MAPK14

MAPK14
MAP quinasa 14
Protein MAPK14 PDB 1a9u.png
Estructura tridimensional de la proteína MAPK14.
HUGO 6876
Símbolo MAPK14
Símbolos alt. CSBP1, CSBP2, CSPB1, EXIP, Mxi2, PRKM14, PRKM15, RK, SAPK2A, p38, p38ALPHA
Datos genéticos
Locus Cr. 6 p21.31
Bases de datos
Entrez 1432
OMIM 600289
PDB 1a9u
RefSeq NP_001306
UniProt Q16539

La MAP quinasa 14 (MAPK14) es una enzima codificada en humanos por el gen mapk14.[1]

La MAPK14 pertenece a la familia de las MAP quinasas. Las MAP quinasas actúan como punto de integración de múltiples señales bioquímicas, y están implicadas en una amplia variedad de procesos celulares tales como proliferación celular, diferenciación celular, regulación de la transcripción y desarrollo. La MAPK14 es activada por diversos estímulos ambientales relacionados con el estrés y por citoquinas proinflamatorias. Dicha activación requiere la fosforilación llevada a cabo por MAP quinasa quinasas (MKKs), o bien su propia autofosforilación llevada a cabo por la interacción del complejo MAP3K7IP1/TAB1 con MAPK14. Los sustratos de esta quinasa incluyen diversas proteínas o factores de transcripción como ATF2, MEF2C, MAX, el regulador del ciclo celular CDC25B y el supresor tumoral p53, lo que sugiere un papel de esta quinasa en regulación del ciclo celular y la transcripción, así como en respuesta a estrés genotóxico. Se han descrito cuatro variantes transcripcionales de este gen, que codifican diversas isoformas de la quinasa.[2]

Interacciones

La proteína MAPK14 ha demostrado ser capaz de interaccionar con:

Véase también

  • MAP quinasas (MAPK)

Referencias

  1. ↑ Lee JC, Laydon JT, McDonnell PC, Gallagher TF, Kumar S, Green D, McNulty D, Blumenthal MJ, Heys JR, Landvatter SW, et al. (Jan 1995). «A protein kinase involved in the regulation of inflammatory cytokine biosynthesis». Nature 372 (6508):  pp. 739–46. doi:10.1038/372739a0. PMID 7997261. 
  2. ↑ «Entrez Gene: MAPK14 mitogen-activated protein kinase 14».
  3. ↑ Sayed, M; Kim S O, Salh B S, Issinger O G, Pelech S L (Jun. 2000). «Stress-induced activation of protein kinase CK2 by direct interaction with p38 mitogen-activated protein kinase». J. Biol. Chem. (UNITED STATES) 275 (22):  pp. 16569–73. doi:10.1074/jbc.M000312200. ISSN 0021-9258. PMID 10747897. 
  4. ↑ Pierrat, B; Correia J S, Mary J L, Tomás-Zuber M, Lesslauer W (Nov. 1998). «RSK-B, a novel ribosomal S6 kinase family member, is a CREB kinase under dominant control of p38alpha mitogen-activated protein kinase (p38alphaMAPK)». J. Biol. Chem. (UNITED STATES) 273 (45):  pp. 29661–71. ISSN 0021-9258. PMID 9792677. 
  5. ↑ a b Rane, M J; Coxon P Y, Powell D W, Webster R, Klein J B, Pierce W, Ping P, McLeish K R (Feb. 2001). «p38 Kinase-dependent MAPKAPK-2 activation functions as 3-phosphoinositide-dependent kinase-2 for Akt in human neutrophils». J. Biol. Chem. (United States) 276 (5):  pp. 3517–23. doi:10.1074/jbc.M005953200. ISSN 0021-9258. PMID 11042204. 
  6. ↑ Janknecht, R (Nov. 2001). «Cell type-specific inhibition of the ETS transcription factor ER81 by mitogen-activated protein kinase-activated protein kinase 2». J. Biol. Chem. (United States) 276 (45):  pp. 41856–61. doi:10.1074/jbc.M106630200. ISSN 0021-9258. PMID 11551945. 
  7. ↑ a b Bulavin, D V; Higashimoto Y, Popoff I J, Gaarde W A, Basrur V, Potapova O, Appella E, Fornace A J (May. 2001). «Initiation of a G2/M checkpoint after ultraviolet radiation requires p38 kinase». Nature (England) 411 (6833):  pp. 102–7. doi:10.1038/35075107. ISSN 0028-0836. PMID 11333986. 
  8. ↑ a b c Tanoue, T; Yamamoto T, Maeda R, Nishida E (Jul. 2001). «A Novel MAPK phosphatase MKP-7 acts preferentially on JNK/SAPK and p38 alpha and beta MAPKs». J. Biol. Chem. (United States) 276 (28):  pp. 26629–39. doi:10.1074/jbc.M101981200. ISSN 0021-9258. PMID 11359773. 
  9. ↑ Slack, D N; Seternes O M, Gabrielsen M, Keyse S M (May. 2001). «Distinct binding determinants for ERK2/p38alpha and JNK map kinases mediate catalytic activation and substrate selectivity of map kinase phosphatase-1». J. Biol. Chem. (United States) 276 (19):  pp. 16491–500. doi:10.1074/jbc.M010966200. ISSN 0021-9258. PMID 11278799. 
  10. ↑ Rual, Jean-François; Venkatesan Kavitha, Hao Tong, Hirozane-Kishikawa Tomoko, Dricot Amélie, Li Ning, Berriz Gabriel F, Gibbons Francis D, Dreze Matija, Ayivi-Guedehoussou Nono, Klitgord Niels, Simon Christophe, Boxem Mike, Milstein Stuart, Rosenberg Jennifer, Goldberg Debra S, Zhang Lan V, Wong Sharyl L, Franklin Giovanni, Li Siming, Albala Joanna S, Lim Janghoo, Fraughton Carlene, Llamosas Estelle, Cevik Sebiha, Bex Camille, Lamesch Philippe, Sikorski Robert S, Vandenhaute Jean, Zoghbi Huda Y, Smolyar Alex, Bosak Stephanie, Sequerra Reynaldo, Doucette-Stamm Lynn, Cusick Michael E, Hill David E, Roth Frederick P, Vidal Marc (Oct. 2005). «Towards a proteome-scale map of the human protein-protein interaction network». Nature (England) 437 (7062):  pp. 1173–8. doi:10.1038/nature04209. PMID 16189514. 
  11. ↑ a b c Tanoue, T; Maeda R, Adachi M, Nishida E (Feb. 2001). «Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions». EMBO J. (England) 20 (3):  pp. 466–79. doi:10.1093/emboj/20.3.466. ISSN 0261-4189. PMID 11157753. 
  12. ↑ Raingeaud, J; Gupta S, Rogers J S, Dickens M, Han J, Ulevitch R J, Davis R J (Mar. 1995). «Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine». J. Biol. Chem. (UNITED STATES) 270 (13):  pp. 7420–6. ISSN 0021-9258. PMID 7535770. 
  13. ↑ a b Chen, Z; Cobb M H (May. 2001). «Regulation of stress-responsive mitogen-activated protein (MAP) kinase pathways by TAO2». J. Biol. Chem. (United States) 276 (19):  pp. 16070–5. doi:10.1074/jbc.M100681200. ISSN 0021-9258. PMID 11279118. 
  14. ↑ Tournier, C; Whitmarsh A J, Cavanagh J, Barrett T, Davis R J (Jul. 1997). «Mitogen-activated protein kinase kinase 7 is an activator of the c-Jun NH2-terminal kinase». Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 94 (14):  pp. 7337–42. ISSN 0027-8424. PMID 9207092. 
  15. ↑ a b Sanz-Moreno, Victoria; Casar Berta, Crespo Piero (May. 2003). «p38alpha isoform Mxi2 binds to extracellular signal-regulated kinase 1 and 2 mitogen-activated protein kinase and regulates its nuclear activity by sustaining its phosphorylation levels». Mol. Cell. Biol. (United States) 23 (9):  pp. 3079–90. ISSN 0270-7306. PMID 12697810. 
  16. ↑ Zhao, M; New L, Kravchenko V V, Kato Y, Gram H, di Padova F, Olson E N, Ulevitch R J, Han J (Jan. 1999). «Regulation of the MEF2 family of transcription factors by p38». Mol. Cell. Biol. (UNITED STATES) 19 (1):  pp. 21–30. ISSN 0270-7306. PMID 9858528. 
  17. ↑ Yang, S H; Galanis A, Sharrocks A D (Jun. 1999). «Targeting of p38 mitogen-activated protein kinases to MEF2 transcription factors». Mol. Cell. Biol. (UNITED STATES) 19 (6):  pp. 4028–38. ISSN 0270-7306. PMID 10330143. 
  18. ↑ Ge, Baoxue; Gram Hermann, Di Padova Franco, Huang Betty, New Liguo, Ulevitch Richard J, Luo Ying, Han Jiahuai (Feb. 2002). «MAPKK-independent activation of p38alpha mediated by TAB1-dependent autophosphorylation of p38alpha». Science (United States) 295 (5558):  pp. 1291–4. doi:10.1126/science.1067289. PMID 11847330. 
  19. ↑ Masuda, K; Shima H, Watanabe M, Kikuchi K (Oct. 2001). «MKP-7, a novel mitogen-activated protein kinase phosphatase, functions as a shuttle protein». J. Biol. Chem. (United States) 276 (42):  pp. 39002–11. doi:10.1074/jbc.M104600200. ISSN 0021-9258. PMID 11489891. 
  20. ↑ Faccio, L; Fusco C, Chen A, Martinotti S, Bonventre J V, Zervos A S (Jan. 2000). «Characterization of a novel human serine protease that has extensive homology to bacterial heat shock endoprotease HtrA and is regulated by kidney ischemia». J. Biol. Chem. (UNITED STATES) 275 (4):  pp. 2581–8. ISSN 0021-9258. PMID 10644717. 
  21. ↑ Tanoue, T; Moriguchi T, Nishida E (Jul. 1999). «Molecular cloning and characterization of a novel dual specificity phosphatase, MKP-5». J. Biol. Chem. (UNITED STATES) 274 (28):  pp. 19949–56. ISSN 0021-9258. PMID 10391943. 
  22. ↑ Kim, Min Jung; Park Bum-Joon, Kang Young-Sun, Kim Hyoung June, Park Jae-Hyun, Kang Jung Woo, Lee Sang Won, Han Jung Min, Lee Han-Woong, Kim Sunghoon (Jul. 2003). «Downregulation of FUSE-binding protein and c-myc by tRNA synthetase cofactor p38 is required for lung cell differentiation». Nat. Genet. (United States) 34 (3):  pp. 330–6. doi:10.1038/ng1182. ISSN 1061-4036. PMID 12819782. 
  23. ↑ Ku, Nam-On; Azhar Salman, Omary M Bishr (Mar. 2002). «Keratin 8 phosphorylation by p38 kinase regulates cellular keratin filament reorganization: modulation by a keratin 1-like disease causing mutation». J. Biol. Chem. (United States) 277 (13):  pp. 10775–82. doi:10.1074/jbc.M107623200. ISSN 0021-9258. PMID 11788583. 
  24. ↑ Raingeaud, J; Whitmarsh A J, Barrett T, Dérijard B, Davis R J (Mar. 1996). «MKK3- and MKK6-regulated gene expression is mediated by the p38 mitogen-activated protein kinase signal transduction pathway». Mol. Cell. Biol. (UNITED STATES) 16 (3):  pp. 1247–55. ISSN 0270-7306. PMID 8622669. 
  25. ↑ Stein, B; Brady H, Yang M X, Young D B, Barbosa M S (May. 1996). «Cloning and characterization of MEK6, a novel member of the mitogen-activated protein kinase kinase cascade». J. Biol. Chem. (UNITED STATES) 271 (19):  pp. 11427–33. ISSN 0021-9258. PMID 8626699. 

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