by Antagonizing TBK1-Mediated STING Phosphorylation and Aggregation, PLOS Pathogens, vol.8, issue.3, 2015. ,
DOI : 10.1371/journal.ppat.1004783.s015
URL : https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.1004783&type=printable
PPM1A Functions as a Smad Phosphatase to Terminate TGF?? Signaling, Cell, vol.125, issue.5, pp.915-928, 2006. ,
DOI : 10.1016/j.cell.2006.03.044
PPM1A is a RelA phosphatase with tumor suppressor-like activity, Oncogene, vol.153, issue.22, pp.2918-2927, 2014. ,
DOI : 10.1007/s10585-006-9011-4
URL : http://europepmc.org/articles/pmc3897569?pdf=render
Cellular Histone Modification Patterns Predict Prognosis and Treatment Response in Resectable Pancreatic Adenocarcinoma: Results From RTOG 9704, Journal of Clinical Oncology, vol.28, issue.8, pp.1358-1365, 2010. ,
DOI : 10.1200/JCO.2009.24.5639
Class IIa histone deacetylases: regulating the regulators, Oncogene, vol.15, issue.37, pp.5450-5467, 2007. ,
DOI : 10.1073/pnas.250494697
Sirtuins in mammals: insights into their biological function, Biochemical Journal, vol.404, issue.1, pp.1-13, 2007. ,
DOI : 10.1042/BJ20070140
A SIRT1-LSD1 Corepressor Complex Regulates Notch Target Gene Expression and Development, Molecular Cell, vol.42, issue.5, pp.689-699, 2011. ,
DOI : 10.1016/j.molcel.2011.04.020
URL : https://doi.org/10.1016/j.molcel.2011.04.020
Mutations in SIRT2 deacetylase which regulate enzymatic activity but not its interaction with HDAC6 and tubulin, Molecular and Cellular Biochemistry, vol.25, issue.Pt 1, pp.221-230, 2007. ,
DOI : 10.1093/jb/mvh084
Sirtuins : Sir2-related NAD-dependent protein deacetylases, Genome Biology, vol.5, issue.5, p.224, 2004. ,
DOI : 10.1186/gb-2004-5-5-224
Interphase Nucleo-Cytoplasmic Shuttling and Localization of SIRT2 during Mitosis, PLoS ONE, vol.7, issue.8, p.784, 2007. ,
DOI : 10.1371/journal.pone.0000784.g006
URL : https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0000784&type=printable
Mitotic Regulation of SIRT2 by Cyclin-dependent Kinase 1-dependent Phosphorylation, Journal of Biological Chemistry, vol.36, issue.27, pp.19546-19555, 2007. ,
DOI : 10.1128/MCB.25.11.4541-4551.2005
, , 2003.
, The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase, Mol. Cell, vol.11, pp.437-444
, , 2004.
, Protein phosphatase 2Cbeta association with the IkappaB kinase complex is involved in regulating NF-kappaB activity, J. Biol. Chem, vol.279, pp.1739-1746
SIRT2 regulates NF-??B-dependent gene expression through deacetylation of p65 Lys310, Journal of Cell Science, vol.123, issue.24, pp.4251-4258, 2010. ,
DOI : 10.1242/jcs.073783
Mycobacterium tuberculosis exploits the PPM1A signaling pathway to block host macrophage apoptosis. Sci, 2017. ,
Global Levels of Histone Modifications Predict Prognosis in Different Cancers, The American Journal of Pathology, vol.174, issue.5, pp.1619-1628, 2009. ,
DOI : 10.2353/ajpath.2009.080874
The serine/threonine phosphatase PPM1B (PP2C??) selectively modulates PPAR?? activity, Biochemical Journal, vol.13, issue.1, pp.45-53, 2013. ,
DOI : 10.1074/jbc.272.36.22464
Crossing the Nuclear Envelope: Hierarchical Regulation of Nucleocytoplasmic Transport, Science, vol.257, issue.4, pp.1412-1416, 2007. ,
DOI : 10.1006/jmbi.1996.0206
SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis, Genes & Development, vol.20, issue.10, pp.1256-1261, 2006. ,
DOI : 10.1101/gad.1412706
Nucleocytoplasmic shuttling of signal transducers, Nature Reviews Molecular Cell Biology, vol.10, issue.3, pp.209-219, 2004. ,
DOI : 10.1006/scdb.1999.0302
Functional Interactions between Erythroid Kruppel-like Factor (EKLF/KLF1) and Protein Phosphatase PPM1B/PP2C??, Journal of Biological Chemistry, vol.31, issue.19, pp.15193-15204, 2012. ,
DOI : 10.1038/emboj.2011.450
URL : http://www.jbc.org/content/287/19/15193.full.pdf
Ran-Binding Protein 3 Phosphorylation Links the Ras and PI3-Kinase Pathways to Nucleocytoplasmic Transport, Molecular Cell, vol.29, issue.3, pp.362-375, 2008. ,
DOI : 10.1016/j.molcel.2007.12.024