Functional domains of SP110 that modulate its transcriptional regulatory function and cellular translocation

Journal of Biomedical Science

Volumn 25, Issue 1, 2018, Pages

  Leu, Jia Shiun ^a   Chang, So Yi ^b   Mu, Chia Yu ^b   Chen, Mei Ling ^b   Yan, Bo Shiun ^b  

^a NATIONAL YANG MING UNIVERSITY   (Taiwan)

^b NATIONAL TAIWAN UNIVERSITY   (Taiwan)

Author keywords

Cellular translocation; Functional domain; Nuclear localization signal; Nucleolar localization signal; Transcriptional regulation

Indexed keywords

AMINO ACID; GREEN FLUORESCENT PROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; ISOPROTEIN; NUCLEAR PROTEIN; PROTEIN P50; SP110 PROTEIN; TUMOR NECROSIS FACTOR; UNCLASSIFIED DRUG; MINOR HISTOCOMPATIBILITY ANTIGEN; SP110 PROTEIN, HUMAN;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL COMPARTMENTALIZATION; CELL FUNCTION; CELL TRANSPORT; CELLULAR DISTRIBUTION; CONFOCAL MICROSCOPY; CONTROLLED STUDY; DELETION MUTANT; DOWN REGULATION; EMBRYO; HEK293T CELL LINE; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; LUCIFERASE ASSAY; MUTATIONAL ANALYSIS; NCI-H1299 CELL LINE; NUCLEOLAR LOCALIZATION SIGNAL; NUCLEOLUS; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN SUBUNIT; PROTEIN TRANSPORT; TRANSCRIPTION REGULATION; WESTERN BLOTTING; GENE EXPRESSION REGULATION; GENETIC TRANSCRIPTION; GENETICS; HEK293 CELL LINE; IMMUNOLOGY; METABOLISM; TUMOR CELL LINE;

CELL LINE, TUMOR; GENE EXPRESSION REGULATION; HEK293 CELLS; HUMANS; MINOR HISTOCOMPATIBILITY ANTIGENS; NF-KAPPA B; NUCLEAR PROTEINS; PROTEIN DOMAINS; PROTEIN ISOFORMS; TRANSCRIPTION, GENETIC;

EID: 85045143322     PISSN: 10217770     EISSN: 14230127     Source Type: Journal    
DOI: 10.1186/s12929-018-0434-4     Document Type: Article

References (63)

1. Tuberculosis Fact sheet N°104. www.who.int/mediacentre/factsheets/fs104/en. Accessed Jan 2018.
2. Hill AVS. Aspects of genetic susceptibility to human infectious diseases. Annu Rev Genet. 2006;40:469-86.
3. Casanova JL, Abel L. Genetic dissection of immunity to mycobacteria: the human model. Annu Rev Immunol. 2002;20:581-620.
4. Lynch CJ, Pierce-Chase CH, Dubos R. A genetic study of susceptibility to experimental tuberculosis in mice infected with mammalian tubercle bacilli. J Exp Med. 1965;121:1051-70.
5. Hill AV. The genomics and genetics of human infectious disease susceptibility. Annu Rev Genomics Hum Genet. 2001;2:373-400.
6. Apt A, Kramnik I. Man and mouse TB: contradictions and solutions. Tuberculosis (Edinb). 2009;89:195-8.
7. Fortin A, Abel L, Casanova JL, Gros P. Host genetics of mycobacterial diseases in mice and men: forward genetic studies of BCG-osis and tuberculosis. Annu Rev Genomics Hum Genet. 2007;8:163-92.
8. Pan H, Yan BS, Rojas M, Shebzukhov YV, Zhou H, Kobzik L, Higgins DE, Daly MJ, Bloom BR, Kramnik I. Ipr1 gene mediates innate immunity to tuberculosis. Nature. 2005;434:767-72.
9. Kramnik I. Genetic dissection of host resistance to Mycobacterium tuberculosis: the sst1 locus and the Ipr1 gene. Curr Top Microbiol Immunol. 2008;321:123-48.
10. Kadereit S, Gewert DR, Galabru J, Hovanessian AG, Meurs EF. Molecular cloning of two new interferon-induced, highly related nuclear phosphoproteins. J Biol Chem. 1993;268:24432-41.
11. Tosh K, Campbell SJ, Fielding K, Sillah J, Bah B, Gustafson P, Manneh K, Lisse I, Sirugo G, Bennett S, et al. Variants in the SP110 gene are associated with genetic susceptibility to tuberculosis in West Africa. Proc Natl Acad Sci U S A. 2006;103:10364-8.
12. Babb C, Keet EH, van Helden PD, Hoal EG. SP110 polymorphisms are not associated with pulmonary tuberculosis in a south African population. Hum Genet. 2007;121:521-2.
13. Thye T, Browne EN, Chinbuah MA, Gyapong J, Osei I, Owusu-Dabo E, Niemann S, Rusch-Gerdes S, Horstmann RD, Meyer CG. No associations of human pulmonary tuberculosis with Sp110 variants. J Med Genet. 2006;43:e32.
14. Szeszko JS, Healy B, Stevens H, Balabanova Y, Drobniewski F, Todd JA, Nejentsev S. Resequencing and association analysis of the SP110 gene in adult pulmonary tuberculosis. Hum Genet. 2007;121:155-60.
15. Fox GJ, Sy DN, Nhung NV, Yu B, Ellis MK, Van Hung N, Cuong NK, Thi Lien L, Marks GB, Saunders BM, et al. Polymorphisms of SP110 are associated with both pulmonary and extra-pulmonary tuberculosis among the Vietnamese. PLoS One. 2014;9:e99496.
16. Leu JS, Chen ML, Chang SY, Yu SL, Lin CW, Wang H, Chen WC, Chang CH, Wang JY, Lee LN, et al. SP110b controls host immunity and susceptibility to tuberculosis. Am J Respir Crit Care Med. 2017;195:369-82.
17. Abhimanyu JP, Jain A, Arora K, Bose M. Genetic association study suggests a role for SP110 variants in lymph node tuberculosis but not pulmonary tuberculosis in north Indians. Hum Immunol. 2011;72:576-80.
18. Png E, Alisjahbana B, Sahiratmadja E, Marzuki S, Nelwan R, Adnan I, van de Vosse E, Hibberd M, van Crevel R, Ottenhoff THM, et al. Polymorphisms in SP110 are not associated with pulmonary tuberculosis in Indonesians. Infect Genet Evol. 2012;12:1319-23.
19. Roscioli T, Cliffe ST, Bloch DB, Bell CG, Mullan G, Taylor PJ, Sarris M, Wang J, Donald JA, Kirk EP, et al. Mutations in the gene encoding the PML nuclear body protein Sp110 are associated with immunodeficiency and hepatic veno-occlusive disease. Nat Genet. 2006;38:620-2.
20. Cliffe ST, Wong M, Taylor PJ, Ruga E, Wilcken B, Lindeman R, Buckley MF, Roscioli T. The first prenatal diagnosis for veno-occlusive disease and immunodeficiency syndrome, an autosomal recessive condition associated with mutations in SP110. Prenat Diagn. 2007;27:674-6.
21. Cliffe ST, Bloch DB, Suryani S, Kamsteeg EJ, Avery DT, Palendira U, Church JA, Wainstein BK, Trizzino A, Lefranc G, et al. Clinical, molecular, and cellular immunologic findings in patients with SP110-associated veno-occlusive disease with immunodeficiency syndrome. J Allergy Clin Immun. 2012;130:735-+.
22. Watashi K, Hijikata M, Tagawa A, Doi T, Marusawa H, Shimotohno K. Modulation of retinoid signaling by a cytoplasmic viral protein via sequestration of Sp110b, a potent transcriptional corepressor of retinoic acid receptor, from the nucleus. Mol Cell Biol. 2003;23:7498-509.
23. Nicewonger J, Suck G, Bloch D, Swaminathan S. Epstein-Barr virus (EBV) SM protein induces and recruits cellular Sp110b to stabilize mRNAs and enhance EBV lytic gene expression. J Virol. 2004;78:9412-22.
24. Bottomley MJ, Collard MW, Huggenvik JI, Liu Z, Gibson TJ, Sattler M. The SAND domain structure defines a novel DNA-binding fold in transcriptional regulation. Nat Struct Biol. 2001;8:626-33.
25. Heery DM, Kalkhoven E, Hoare S, Parker MG. A signature motif in transcriptional co-activators mediates binding to nuclear receptor. Nature. 1997;387:733-6.
26. Horlein AJ, Naar AM, Heinzel T, Torchia J, Gloss B, Kurokawa R, Ryan A, Kamei Y, Soderstrom M, Glass CK, et al. Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor. Nature. 1995;377:397-404.
27. Plevin MJ, Mills MM, Ikura M. The LxxLL motif: a multifunctional binding sequence in transcriptional regulation. Trends Biochem Sci. 2005;30:66-9.
28. Bloch DB, Nakajima A, Gulick T, Chiche JD, Orth D, de La Monte SM, Bloch KD. Sp110 localizes to the PML-Sp100 nuclear body and may function as a nuclear hormone receptor transcriptional coactivator. Mol Cell Biol. 2000;20:6138-46.
29. Pitkanen J, Peterson P. Autoimmune regulator: from loss of function to autoimmunity. Genes Immun. 2003;4:12-21.
30. Bernardi R, Pandolfi PP. Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies. Nat Rev Mol Cell Bio. 2007;8:1006-16.
31. Lallemand-Breitenbach V, de The H. PML nuclear bodies. Cold Spring Harb Perspect Biol. 2010;2:a000661.
32. Dinkel H, Van Roey K, Michael S, Kumar M, Uyar B, Altenberg B, Milchevskaya V, Schneider M, Kuhn H, Behrendt A, et al. ELM 2016-data update and new functionality of the eukaryotic linear motif resource. Nucleic Acids Res. 2016;44:D294-300.
33. Kalderon D, Roberts BL, Richardson WD, Smith AE. A short amino-acid sequence able to specify nuclear location. Cell. 1984;39:499-509.
34. Kalderon D, Richardson WD, Markham AF, Smith AE. Sequence requirements for nuclear location of simian Virus-40 large-T-antigen. Nature. 1984;311:33-8.
35. Robbins J, Dilworth SM, Laskey RA, Dingwall C. 2 interdependent basic domains in Nucleoplasmin nuclear targeting sequence - identification of a class of bipartite nuclear targeting sequence. Cell. 1991;64:615-23.
36. Fiol CJ, Mahrenholz AM, Wang Y, Roeske RW, Roach PJ. Formation of protein-kinase recognition sites by covalent modification of the substrate - molecular mechanism for the synergistic action of casein kinase-ii and glycogen-synthase Kinase-3. J Biol Chem. 1987;262:14042-8.
37. Cohen P, Frame S. The renaissance of GSK3. Nat Rev Mol Cell Bio. 2001;2:769-76.
38. Jope RS, Johnson GVW. The glamour and gloom of glycogen synthase kinase-3. Trends Biochem Sci. 2004;29:95-102.
39. Vallabhapurapu S, Karin M. Regulation and function of NF-kappaB transcription factors in the immune system. Ann Rev Immunol. 2009;27:693-733.
40. Oeckinghaus A, Hayden MS, Ghosh S. Crosstalk in NF-kappaB signaling pathways. Nat Immunol. 2011;12:695-708.
41. Smale ST. Hierarchies of NF-kappaB target-gene regulation. Nat Immunol. 2011;12:689-94.
42. Saccani S, Pantano S, Natoli G. Modulation of NF-kappaB activity by exchange of dimers. Mol Cell. 2003;11:1563-74.
43. Wang VY, Huang W, Asagiri M, Spann N, Hoffmann A, Glass C, Ghosh G. The transcriptional specificity of NF-kappaB dimers is coded within the kappaB DNA response elements. Cell Rep. 2012;2:824-39.
44. Baeuerle PA, Henkel T. Function and activation of NF-kappa B in the immune system. Annu Rev Immunol. 1994;12:141-79.
45. Lin R, Gewert D, Hiscott J. Differential transcriptional activation in vitro by NF-kappa B/Rel proteins. J Biol Chem. 1995;270:3123-31.
46. Katto J, Engel N, Abbas W, Herbein G, Mahlknecht U. Transcription factor NF kappa B regulates the expression of the histone deacetylase SIRT1. Clin Epigenetics. 2013;5
47. Sheppard KA, Rose DW, Haque ZK, Kurokawa R, McInerney E, Westin S, Thanos D, Rosenfeld MG, Glass CK, Collins T. Transcriptional activation by NF-kappaB requires multiple coactivators. Mol Cell Biol. 1999;19:6367-78.
48. Hoffmann A, Baltimore D. Circuitry of nuclear factor kappaB signaling. Immunol Rev. 2006;210:171-86.
49. Schindler U, Beckmann H, Cashmore AR. HAT3.1, a novel Arabidopsis homeodomain protein containing a conserved cysteine-rich region. Plant J. 1993;4:137-50.
50. Mellor J. It takes a PHD to read the histone code. Cell. 2006;126:22-4.
51. Tamkun JW, Deuring R, Scott MP, Kissinger M, Pattatucci AM, Kaufman TC, Kennison JA. brahma: a regulator of Drosophila homeotic genes structurally related to the yeast transcriptional activator SNF2/SWI2. Cell. 1992;68:561-72.
52. Sanchez R, Zhou MM. The role of human bromodomains in chromatin biology and gene transcription. Curr Opin Drug Discov Devel. 2009;12:659-65.
53. Tsai WW, Wang Z, Yiu TT, Akdemir KC, Xia W, Winter S, Tsai CY, Shi X, Schwarzer D, Plunkett W, et al. TRIM24 links a non-canonical histone signature to breast cancer. Nature. 2010;468:927-32.
54. Xi Q, Wang Z, Zaromytidou AI, Zhang XH, Chow-Tsang LF, Liu JX, Kim H, Barlas A, Manova-Todorova K, Kaartinen V, et al. A poised chromatin platform for TGF-beta access to master regulators. Cell. 2011;147:1511-24.
55. Plotnikov AN, Yang S, Zhou TJ, Rusinova E, Frasca A, Zhou MM. Structural insights into acetylated-histone H4 recognition by the Bromodomain-PHD finger module of human transcriptional coactivator CBP. Structure. 2014;22:353-60.
56. Jang HD, Yoon K, Shin YJ, Kim J, Lee SY. PIAS3 suppresses NF-kappaB-mediated transcription by interacting with the p65/RelA subunit. J Biol Chem. 2004;279:24873-80.
57. Sternsdorf T, Jensen K, Reich B, Will H. The nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers. J Biol Chem. 1999;274:12555-66.
58. Wasylyk C, Schlumberger SE, Criqui-Filipe P, Wasylyk B. Sp100 interacts with ETS-1 and stimulates its transcriptional activity. Mol Cell Biol. 2002;22:2687-702.
59. Seeler JS, Marchio A, Sitterlin D, Transy C, Dejean A. Interaction of SP100 with HP1 proteins: a link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartment. Proc Natl Acad Sci U S A. 1998;95:7316-21.
60. Moller A, Sirma H, Hofmann TG, Staege H, Gresko E, Ludi KS, Klimczak E, Droge W, Will H, Schmitz ML. Sp100 is important for the stimulatory effect of homeodomain-interacting protein kinase-2 on p53-dependent gene expression. Oncogene. 2003;22:8731-7.
61. Pederson T. The nucleolus. Cold Spring Harb Perspect Biol. 2011;3
62. Lohrum MAE, Ashcroft M, Kubbutat MHG, Vousden KH. Identification of a cryptic nucleolar-localization signal in MDM2. Nat Cell Biol. 2000;2:179-81.
63. Weber JD, Taylor LJ, Roussel MF, Sherr CJ, Bar-Sagi D. Nucleolar Arf sequesters Mdm2 and activates p53. Nat Cell Biol. 1999;1:20-6.