SUMOylation is a regulator of the translocation of Jak2 between nucleus and cytosol

Biochemical Journal

Volumn 453, Issue 2, 2013, Pages 231-239

  Sedek, Magdalena ^a   Strous, Ger J ^a  

^a UNIVERSITY MEDICAL CENTER UTRECHT   (Netherlands)

Author keywords

Growth hormone; Janus kinase 2 (Jak2); Nuclear translocation; Stress; SUMOylation

Indexed keywords

GROWTH HORMONE; JANUS KINASE 2;

ARTICLE; CATALYSIS; CELL FRACTIONATION; EMBRYO; ENVIRONMENTAL STRESS; HUMAN; HUMAN CELL; MOUSE; MUTANT; MYELOPROLIFERATIVE DISORDER; NONHUMAN; PRIORITY JOURNAL; SUMOYLATION;

ANIMALS; CELL NUCLEUS; CYTOPLASM; GROWTH HORMONE; HEK293 CELLS; HUMANS; JANUS KINASE 2; MICE; PROTEIN TRANSPORT; SUMOYLATION;

EID: 84879557841     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20121375     Document Type: Article

References (32)

1. Levine, R. L., Pardanani, A., Tefferi, A. and Gilliland, D. G. (2007) Role of JAK2 in the pathogenesis and therapy of myeloproliferative disorders. Nat. Rev. Cancer 7, 673-683 (Pubitemid 47327415)
2. Dawson, M. A., Bannister, A. J., Gottgens, B., Foster, S. D., Bartke, T., Green, A. R. and Kouzarides, T. (2009) JAK2 phosphorylates histone H3Y41 and excludes HP1α from chromatin. Nature 461, 819-822
3. Rinaldi, C. R., Rinaldi, P., Alagia, A., Gemei, M., Esposito, N., Formiggini, F., Martinelli, V., Senyuk, V., Nucifora, G. and Pane, F. (2010) Preferential nuclear accumulation of JAK2V617F in CD34+ but not in granulocytic, megakaryocytic, or erythroid cells of patients with Philadelphia-negative myeloproliferative neoplasia. Blood 116, 6023-6026
4. Geiss-Friedlander, R. and Melchior, F. (2007) Concepts in sumoylation: a decade on. Nat. Rev. Mol. Cell Biol. 8, 947-956 (Pubitemid 350176509)
5. Sampson, D. A., Wang, M. and Matunis, M. J. (2001) The SUMO-1 consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification. J. Biol. Chem. 276, 21664-21669
6. Matic, I., Schimmel, J., Hendriks, I. A., van Santen, M. A., van de Rijke, F., van Dam, H., Gnad, F., Mann, M. and Vertegaal, A. C. (2010) Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif. Mol. Cell 39, 641-652
7. Yang, X. J. and Gregoire, S. (2006) A recurrent phospho-sumoyl switch in transcriptional repression and beyond. Mol. Cell 23, 779-786
8. Hietakangas, V., Ahlskog, J. K., Jakobsson, A. M., Hellesuo, M., Sahlberg, N. M., Holmberg, C. I., Mikhailov, A., Palvimo, J. J., Pirkkala, L. and Sistonen, L. (2003) Phosphorylation of serine 303 is a prerequisite for the stress-inducible SUMO modification of heat shock factor 1. Mol. Cell. Biol. 23, 2953-2968 (Pubitemid 36403091)
9. Müller, S., Matunis, M. J. and Dejean, A. (1998) Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus. EMBO J. 17, 61-70
10. Yang, S. H., Jaffray, E., Senthinathan, B., Hay, R. T. and Sharrocks, A. D. (2003) SUMO and transcriptional repression: dynamic interactions between the MAP kinase and SUMO pathways. Cell Cycle 2, 528-530
11. Lin, X., Sun, B., Liang, M., Liang, Y. Y., Gast, A., Hildebrand, J., Brunicardi, F. C., Melchior, F. and Feng, X. H. (2003) Opposed regulation of corepressor CtBP by SUMOylation and PDZ binding. Mol. Cell 11, 1389-1396 (Pubitemid 36645156)
12. Huang, T. T., Wuerzberger-Davis, S. M., Wu, Z. H. and Miyamoto, S. (2003) Sequential modification of NEMO/IKKγ by SUMO-1 and ubiquitin mediates NF-κB activation by genotoxic stress. Cell 115, 565-576 (Pubitemid 37506045)
13. Sehat, B., Tofigh, A., Lin, Y., Trocme, E., Liljedahl, U., Lagergren, J. and Larsson, O. (2010) SUMOylation mediates the nuclear translocation and signaling of the IGF-1 receptor. Sci. Signaling 3, ra10
14. Sobko, A., Ma, H. and Firtel, R. A. (2002) Regulated SUMOylation and ubiquitination of DdMEK1 is required for proper chemotaxis. Dev. Cell 2, 745-756 (Pubitemid 34650071)
15. Wood, L. D., Irvin, B. J., Nucifora, G., Luce, K. S. and Hiebert, S. W. (2003) Small ubiquitin-like modifier conjugation regulates nuclear export of TEL, a putative tumor suppressor. Proc. Natl. Acad. Sci. U.S.A. 100, 3257-3262 (Pubitemid 36356570)
16. van Kerkhof, P., Govers, R., Alves dos Santos, C. M. and Strous, G. J. (2000) Endocytosis and degradation of the growth hormone receptor are proteasome-dependent. J. Biol. Chem. 275, 1575-1580 (Pubitemid 30060771)
17. Strous, G. J., van Kerkhof, P., Govers, R., Ciechanover, A. and Schwartz, A. L. (1996) The ubiquitin conjugation system is required for ligand-induced endocytosis and degradation of the growth hormone receptor. EMBO J. 15, 3806-3812 (Pubitemid 26289790)
18. Alves dos Santos, C. M., van Kerkhof, P. and Strous, G. J. (2001) The signal transduction of the growth hormone receptor is regulated by the ubiquitin/proteasome system and continues after endocytosis. J. Biol. Chem. 276, 10839-10846
19. Lu, X., Levine, R., Tong, W., Wernig, G., Pikman, Y., Zarnegar, S., Gilliland, D. G. and Lodish, H. (2005) Expression of a homodimeric type I cytokine receptor is required for JAK2V617F-mediated transformation. Proc. Natl. Acad. Sci. U.S.A. 102, 18962-18967 (Pubitemid 43049549)
20. Hofmann, W. A., Arduini, A., Nicol, S. M., Camacho, C. J., Lessard, J. L., Fuller-Pace, F. V. and de Lanerolle, P. (2009) SUMOylation of nuclear actin. J. Cell Biol. 186, 193-200
21. Putters, J., da Silva Almeida, A. C., van Kerkhof, P., van Rossum, A. G., Gracanin, A. and Strous, G. J. (2011) Jak2 is a negative regulator of ubiquitin-dependent endocytosis of the growth hormone receptor. PLoS ONE 6, e14676
22. Cimarosti, H., Lindberg, C., Bomholt, S. F., Ronn, L. C. and Henley, J. M. (2008) Increased protein SUMOylation following focal cerebral ischemia. Neuropharmacology 54, 280-289
23. Lee, Y. J., Castri, P., Bembry, J., Maric, D., Auh, S. and Hallenbeck, J. M. (2009) SUMOylation participates in induction of ischemic tolerance. J. Neurochem. 109, 257-267
24. Loftus, L. T., Gala, R., Yang, T., Jessick, V. J., Ashley, M. D., Ordonez, A. N., Thompson, S. J., Simon, R. P. and Meller, R. (2009) Sumo-2/3-ylation following in vitro modeled ischemia is reduced in delayed ischemic tolerance. Brain Res. 1272, 71-80
25. Saitoh, H. and Hinchey, J. (2000) Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3. J. Biol. Chem. 275, 6252-6258 (Pubitemid 30129915)
26. Yang, W., Sheng, H., Warner, D. S. and Paschen, W. (2008) Transient focal cerebral ischemia induces a dramatic activation of small ubiquitin-like modifier conjugation. J. Cereb. Blood Flow Metab. 28, 892-896 (Pubitemid 351589638)
27. Yang, W., Sheng, H., Warner, D. S. and Paschen, W. (2008) Transient global cerebral ischemia induces a massive increase in protein sumoylation. J. Cereb. Blood Flow Metab. 28, 269-279 (Pubitemid 351161280)
28. James, C., Ugo, V., Le Couedic, J. P., Staerk, J., Delhommeau, F., Lacout, C., Garcon, L., Raslova, H., Berger, R., Bennaceur-Griscelli, A. et al. (2005) A unique clonal JAK2 mutation leading to constitutive signalling causes polycythaemia vera. Nature 434, 1144-1148 (Pubitemid 40663494)
29. Baxter, E. J., Scott, L. M., Campbell, P. J., East, C., Fourouclas, N., Swanton, S., Vassiliou, G. S., Bench, A. J., Boyd, E. M., Curtin, N. et al. (2005) Acquired mutation of the tyrosine kinase JAK2 in human myeloproliferative disorders. Lancet 365, 1054-1061 (Pubitemid 40386783)
30. Kralovics, R., Passamonti, F., Buser, A. S., Teo, S. S., Tiedt, R., Passweg, J. R., Tichelli, A., Cazzola, M. and Skoda, R. C. (2005) A gain-of-function mutation of JAK2 in myeloproliferative disorders. N. Engl. J. Med. 352, 1779-1790 (Pubitemid 40570926)
31. Levine, R. L., Wadleigh, M., Cools, J., Ebert, B. L., Wernig, G., Huntly, B. J., Boggon, T. J., Wlodarska, I., Clark, J. J., Moore, S. et al. (2005) Activating mutation in the tyrosine kinase JAK2 in polycythemia vera, essential thrombocythemia, and myeloid metaplasia with myelofibrosis. Cancer Cell 7, 387-397 (Pubitemid 40544655)
32. Zhao, R., Xing, S., Li, Z., Fu, X., Li, Q., Krantz, S. B. and Zhao, Z. J. (2005) Identification of an acquired JAK2 mutation in polycythemia vera. J. Biol. Chem. 280, 22788-22792 (Pubitemid 40853184)