Tat-binding protein-1, a component of the 26S proteasome, contributes to the E3 ubiquitin ligase function of the von Hippel-Lindau protein

Nature Genetics

Volumn 35, Issue 3, 2003, Pages 229-237

  Corn, Paul G ^a   McDonald III, E Robert ^a   Herman, James G ^b   El Deiry, Wafik S ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b JOHNS HOPKINS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BINDING PROTEIN; HYPOXIA INDUCIBLE FACTOR 1ALPHA; PROTEASOME; PROTEIN SUBUNIT; RNA; SMALL INTERFERING RNA; TAT BINDING PROTEIN 1; TRANSACTIVATOR PROTEIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG; VON HIPPEL LINDAU PROTEIN;

ARTICLE; GENE DISRUPTION; GENE INACTIVATION; GENE MUTATION; GENE SILENCING; GENETIC PREDISPOSITION; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; TARGET CELL; TUMOR SUPPRESSOR GENE; VON HIPPEL LINDAU DISEASE;

BASE SEQUENCE; DNA-BINDING PROTEINS; HUMANS; HYDROLYSIS; HYPOXIA-INDUCIBLE FACTOR 1, ALPHA SUBUNIT; MOLECULAR SEQUENCE DATA; PEPTIDE HYDROLASES; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN BINDING; RNA, SMALL INTERFERING; TRANSCRIPTION FACTORS; TUMOR SUPPRESSOR PROTEINS; UBIQUITIN-PROTEIN LIGASES; VON HIPPEL-LINDAU TUMOR SUPPRESSOR PROTEIN;

EID: 0242298321     PISSN: 10614036     EISSN: None     Source Type: Journal    
DOI: 10.1038/ng1254     Document Type: Article

References (38)

1. Kaelin, W.G. Jr. Molecular basis of the VHL hereditary cancer syndrome. Nat. Rev. Cancer 2, 673-682 (2002).
2. Herman, J.G. et al. Silencing of the VHL tumor-suppressor gene by DNA methylation in renal carcinoma. Proc. Natl. Acad. Sci. USA 91, 9700-9704 (1994).
3. Maxwell, P.H. et al. The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis. Nature 399, 271-275 (1999).
4. Ohh, M. et al. Ubiquitination of hypoxia-inducible factor requires direct binding to the beta-domain of the von Hippel-Lindau protein. Nat. Cell Biol. 2, 423-427 (2000).
5. Stebbins, C.E., Kaelin, W.G. Jr. & Pavletich, N.P. Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function. Science 284, 455-461 (1999).
6. Kamura, T., Conrad, M.N., Yan, Q., Conaway, R.C. & Conaway, J.W. The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2. Genes Dev. 13, 2928-2933 (1999).
7. Semenza, G.L. HIF-1 and human disease: one highly involved factor. Genes Dev. 14, 1983-1991 (2000).
8. Ivan, M. et al. HIFα targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing. Science 292, 464-468 (2001).
9. 2-regulated prolyl hydroxylation. Science 292, 468-472 (2001).
10. Bruick, R.K. & McKnight, S.L. A conserved family of prolyl-4-hydroxylases that modify HIF. Science 294, 2 1337-1340 (2001).
11. Epstein, A.C.R. et al. C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 107, 43-54 (2001).
12. Gnarra, J.R. et al. Molecular cloning of the von Hippel-Lindau tumor suppressor gene and its role in renal carcinoma. Biochim. Biophys. Acta 1242, 201-210 (1996).
13. Clifford, S.C. et al. Contrasting effects on HIF-1α regulation by disease-causing pVHL mutations correlate with patterns of tumourigenesis in von Hippel-Lindau disease. Hum. Mol. Genet. 10, 1029-1038 (2001).
14. Hoffman, M.A. et al. von Hippel-Lindau protein mutants linked to type 2C VHL disease preserve the ability to downregulate HIF. Hum. Mol. Genet. 10, 1019-1027 (2001).
15. 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. 5, 64-70 (2003).
16. Ohh, M. et al. The von Hippel-Lindau tumor suppressor protein is required for proper assembly of an extracellular fibronectin matrix. Mol. Cell 1, 959-968 (1998).
17. DeMartino, G.N. et al. Identification, purification, and characterization of a PA700-dependent activator of the proteasome. J. Biol. Chem. 271, 3112-3118 (1996).
18. Nakamura, T., Tanaka, T., Takagi, H. & Sato, M. Cloning and heterogeneous in vivo expression of Tat binding protein-1 (TBP-1) in the mouse. Biochim. Biophys. Acta 1399, 93-100 (1998).
19. Hoyle, J., Tan, K.H. & Fisher, E.M. Localization of genes encoding two human one-domain members of the AAA family: PSMC5 (the thyroid hormone receptor-interacting protein, TRIP1) and PSMC3 (the Tat-binding protein, TBP1). Hum. Genet. 99, 285-288 (1997).
20. Braun, B.C. et al. The base of the proteasome regulatory particle exhibits chaperone-like activity. Nat. Cell Biol. 1, 221-226 (1999).
21. Ferrell, K., Wilkinson, C.R., Dubiel, W. & Gordon, C. Regulatory subunit interactions of the 26S proteasome, a complex problem. Trends Biochem. Sci. 25, 83-88 (2000).
22. 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-induced changes. J. Biol. Chem. 272, 22642-22647 (1997).
23. Rubin, D.M., Glickman, M.H., Larsen, C.N., Dhruvakumar, S. & Finley, D. Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome. EMBO J. 17, 4909-4919 (1998).
24. Sung, P., Higgins, D., Prakash, L. & Prakash, S. Mutation of lysine-48 to arginine in the yeast RAD3 protein abolishes its ATPase and DNA helicase activities but not the ability to bind ATP. EMBO J. 7, 3263-3269 (1988).
25. Honda, R., Tanaka, H. & Yasuda, H. Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53. FEBS Lett. 420, 25-27 (1997).
26. Strohmaier, H. et al. Human F-box protein hCdc4 targets cyclin E for proteolysis and is mutated in a breast cancer cell line. Nature 413, 316-322 (2001).
27. Sudakin, V. et al. The cyclosome, a large complex containing cyclin-selective ubiquitin ligase activity, targets cyclins for destruction at the end of mitosis. Mol. Biol. Cell 6, 185-197 (1995).
28. Zachariae, W., Shin, T.H., Galova, M., Obermaier, B. & Nasmyth, K. Identification of subunits of the anaphase-promoting complex of Saccharomyces cerevisiae. Science 274, 1201-1204 (1996).
29. Gnarra, J.R. et al. Mutations of the VHL tumour suppressor gene in renal carcinoma. Nat. Genet. 7, 85-90 (1994).
30. Whaley, J.M. et al. Germ-line mutations in the von Hippel-Lindau tumor-suppressor gene are similar to somatic von Hippel-Lindau aberrations in sporadic renal cell carcinoma. Am. J. Hum. Mol. Genet. 55, 1092-1102 (1994).
31. Crossey, P.A. et al. Identification of intragenic mutations in the von Hippel-Lindau disease tumour suppressor gene and correlation with disease phenotype. Hum. Mol. Genet. 3, 1303-1308 (1994).
32. Hon, W.C. et al. Structural basis for the recognition of hydroxyproline in HIF-1α by pVHL. Nature 417, 975-978 (2002).
33. Liu, C.W. et al. Conformational remodeling of proteasomal substrates by PA700, the 19S regulatory complex of the 26S proteasome. J. Biol. Chem. 277, 26815-26820 (2002).
34. Xie, Y. & Varshavsky, A. UFD4 lacking the proteasome-binding region catalyses ubiquitination but is impaired in proteolysis. Nat. Cell Biol. 4, 1003-1007 (2002).
35. Iliopoulos, O. et al. Negative regulation of hypoxia-inducible genes by the von Hippel-Lindau protein. Proc. Natl. Acad. Sci. USA 93, 10595-10599 (1996).
36. He, T.C. et al. A simplified system for generating recombinant adenoviruses. Proc. Natl. Acad. Sci. USA 95, 2509-2514 (1998).
37. Gardner, L.B. et al. Hypoxia inhibits G1/S transition through regulation of p27 expression. J. Biol. Chem. 276, 7919-7926 (2001).
38. Elbashir, S.M. et al. Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature 411, 494-498 (2001).