HIF1α protein stability is increased by acetylation at lysine 709

Journal of Biological Chemistry

Volumn 287, Issue 42, 2012, Pages 35496-35505

  Geng, Hao ^a   Liu, Qiong ^a   Xue, Changhui ^a   David, Larry L ^a   Beer, Tomasz M ^a   Thomas, George V ^a   Dai, Mu Shui ^a   Qian, David Z ^a  

^a OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CANCER CELLS; ENDOGENOUS TARGET GENES; GROWTH ARREST; MOLECULAR MECHANISM; MUTANT PROTEINS; OVER-EXPRESSION; POLYUBIQUITINATION; PROTEIN STABILITY; TRANSACTIVATION; TRANSCRIPTIONAL COMPLEXES; WILD TYPES; WILD-TYPE PROTEINS;

ACETYLATION; AMINO ACIDS; CELLS; STABILITY;

PROTEINS;

ALANINE; E1A ASSOCIATED P300 PROTEIN; HISTONE DEACETYLASE 1; HISTONE DEACETYLASE 3; HYPOXIA INDUCIBLE FACTOR 1ALPHA; LYSINE; MUTANT PROTEIN;

ACETYLATION; ARTICLE; CANCER CELL; CONTROLLED STUDY; GENE TARGETING; HUMAN; HUMAN CELL; HYPOXIA; PRIORITY JOURNAL; PROTEIN DEFECT; PROTEIN DEPLETION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; TRANSLATION REGULATION; UBIQUITINATION;

ACETYLATION; AMINO ACID SUBSTITUTION; CELL CYCLE CHECKPOINTS; CELL HYPOXIA; CELL LINE, TUMOR; HEK293 CELLS; HISTONE DEACETYLASE 1; HISTONE DEACETYLASES; HUMANS; HYPOXIA-INDUCIBLE FACTOR 1, ALPHA SUBUNIT; LYSINE; MUTATION, MISSENSE; P300-CBP TRANSCRIPTION FACTORS; PROTEIN STABILITY;

EID: 84867424393     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.400697     Document Type: Article

References (33)

1. Semenza, G. L. (2012) Hypoxia-inducible factors in physiology and medicine. Cell 148, 399-408
2. Ivan, M., Kondo, K., Yang, H., Kim, W., Valiando, J., Ohh, M., Salic, A., Asara, J. M., Lane, W. S., and Kaelin, W. G., Jr. (2001) HIFα targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing. Science 292, 464-468 (Pubitemid 32335941)
3. Yu, F., White, S. B., Zhao, Q., and Lee, F. S. (2001) HIF-1α binding to VHL is regulated by stimulus-sensitive proline hydroxylation. Proc. Natl. Acad. Sci. U.S.A. 98, 9630-9635 (Pubitemid 32769354)
4. Semenza, G. L. (2012) Hypoxia-inducible factors: mediators of cancer progression and targets for cancer therapy. Trends Pharmacol. Sci. 33, 207-214
5. Semenza, G. L. (2004) Intratumoral hypoxia, radiation resistance, and HIF-1. Cancer Cell 5, 405-406
6. Isaacs, J. S., Jung, Y. J., Mimnaugh, E. G., Martinez, A., Cuttitta, F., and Neckers, L. M. (2002) Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1 α-degradative pathway. J. Biol. Chem. 277, 29936-29944
7. Liu, Y. V., and Semenza, G. L. (2007) RACK1 versus HSP90: competition for HIF-1 α degradation versus stabilization. Cell Cycle 6, 656-659 (Pubitemid 46535675)
8. Luo, W., Zhong, J., Chang, R., Hu, H., Pandey, A., and Semenza, G. L. (2010) Hsp70 and CHIP selectively mediate ubiquitination and degradation of hypoxia-inducible factor (HIF)-1α but Not HIF-2α. J. Biol. Chem. 285, 3651-3663
9. Ellis, L., Hammers, H., and Pili, R. (2009) Targeting tumor angiogenesis with histone deacetylase inhibitors. Cancer Lett. 280, 145-153
10. Qian, D. Z., Kachhap, S. K., Collis, S. J., Verheul, H. M., Carducci, M. A., Atadja, P., and Pili, R. (2006) Class II histone deacetylases are associated with VHL-independent regulation of hypoxia-inducible factor 1 α. Cancer Res. 66, 8814-8821 (Pubitemid 44449199)
11. Jeong, J. W., Bae, M. K., Ahn, M. Y., Kim, S. H., Sohn, T. K., Bae, M. H., Yoo, M. A., Song, E. J., Lee, K. J., and Kim, K. W. (2002) Regulation and destabilization of HIF-1α by ARD1-mediated acetylation. Cell 111, 709-720 (Pubitemid 35441252)
12. Kato, H., Tamamizu-Kato, S., and Shibasaki, F. (2004) Histone deacetylase 7 associates with hypoxia-inducible factor 1α and increases transcriptional activity. J. Biol. Chem. 279, 41966-41974 (Pubitemid 39313647)
13. Finley, L. W., Carracedo, A., Lee, J., Souza, A., Egia, A., Zhang, J., Teruya- Feldstein, J., Moreira, P. I., Cardoso, S. M., Clish, C. B., Pandolfi, P. P., and Haigis, M. C. (2011) SIRT3 opposes reprogramming of cancer cell metabolism through HIF1α destabilization. Cancer Cell 19, 416-428
14. Lim, J. H., Lee, Y. M., Chun, Y. S., Chen, J., Kim, J. E., and Park, J. W. (2010) Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxia-inducible factor 1α. Mol. Cell 38, 864-878
15. Laemmle, A., Lechleiter, A., Roh, V., Schwarz, C., Portmann, S., Furer, C., Keogh, A., Tschan, M. P., Candinas, D., Vorburger, S. A., and Stroka, D. (2012) Inhibition of SIRT1 impairs the accumulation and transcriptional activity of HIF-1α protein under hypoxic conditions. PLoS One 7, e33433
16. Kim, S. H., Jeong, J. W., Park, J. A., Lee, J. W., Seo, J. H., Jung, B. K., Bae, M. K., and Kim, K. W. (2007) Regulation of the HIF-1α stability by histone deacetylases. Oncol. Rep. 17, 647-651
17. Sadoul, K., Boyault, C., Pabion, M., and Khochbin, S. (2008) Regulation of protein turnover by acetyltransferases and deacetylases. Biochimie 90, 306-312 (Pubitemid 351172566)
18. Geng, H., Harvey, C. T., Pittsenbarger, J., Liu, Q., Beer, T. M., Xue, C., and Qian, D. Z. (2011) HDAC4 protein regulates HIF1α protein lysine acetylation and cancer cell response to hypoxia. J. Biol. Chem. 286, 38095-38102
19. Arany, Z., Huang, L. E., Eckner, R., Bhattacharya, S., Jiang, C., Goldberg, M. A., Bunn, H. F., and Livingston, D. M. (1996) An essential role for p300/CBP in the cellular response to hypoxia. Proc. Natl. Acad. Sci. U.S.A. 93, 12969-12973 (Pubitemid 26382753)
20. Dann, C. E., 3rd, Bruick, R. K., and Deisenhofer, J. (2002) Structure of factor-inhibiting hypoxia-inducible factor 1: An asparaginyl hydroxylase involved in the hypoxic response pathway. Proc. Natl. Acad. Sci. U.S.A. 99, 15351-15356 (Pubitemid 35403938)
21. Kung, A. L., Wang, S., Klco, J. M., Kaelin, W. G., and Livingston, D. M. (2000) Suppression of tumor growth through disruption of hypoxia-inducible transcription. Nat. Med. 6, 1335-1340 (Pubitemid 32001016)
22. Kung, A. L., Zabludoff, S. D., France, D. S., Freedman, S. J., Tanner, E. A., Vieira, A., Cornell-Kennon, S., Lee, J., Wang, B., Wang, J., Memmert, K., Naegeli, H. U., Petersen, F., Eck, M. J., Bair, K. W., Wood, A. W., and Livingston, D. M. (2004) Small molecule blockade of transcriptional coactivation of the hypoxia-inducible factor pathway. Cancer Cell 6, 33-43 (Pubitemid 38903160)
23. Chan, H. M., and La Thangue, N. B. (2001) p300/CBP proteins: HATs for transcriptional bridges and scaffolds. J. Cell Sci. 114, 2363-2373 (Pubitemid 32684792)
24. Geng, H., Rademacher, B. L., Pittsenbarger, J., Huang, C. Y., Harvey, C. T., Lafortune, M. C., Myrthue, A., Garzotto, M., Nelson, P. S., Beer, T. M., and Qian, D. Z. (2010) ID1 enhances docetaxel cytotoxicity in prostate cancer cells through inhibition of p21. Cancer Res. 70, 3239-3248
25. Harten, S. K., Esteban, M. A., and Maxwell, P. H. (2009) Identification of novel VHL regulated genes by transcriptomic analysis of RCC10 renal carcinoma cells. Adv. Enzyme Regul. 49, 43-52
26. Semenza, G. L. (2007) Hypoxia-inducible factor 1 (HIF-1) pathway. Sci. STKE 2007, cm8
27. Mahon, P. C., Hirota, K., and Semenza, G. L. (2001) FIH-1: a novel protein that interacts with HIF-1α and VHL to mediate repression of HIF-1 transcriptional activity. Genes Dev. 15, 2675-2686 (Pubitemid 32988878)
28. Chen, L. F., Mu, Y., and Greene, W. C. (2002) Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-κB. EMBO J. 21, 6539-6548 (Pubitemid 35448431)
29. Kim, W., Bennett, E. J., Huttlin, E. L., Guo, A., Li, J., Possemato, A., Sowa, M. E., Rad, R., Rush, J., Comb, M. J., Harper, J. W., and Gygi, S. P. (2011) Systematic and quantitative assessment of the ubiquitin-modified proteome. Mol. Cell 44, 325-340
30. 2-independent and HSP90 inhibitor-induced degradation of HIF-1α. Mol. Cell 25, 207-217
31. Zhang, H., Qian, D. Z., Tan, Y. S., Lee, K., Gao, P., and Ren, Y. R. (2008) Digoxin and other cardiac glycosides inhibit HIF-1α synthesis and block tumor growth. Proc. Natl. Acad. Sci. U.S.A. 105, 19579-19586
32. Koh, M. Y., Darnay, B. G., and Powis, G. (2008) Hypoxia-associated factor, a novel E3-ubiquitin ligase, binds and ubiquitinates hypoxia-inducible factor 1α, leading to its oxygen-independent degradation. Mol. Cell. Biol. 28, 7081-7095
33. Luo, W., Hu, H., Chang, R., Zhong, J., Knabel, M., O'Meally, R., Cole, R. N., Pandey, A., and Semenza, G. L. (2011) Pyruvate kinase M2 is a PHD3-stimulated coactivator for hypoxia-inducible factor 1. Cell 145, 732-744