Role of monoubiquitylation on the control of IκBα degradation and NF-κB activity

PLoS ONE

Volumn 6, Issue 10, 2011, Pages

  da Silva Ferrada, Elisa ^a   Torres Ramos, Mónica ^a,d   Aillet, Fabienne ^a   Campagna, Michela ^b   Matute, Carlos ^c   Rivas, Carmen ^b   Rodríguez, Manuel S ^a,c   Lang, Valérie ^a  

^a INSTITUTO DE SALUD CARLOS III   (Spain)

^b UNIVERSIDAD AUTÓNOMA DE MADRID   (Spain)

^c UNIVERSITY OF THE BASQUE COUNTRY UPV EHU   (Spain)

^d NATIONAL INSTITUTE OF NEUROLOGY AND NEUROSURGERY   (Mexico)

Author keywords

[No Author keywords available]

Indexed keywords

HYBRID PROTEIN; I KAPPA B ALPHA; I KAPPA B KINASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LYSINE; SERINE; TUMOR NECROSIS FACTOR ALPHA; UBIQUITIN; UBIQUITINATED PROTEIN; I KAPPA B; NF KAPPAB INHIBITOR ALPHA; NF-KAPPAB INHIBITOR ALPHA;

ANIMAL CELL; ANIMAL EXPERIMENT; ARTICLE; CONTROLLED STUDY; DENATURING GRADIENT GEL ELECTROPHORESIS; GEL MOBILITY SHIFT ASSAY; HALF LIFE TIME; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DNA BINDING; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; RAT; SIGNAL TRANSDUCTION; SUMOYLATION; UBIQUITINATION; WESTERN BLOTTING; ANIMAL; ANTIBODY SPECIFICITY; BIOLOGICAL MODEL; CELL LINE; DRUG EFFECT; MALE; METABOLISM; MOUSE; PHOSPHORYLATION; PROTEIN STABILITY; SPRAGUE DAWLEY RAT; TIME;

RATTUS;

ANIMALS; CELL LINE; HALF-LIFE; HUMANS; I-KAPPA B PROTEINS; MALE; MICE; MODELS, BIOLOGICAL; NF-KAPPA B; ORGAN SPECIFICITY; PHOSPHORYLATION; PROTEIN STABILITY; PROTEOLYSIS; RATS; RATS, SPRAGUE-DAWLEY; RECOMBINANT FUSION PROTEINS; TIME FACTORS; TUMOR NECROSIS FACTOR-ALPHA; UBIQUITINATION; UBIQUITINS;

EID: 80053985081     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0025397     Document Type: Article

References (24)

1. Hayden MS, Ghosh S, (2008) Shared principles in NF-kappaB signaling. Cell 132: 344-362.
2. Li H, Lin X, (2008) Positive and negative signaling components involved in TNFalpha-induced NF-kappaB activation. Cytokine 41: 1-8.
3. Mabb AM, Miyamoto S, (2007) SUMO and NF-kappaB ties. Cell Mol Life Sci 64: 1979-1996.
4. Lang V, Rodriguez MS, (2008) Innate link between NF-kappaB activity and ubiquitin-like modifiers. Biochem Soc Trans 36: 853-857.
5. Liu S, Chen ZJ, (2010) Expanding role of ubiquitination in NF-kappaB signaling. Cell Res.
6. Krappmann D, Scheidereit C, (2005) A pervasive role of ubiquitin conjugation in activation and termination of IkappaB kinase pathways. EMBO Rep 6: 321-326.
7. Chen ZJ, (2005) Ubiquitin signalling in the NF-kappaB pathway. Nat Cell Biol 7: 758-765.
8. Baldi L, Brown K, Franzoso G, Siebenlist U, (1996) Critical role for lysines 21 and 22 in signal-induced, ubiquitin-mediated proteolysis of I kappa B-alpha. J Biol Chem 271: 376-379.
9. Karin M, Ben-Neriah Y, (2000) Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity. Annu Rev Immunol 18: 621-663.
10. Desterro JM, Rodriguez MS, Hay RT, (1998) SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation. Mol Cell 2: 233-239.
11. Ghosh S, Baltimore D, (1990) Activation in vitro of NF-kappa B by phosphorylation of its inhibitor I kappa B. Nature 344: 678-682.
12. Arenzana-Seisdedos F, Thompson J, Rodriguez MS, Bachelerie F, Thomas D, et al. (1995) Inducible nuclear expression of newly synthesized I kappa B alpha negatively regulates DNA-binding and transcriptional activities of NF-kappa B. Mol Cell Biol 15: 2689-2696.
13. Rodriguez MS, Thompson J, Hay RT, Dargemont C, (1999) Nuclear retention of IkappaBalpha protects it from signal-induced degradation and inhibits nuclear factor kappaB transcriptional activation. J Biol Chem 274: 9108-9115.
14. Hjerpe R, Aillet F, Lopitz-Otsoa F, Lang V, England P, et al. (2009) Efficient protection and isolation of ubiquitylated proteins using tandem ubiquitin-binding entities. EMBO Rep 10: 1250-1258.
15. Carter S, Vousden KH, (2008) p53-Ubl fusions as models of ubiquitination, sumoylation and neddylation of p53. Cell Cycle 7: 2519-2528.
16. Scherer DC, Brockman JA, Chen Z, Maniatis T, Ballard DW, (1995) Signal-induced degradation of I kappa B alpha requires site-specific ubiquitination. Proc Natl Acad Sci U S A 92: 11259-11263.
17. Rodriguez MS, Wright J, Thompson J, Thomas D, Baleux F, et al. (1996) Identification of lysine residues required for signal-induced ubiquitination and degradation of I kappa B-alpha in vivo. Oncogene 12: 2425-2435.
18. Salmena L, Pandolfi PP, (2007) Changing venues for tumour suppression: balancing destruction and localization by monoubiquitylation. Nat Rev Cancer 7: 409-413.
19. Mathes E, Wang L, Komives E, Ghosh G, (2010) Flexible regions within I{kappa}B{alpha} create the ubiquitin-independent degradation signal. J Biol Chem 285: 32927-32936.
20. Hoeller D, Hecker CM, Wagner S, Rogov V, Dotsch V, et al. (2007) E3-independent monoubiquitination of ubiquitin-binding proteins. Mol Cell 26: 891-898.
21. Isasa M, Katz EJ, Kim W, Yugo V, Gonzalez S, et al. (2010) Monoubiquitination of RPN10 regulates substrate recruitment to the proteasome. Mol Cell 38: 733-745.
22. Nelson DE, Ihekwaba AE, Elliott M, Johnson JR, Gibney CA, et al. (2004) Oscillations in NF-kappaB signaling control the dynamics of gene expression. Science 306: 704-708.
23. Hoffmann A, Levchenko A, Scott ML, Baltimore D, (2002) The IkappaB-NF-kappaB signaling module: temporal control and selective gene activation. Science 298: 1241-1245.
24. Tian B, Nowak DE, Brasier AR, (2005) A TNF-induced gene expression program under oscillatory NF-kappaB control. BMC Genomics 6: 137.