Degradation of the hypoxia-inducible factor 1α: Where does it happen?

Cell Cycle

Volumn 5, Issue 23, 2006, Pages 2720-2722

  Pereira, Teresa ^a   Zheng, Xiaowei ^a   Poellinger, Lorenz ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

Author keywords

Hypoxia; Hypoxia inducible factor; Proteasomal activity; Proteasome; Protein degradation; Subcellular distribution; Subcellular localization

Indexed keywords

HYPOXIA INDUCIBLE FACTOR 1ALPHA;

CELL TYPE; GENE ACTIVATION; HUMAN; HYDROXYLATION; HYPOXIA; NONHUMAN; PROTEIN DEGRADATION; PROTEIN LOCALIZATION; SHORT SURVEY; UBIQUITINATION;

EID: 33845420006     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.5.23.3536     Document Type: Short Survey

References (30)

1. Semenza GL. Targeting HIF-1 for cancer therapy. Nat Rev Cancer 2003; 54:17-28.
2. Carmeliet P, Dor Y, Herbert JM, Fukumura D, Brusselmans K, Dewerchin M, Neeman M, Bono F, Abramovitch R, Maxwell P, Koch CJ, Ratcliffe P, Moons L, Jain RK, Collen D, Keshert E. Role of HIF-1α in hypoxia-mediated apoptosis, cell proliferation and tumor angiogenesis. Nature 1998; 394:485-90.
3. Ryan HE, Lo J, Johnson RS. HIF-1 alpha is required for solid tumor formation and embryonic vascularization. EMBO J 1998; 17:3005-15.
4. Tian H, Hammer RE, Matsumono AM, Russel DW, McKnight SL. The hypoxia-responsive transcription EPAS1 is essential for catecholamine homeostasis and protection against heart failure during embryonic development. Genes Dev 1998; 12:3320-4.
5. Salceda S, Caro J. Hypoxia-inducible factor 1α (HIF-1α) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induces changes. J Biol Chem 1997; 272:22642-7.
6. 2-dependent degradation domain via the ubiquitin-proteasome pathway. Proc Natl Acad Sci USA 1998; 95:7987-92.
7. Kallio PJ, Wilson WJ, O'Brien S, Makino Y, Poellinger L. Regulation of the hypoxia-inducible transcription factor 1α by the ubiquitin-proteasome pathway. J Biol Chem 1999; 274:6519-25.
8. Cockman ME, Masson N, Mole DR, Jaakkola P, Chang GW, Clifford SC, Maher ER, Pugh CW, Ratcliffe PJ, Maxwell PH. Hypoxia inducible factor-α binding and ubiquitylation by the von Hippel-Linadu tumor supressor protein. J Biol Chem 2000; 275:25733-41.
9. Kamura T, Sato S, Iwai K, Czyzyk-Krzeska M, Conaway RC, Conaway JW. Activation of HIF1α ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex. Proc Natl Acad Sci USA 2000; 97:10430-5.
10. Ohh M, Park CW, Ivan M, Hoffman MA, Kim TY, Huang LE, Pavletich N, Chau V, Kaelin WG. Ubiquitination of hypoxia-inducible factor requires direct binding to the beta-domain of the von Hippel-Lindau protein. Nat Cell Biol 2000; 2:423-7.
11. Tanimoto K, Makino Y, Pereira T, Poellinger L. Mechanism of regulation of the hypoxia-inducible factor-1α by the von Hippel-Lindau tumor suppressor protein. EMBO J 2000; 19:4298-309.
12. 2 sensing. Science 2001; 292:464-8.
13. 2-regulated prolyl hydroxylation. Science 2001; 292:468-72.
14. Masson N, Willam C, Maxwell PH, Pugh CW, Ratcliffe PJ. Independent function of two destruction domains in hypoxia-inducible factor-α chains activated by prolyl hydroxylation. EMBO J 2001; 20:5197-206.
15. Yu F, White SB, Zhao Q, Lee FS. HIF-1α binding to VHL is regulated by stimulus-sensitive proline hydroxylation. Proc Natl Acad Sci USA 2001; 98:9630-5.
16. Bruick RK, McKnight SL. A concerved family of prolyl-4-hydroxylases that modify HIF. Science 2001; 294:1337-40.
17. Epstein AC, Gleadle JM, McNeil LA, Hewitson KS, O'Rourke J, Mole DR, Mukherji M, Metzen E, Wilson MI, Dhanda A, Tian YM, Masson N, Hamilton DL, Jaakkola P, Barstead R, Hodgkin J, Maxwell PH, Pugh CW, Schofield CJ, Ratcliffe PJ. C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 2001; 107:43-54.
18. Zheng X, Ruas JL, Cao R, Salomons FA, Cao Y, Poellinger L, Pereira T. Cell-type-specific regulation of degradation of hypoxia-inducible factor 1α: Role of subcellular compartmentalization. Mol Cell Biol 2006; 26:4628-41.
19. Chan DA, Sutphin PD, Denko NC, Giaccia AJ. Role of prolyl hydroxylation in oncogenically stabilized hypoxia-inducible factor-1α. J Biol Chem 2002; 277:40112-7.
20. Groulx I, Lee S. Oxygen-dependent ubiquitination and degradation of hypoxia-inducible factor requires nuclear-cytoplasmic trafficking of the von Hippel-Lindau tumor supressor protein. Mol Cell Biol 2002; 22:5319-36.
21. 2-driven proteasomal degradation irrespective of its subcellular localization: Nucleus or cytoplasm. EMBO Rep 2001; 2:615-20.
22. Mylonis I, Chachami G, Samiotaki M, Panayotou G, Paraskeva R, Kalousi A, Georgatsou E, Bonanou S, Simos G. Identification of MAPK phosphorylation sites and their role in the localization and activity of hypoxia-inducible factor 1α. J Biol Chem 2006, (in press, 10.1074/jbc.M605058200).
23. Berra E, Benizri E, Ginouves A, Volmat V, Roux D, Pouyssegur J. HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1α in normoxia. EMBO J 2003; 22:4082-92.
24. Metzen E, Berchner-Pfannschmidt U, Stengel P, Marxsen JH, Stolze I, Klinger M, Huang WQ, Wotzlaw C, Hellwig-Burgel T, Jelkmann W, Acker H, Fandrey J. Intracellular localisation of human HIF-1α hydroxylases: Implications for oxygen sensing. J Cell Sci 2003; 116:1319-26.
25. Jokilehto T, Rantanen K, Luukkaa M, Heikkinen P, Grenman R, Minn H, Kronqvist P, Jaakkola PM. Overexpression and nuclear translocation of hypoxia-inducible factor prolyl hydroxylase PHD2 in head and neck squamous cell carcinoma is associated with tumor aggressiveness. Clin Cancer Res 2006; 12:1080-7.
26. Soilleux EJ, Turley H, Tian YM, Pugh CW, Gatter KC, Harris AL. Use of novel monoclonal antibodies to determine the expression and distribution of the hypoxia regulatory factors PHD-1, PHD-2, PHD-3 and FIH in normal and neoplastic human tisues. Histopathology 2005; 47:602-610.
27. Hergovich A, Lisztwan J, Barry R, Ballschmieter P, Krek W. Regulation of microtubule stability by the von Hippel-Lindau tumour suppressor protein pVHL. Nat Cell Biol 2003; 5:64-70.
28. Illiopoulus O, Ohh M, Kaelin Jr WG. pVHL19 is a biologically active product of the von Hippel-Lindau gene arising from internal translation initiation. Proc Natl Acad Sci USA 1998; 95:11661-6.
29. Lewis MD, Roberts BJ. Role of nuclear and cytoplasmic localization in the tumour-suppressor activity of the von Hippel-Lindau protein. Oncogene 2003; 22:3992-7.
30. Li Z, Wang D, Messing EM, Wu G. VHL protein-interacting deubiquitinating enzyme 2 deubiquitinates and stabilizes HIF-1α. EMBO Rep 2005; 6:373-8.