Mutations in SIRT2 deacetylase which regulate enzymatic activity but not its interaction with HDAC6 and tubulin

Molecular and Cellular Biochemistry

Volumn 303, Issue 1-2, 2007, Pages 221-230

  Nahhas, Fatimah ^a   Dryden, Sylvia C ^a   Abrams, Judith ^b   Tainsky, Michael A ^a  

^a WAYNE STATE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b KARMANOS CANCER INSTITUTE   (United States)

Author keywords

Deacetylation; HDAC; Microtubules; Mitotic checkpoint; Phosphorylation; Sir2

Indexed keywords

ALANINE; HISTONE DEACETYLASE 6; NICOTINAMIDE ADENINE DINUCLEOTIDE; SERINE; SILENT INFORMATION REGULATOR PROTEIN 2; THREONINE; TUBULIN; TYROSINE;

AMINO ACID SUBSTITUTION; ARTICLE; CELL CYCLE; CELL SURVIVAL; CONTROLLED STUDY; CYTOPLASM; ENZYME ACTIVITY; ENZYME BINDING; ENZYME REGULATION; GENE MUTATION; GENE OVEREXPRESSION; GENETIC CONSERVATION; HUMAN; HUMAN CELL; MICROTUBULE; MITOSIS; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN INTERACTION; PROTEIN PHOSPHORYLATION; WILD TYPE;

ACETYLATION; AMINO ACID SEQUENCE; ANTINEOPLASTIC AGENTS; HISTONE DEACETYLASES; HUMANS; MICROTUBULES; MITOSIS; MOLECULAR SEQUENCE DATA; MUTATION; NOCODAZOLE; PHOSPHORYLATION; PROTEIN BINDING; SEQUENCE HOMOLOGY, AMINO ACID; SIRTUINS; TUBULIN;

EID: 34547920351     PISSN: 03008177     EISSN: 15734919     Source Type: Journal    
DOI: 10.1007/s11010-007-9478-6     Document Type: Article

References (53)

1. Imai S, Armstrong CM, Kaeberlein M, Guarente L (2000) Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403:795-800
2. Landry J, Sutton A, Tafrov ST, Heller RC et al (2000) The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases. Proc Natl Acad Sci U S A 97:5807-5811
3. Aparicio OM, Billington BL, Gottschling DE (1991) Modifiers of position effect are shared between telomeric and silent mating-type loci in S. cerevisiae. Cell 66:1279-1287
4. Gottlieb S, Esposito RE (1989) A new role for a yeast transcriptional silencer gene, SIR2, in regulation of recombination in ribosomal DNA. Cell 56:771-776
5. Smith JS, Boeke JD (1997) An unusual form of transcriptional silencing in yeast ribosomal DNA. Genes Dev 11:241-254
6. Braunstein M, Rose AB, Holmes SG et al (1993) Transcriptional silencing in yeast is associated with reduced nucleosome acetylation. Genes Dev 7:592-604
7. Kaeberlein M, McVey M, Guarente L (1999) The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms. Genes Dev 13:2570-2580
8. Sinclair DA, Guarente L (1997) Extrachromosomal rDNA circles - a cause of aging in yeast. Cell 91:1033-1042
9. Tissenbaum HA, Guarente L (2001) Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans. Nature 410:227-230
10. Lin SJ, Defossez PA, Guarente L (2000) Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae. Science 289:2126-2128
11. Davenport RJ (2004) UnSIRtainty principle. Conflicting results underscore questions about how calorie restriction activates yeast longevity enzyme. Sci Aging Knowledge Environ 2004:nF5
12. Anderson RM, Latorre-Esteves M, Neves AR et al (2003) Yeast life-span extension by calorie restriction is independent of NAD fluctuation. Science 302:2124-2126
13. Anderson RM, Bitterman KJ, Wood JG et al (2003) Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae. Nature 423:181-185
14. Lin SJ, Ford E, Haigis M et al (2004) Calorie restriction extends yeast life span by lowering the level of NADH. Genes Dev 18:12-16
15. Sauve AA, Moir RD, Schramm VL et al (2005) Chemical activation of Sir2-dependent silencing by relief of nicotinamide inhibition. Mol Cell 17:595-601
16. Frye RA (1999) Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity. Biochem Biophys Res Commun 260:273-279
17. Tanny JC, Dowd GJ, Huang J et al (1999) An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing. Cell 99:735-745
18. Tanny JC, Moazed D (2001) Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2: Evidence for acetyl transfer from substrate to an NAD breakdown product. Proc Natl Acad Sci U S A 98:415-420
19. Tanner KG, Landry J, Sternglanz R et al (2000) Silent information regulator 2 family of NAD-dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose. Proc Natl Acad Sci U S A 97:14178-14182
20. Sherman JM, Stone EM, Freeman-Cook LL et al (1999) The conserved core of a human SIR2 homologue functions in yeast silencing. Mol Biol Cell 10:3045-3059
21. Lamming DW, Latorre-Esteves M, Medvedik O et al (2005) HST2 mediates SIR2-independent life-span extension by calorie restriction. Science 310:1124-1125
22. Frye RA (2000) Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem Biophys Res Commun 273:793-798
23. North BJ, Verdin E (2004) Sirtuins: Sir2-related NAD-dependent protein deacetylases. Genome Biol 5:224
24. Dryden SC, Nahhas FA, Nowak JE (2003) Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle. Mol Cell Biol 23:3173-3185
25. Afshar G, Murnane JP (1999) Characterization of a human gene with sequence homology to Saccharomyces cerevisiae SIR2. Gene 234:161-168
26. Yang YH, Chen YH, Zhang CY et al (2000) Cloning and characterization of two mouse genes with homology to the yeast Sir2 gene. Genomics 69:355-369
27. Bae NS, Swanson MJ, Vassilev A et al (2004) Human histone deacetylase SIRT2 interacts with the homeobox transcription factor HOXA10. J Biochem (Tokyo) 135:695-700
28. North BJ, Marshall BL, Borra MT et al (2003) The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol Cell 11:437-444
29. Hiratsuka M, Inoue T, Toda T et al (2003) Proteomics-based identification of differentially expressed genes in human gliomas: down-regulation of SIRT2 gene. Biochem Biophys Res Commun 309:558-566
30. Gelfand VI, Bershadsky AD (1991) Microtubule dynamics: Mechanism, regulation, and function. Annu Rev Cell Biol 7:93-116
31. Wolf KW, Spanel-Borowski K (1995) Acetylation of alpha-tubilin in different bovine cell types: Implications for microtubule dynamics in interphase and mitosis. Cell Biol Int 19:43-52
32. Westermann S, Weber K (2003) Post-translational modifications regulate microtubule function. Nat Rev Mol Cell Biol 4:938-947
33. Draberova E, Viklicky V, Draber P (2000) Exposure of lumenal microtubule sites after mild fixation. Eur J Cell Biol 79:982-985
34. Cambray-Deakin MA, Burgoyne RD (1987) Acetylated and detyrosinated alpha-tubulins are co-localized in stable microtubules in rat meningeal fibroblasts. Cell Motil Cytoskeleton 8:284-291
35. Webster DR, Borisy GG (1989) Microtubules are acetylated in domains that turn over slowly. J Cell Sci 92(Pt 1):57-65
36. Smith JS, Tachibana I, Pohl U et al (2000) A transcript map of the chromosome 19q-arm glioma tumor suppressor region. Genomics 64:44-50
37. Matsuyama A, Shimazu T, Sumida Y et al (2002) In vivo destabilization of dynamic microtubules by HDAC6-mediated deacetylation. Embo J 21:6820-6831
38. Hubbert C, Guardiola A, Shao R et al (2002) HDAC6 is a microtubule-associated deacetylase. Nature 417:455-458
39. Satokata I, Benson G, Maas R (1995) Sexually dimorphic sterility phenotypes in Hoxa10-deficient mice. Nature 374:460-463
40. Moretti P, Freeman K, Coodly L et al (1994) Evidence that a complex of SIR proteins interacts with the silencer and telomere-binding protein RAP1. Genes Dev 8:2257-2269
41. Seigneurin-Berny D, Verdel A, Curtet S et al (2001) Identification of components of the murine histone deacetylase 6 complex: Link between acetylation and ubiquitination signaling pathways. Mol Cell Biol 21: 8035-8044
42. Hook SS, Orian A, Cowley SM et al (2002) Histone deacetylase 6 binds polyubiquitin through its zinc finger (PAZ domain) and copurifies with deubiquitinating enzymes. Proc Natl Acad Sci U S A 99:13425-13430
43. Brush MH, Guardiola A, Connor JH et al (2004) Deactylase inhibitors disrupt cellular complexes containing protein phosphatases and deacetylases. J Biol Chem 279:7685-7691
44. Zhang Y, Li N, Caron C et al (2003) HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo. Embo J 22:1168-1179
45. Westendorf JJ, Zaidi SK, Cascino JE et al (2002) Runx2 (Cbfa1, AML-3) interacts with histone deacetylase 6 and represses the p21(CIP1/WAF1) promoter. Mol Cell Biol 22:7982-7992
46. Blander G, Olejnik J, Krzymanska-Olejnik E et al (2005) SIRT1 shows no substrate specificity in vitro. J Biol Chem 280:9780-9785
47. Juan LJ, Shia WJ, Chen MH et al (2000) Histone deacetylases specifically down-regulate p53-dependent gene activation. J Biol Chem 275:20436-20443
48. Blom N, Gammeltoft S, Brunak S (1999) Sequence and structure-based prediction of eukaryotic protein phosphorylation sites. J Mol Biol 294:1351-1362
49. Vaquero A, Scher MB, Lee DH et al (2006) SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis. Genes Dev 20:1256-1261
50. Finnin MS, Donigian JR, Pavletich NP (2001) Structure of the histone deacetylase SIRT2. Nat Struct Biol 8:621-625
51. Avalos JL, Boeke JD, Wolberger C (2004) Structural basis for the mechanism and regulation of Sir2 enzymes. Mol Cell 13:639-648
52. Avalos JL, Bever KM, Wolberger C (2005) Mechanism of sirtuin inhibition by nicotinamide: Altering the NAD(+) cosubstrate specificity of a Sir2 enzyme. Mol Cell 17:855-868
53. Cho HP, Liu Y, Gomez M et al (2005) The dual-specificity phosphatase CDC14B bundles and stabilizes microtubules. Mol Cell Biol 25: 4541-4551