NFKB1

NFKB1
Subunidad p105 del factor nuclear NF-kappa-B
Protein NFKB1 PDB 1bfs.png
Estructura tridimensional de la proteína NFKB1.
HUGO 7794
Símbolo NFKB1
Símbolos alt. DKFZp686C01211; EBP-1; KBF1; MGC54151; NF-kappa-B; NFKB-p105; NFKB-p50
Datos genéticos
Locus Cr. 4 q24
Bases de datos
Entrez 4790
OMIM 164011
PDB 1bfs
RefSeq NP_003989
UniProt P19838

La subunidad p105 del factor nuclear NF-kappa-B (NFKB1) es una proteína codificada en humanos por el gen NFKB1.[1]

Este gen codifica una proteína de 105 kDa que puede sufrir procesamiento co-traduccional el proteasoma 26S para generar una proteína de 50 kDa. La proteína de 105 kDa es un inhibidor Rel específico de transcripción y la de 50 kDa es una subunidad de unión a ADN del complejo proteico NF-κB. NF-κB es un factor de transcripción que es activado por diversos estímulos intra- y extracelulares, tales como citoquinas, radicales libres de oxígeno, radiación UV y productos bacterianos y virales. El complejo NF-κB activado es traslocado al núcleo celular y estimula la expresión de genes implicados en una amplia variedad de procesos biológicos; en torno a 200 genes conocidos son dianas de NF-κB en varios tipos de células diferentes, bajo condiciones específicas. Una activación inapropiada de NF-κB se ha asociado con un cierto número de enfermedades inflamatorias, mientras que una inhibición persistente de NF-κB conduce a un desarrollo incorrecto de células del sistema inmune o un retraso en el crecimiento celular.[2]

Interacciones

La proteína NFKB1 ha demostrado ser capaz de interaccionar con:

Referencias

  1. ↑ Meyer R, Hatada EN, Hohmann HP, Haiker M, Bartsch C, Rothlisberger U, Lahm HW, Schlaeger EJ, van Loon AP, Scheidereit C (Mar 1991). «Cloning of the DNA-binding subunit of human nuclear factor kappa B: the level of its mRNA is strongly regulated by phorbol ester or tumor necrosis factor alpha». Proc Natl Acad Sci U S A 88 (3):  pp. 966–70. PMID 1992489. 
  2. ↑ «Entrez Gene: NF-κB nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 (p105)».
  3. ↑ Li, Z; Nabel G J (Oct. 1997). «A new member of the I kappaB protein family, I kappaB epsilon, inhibits RelA (p65)-mediated NF-kappaB transcription». Mol. Cell. Biol. (UNITED STATES) 17 (10):  pp. 6184–90. ISSN 0270-7306. PMID 9315679. 
  4. ↑ Heissmeyer, V; Krappmann D, Hatada E N, Scheidereit C (Feb. 2001). «Shared pathways of IkappaB kinase-induced SCF(betaTrCP)-mediated ubiquitination and degradation for the NF-kappaB precursor p105 and IkappaBalpha». Mol. Cell. Biol. (United States) 21 (4):  pp. 1024–35. doi:10.1128/MCB.21.4.1024-1035.2001. ISSN 0270-7306. PMID 11158290. 
  5. ↑ a b Heissmeyer, V; Krappmann D, Wulczyn F G, Scheidereit C (Sep. 1999). «NF-kappaB p105 is a target of IkappaB kinases and controls signal induction of Bcl-3-p50 complexes». EMBO J. (ENGLAND) 18 (17):  pp. 4766–78. doi:10.1093/emboj/18.17.4766. ISSN 0261-4189. PMID 10469655. 
  6. ↑ Baek, Sung Hee; Ohgi Kenneth A, Rose David W, Koo Edward H, Glass Christopher K, Rosenfeld Michael G (Jul. 2002). «Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-kappaB and beta-amyloid precursor protein». Cell (United States) 110 (1):  pp. 55–67. ISSN 0092-8674. PMID 12150997. 
  7. ↑ Shen, C H; Stavnezer J (Jun. 1998). «Interaction of stat6 and NF-kappaB: direct association and synergistic activation of interleukin-4-induced transcription». Mol. Cell. Biol. (UNITED STATES) 18 (6):  pp. 3395–404. ISSN 0270-7306. PMID 9584180. 
  8. ↑ Besta, Felicitas; Massberg Steffen, Brand Korbinian, Müller Elke, Page Sharon, Grüner Sabine, Lorenz Michael, Sadoul Karin, Kolanus Waldemar, Lengyel Ernst, Gawaz Meinrad (Oct. 2002). «Role of beta(3)-endonexin in the regulation of NF-kappaB-dependent expression of urokinase-type plasminogen activator receptor». J. Cell. Sci. (England) 115 (Pt 20):  pp. 3879–88. ISSN 0021-9533. PMID 12244126. 
  9. ↑ Hay, D C; Kemp G D, Dargemont C, Hay R T (May. 2001). «Interaction between hnRNPA1 and IkappaBalpha is required for maximal activation of NF-kappaB-dependent transcription». Mol. Cell. Biol. (United States) 21 (10):  pp. 3482–90. doi:10.1128/MCB.21.10.3482-3490.2001. ISSN 0270-7306. PMID 11313474. 
  10. ↑ Malek, S; Huxford T, Ghosh G (Sep. 1998). «Ikappa Balpha functions through direct contacts with the nuclear localization signals and the DNA binding sequences of NF-kappaB». J. Biol. Chem. (UNITED STATES) 273 (39):  pp. 25427–35. ISSN 0021-9258. PMID 9738011. 
  11. ↑ a b c d Bouwmeester, Tewis; Bauch Angela, Ruffner Heinz, Angrand Pierre-Olivier, Bergamini Giovanna, Croughton Karen, Cruciat Cristina, Eberhard Dirk, Gagneur Julien, Ghidelli Sonja, Hopf Carsten, Huhse Bettina, Mangano Raffaella, Michon Anne-Marie, Schirle Markus, Schlegl Judith, Schwab Markus, Stein Martin A, Bauer Andreas, Casari Georg, Drewes Gerard, Gavin Anne-Claude, Jackson David B, Joberty Gerard, Neubauer Gitte, Rick Jens, Kuster Bernhard, Superti-Furga Giulio (Feb. 2004). «A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway». Nat. Cell Biol. (England) 6 (2):  pp. 97–105. doi:10.1038/ncb1086. ISSN 1465-7392. PMID 14755267. 
  12. ↑ Palvimo, J J; Reinikainen P, Ikonen T, Kallio P J, Moilanen A, Jänne O A (Sep. 1996). «Mutual transcriptional interference between RelA and androgen receptor». J. Biol. Chem. (UNITED STATES) 271 (39):  pp. 24151–6. ISSN 0021-9258. PMID 8798655. 
  13. ↑ Ayroldi, E; Migliorati G, Bruscoli S, Marchetti C, Zollo O, Cannarile L, D'Adamio F, Riccardi C (Aug. 2001). «Modulation of T-cell activation by the glucocorticoid-induced leucine zipper factor via inhibition of nuclear factor kappaB». Blood (United States) 98 (3):  pp. 743–53. ISSN 0006-4971. PMID 11468175. 
  14. ↑ Guan, E; Wang J, Laborda J, Norcross M, Baeuerle P A, Hoffman T (May. 1996). «T cell leukemia-associated human Notch/translocation-associated Notch homologue has I kappa B-like activity and physically interacts with nuclear factor-kappa B proteins in T cells». J. Exp. Med. (UNITED STATES) 183 (5):  pp. 2025–32. ISSN 0022-1007. PMID 8642313. 
  15. ↑ Wang, J; Shelly L, Miele L, Boykins R, Norcross M A, Guan E (Jul. 2001). «Human Notch-1 inhibits NF-kappa B activity in the nucleus through a direct interaction involving a novel domain». J. Immunol. (United States) 167 (1):  pp. 289–95. ISSN 0022-1767. PMID 11418662. 
  16. ↑ Zhong, Haihong; May Michael J, Jimi Eijiro, Ghosh Sankar (Mar. 2002). «The phosphorylation status of nuclear NF-kappa B determines its association with CBP/p300 or HDAC-1». Mol. Cell (United States) 9 (3):  pp. 625–36. ISSN 1097-2765. PMID 11931769. 
  17. ↑ Ferrier, R; Nougarede R, Doucet S, Kahn-Perles B, Imbert J, Mathieu-Mahul D (Jan. 1999). «Physical interaction of the bHLH LYL1 protein and NF-kappaB1 p105». Oncogene (ENGLAND) 18 (4):  pp. 995–1005. doi:10.1038/sj.onc.1202374. ISSN 0950-9232. PMID 10023675. 
  18. ↑ Thornburg, Natalie J; Pathmanathan Rajadurai, Raab-Traub Nancy (Dec. 2003). «Activation of nuclear factor-kappaB p50 homodimer/Bcl-3 complexes in nasopharyngeal carcinoma». Cancer Res. (United States) 63 (23):  pp. 8293–301. ISSN 0008-5472. PMID 14678988. 
  19. ↑ Naumann, M; Wulczyn F G, Scheidereit C (Jan. 1993). «The NF-kappa B precursor p105 and the proto-oncogene product Bcl-3 are I kappa B molecules and control nuclear translocation of NF-kappa B». EMBO J. (ENGLAND) 12 (1):  pp. 213–22. ISSN 0261-4189. PMID 8428580. 
  20. ↑ Yu, Zhiyuan; Zhang Wenzheng, Kone Bruce C (Oct. 2002). «Signal transducers and activators of transcription 3 (STAT3) inhibits transcription of the inducible nitric oxide synthase gene by interacting with nuclear factor kappaB». Biochem. J. (England) 367 (Pt 1):  pp. 97–105. doi:10.1042/BJ20020588. ISSN 0264-6021. PMID 12057007. 
  21. ↑ Belich, M P; Salmerón A, Johnston L H, Ley S C (Jan. 1999). «TPL-2 kinase regulates the proteolysis of the NF-kappaB-inhibitory protein NF-kappaB1 p105». Nature (ENGLAND) 397 (6717):  pp. 363–8. doi:10.1038/16946. ISSN 0028-0836. PMID 9950430. 
  22. ↑ Heppner, C; Bilimoria K Y, Agarwal S K, Kester M, Whitty L J, Guru S C, Chandrasekharappa S C, Collins F S, Spiegel A M, Marx S J, Burns A L (Aug. 2001). «The tumor suppressor protein menin interacts with NF-kappaB proteins and inhibits NF-kappaB-mediated transactivation». Oncogene (England) 20 (36):  pp. 4917–25. doi:10.1038/sj.onc.1204529. ISSN 0950-9232. PMID 11526476. 
  23. ↑ Lee, S K; Na S Y, Jung S Y, Choi J E, Jhun B H, Cheong J, Meltzer P S, Lee Y C, Lee J W (Jun. 2000). «Activating protein-1, nuclear factor-kappaB, and serum response factor as novel target molecules of the cancer-amplified transcription coactivator ASC-2». Mol. Endocrinol. (UNITED STATES) 14 (6):  pp. 915–25. ISSN 0888-8809. PMID 10847592. 
  24. ↑ Na, S Y; Lee S K, Han S J, Choi H S, Im S Y, Lee J W (May. 1998). «Steroid receptor coactivator-1 interacts with the p50 subunit and coactivates nuclear factor kappaB-mediated transactivations». J. Biol. Chem. (UNITED STATES) 273 (18):  pp. 10831–4. ISSN 0021-9258. PMID 9556555. 
  25. ↑ Noro, Barbara; Licheri Barbara, Sgarra Riccardo, Rustighi Alessandra, Tessari Michela A, Chau Kai-Yin, Ono Santa Jeremy, Giancotti Vincenzo, Manfioletti Guidalberto (Apr. 2003). «Molecular dissection of the architectural transcription factor HMGA2». Biochemistry (United States) 42 (15):  pp. 4569–77. doi:10.1021/bi026605k. ISSN 0006-2960. PMID 12693954. 

Enlaces externos


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