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Science 8 September 1995:
Vol. 269. no. 5229, pp. 1444 - 1446
DOI: 10.1126/science.7660130
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Articles

Science, Vol 269, Issue 5229, 1444-1446
Copyright © 1995 by American Association for the Advancement of Science

articles

Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C

A Kibel, O Iliopoulos, JA DeCaprio, and WG Kaelin Jr

Dana-Farber Cancer Institute, Boston, MA 02115, USA.

Germ-line mutations of the von Hippel-Lindau tumor suppressor gene (VHL) predispose individuals to a variety of human tumors, and somatic mutations of this gene have been identified in sporadic renal cell carcinomas and cerebellar hemangioblastomas. Two transcriptional elongation factors, Elongin B and C, were shown to bind in vitro and in vivo to a short, colinear region of the VHL protein (pVHL) that is frequently mutated in human tumors. A peptide replica of this region inhibited binding of pVHL to Elongin B and C whereas a point-mutant derivative, corresponding to a naturally occurring VHL missense mutation, had no effect. These results suggest that the tumor suppression function of pVHL may be linked to its ability to bind to Elongin B and C.


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Regulation of Gene Expression by the Hypoxia-Inducible Factors.
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Genotype-phenotype correlation in von Hippel-Lindau syndrome.
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Vascular tumors in livers with targeted inactivation of the von Hippel-Lindau tumor suppressor.
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Role of chromosome 3p12-p21 tumour suppressor genes in clear cell renal cell carcinoma: analysis of VHL dependent and VHL independent pathways of tumorigenesis.
A Martinez, P Fullwood, K Kondo, T Kishida, M Yao, E R Maher, and F Latif (2000)
Mol. Pathol. 53, 137-144
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Elongin from Saccharomyces cerevisiae.
C. M. Koth, M. V. Botuyan, R. J. Moreland, D. B. Jansma, J. W. Conaway, R. C. Conaway, W. J. Chazin, J. D. Friesen, C. H. Arrowsmith, and A. M. Edwards (2000)
J. Biol. Chem. 275, 11174-11180
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VHL Alterations in Human Clear Cell Renal Cell Carcinoma: Association with Advanced Tumor Stage and a Novel Hot Spot Mutation.
H. Brauch, G. Weirich, J. Brieger, D. Glavac, H. Rödl, M. Eichinger, M. Feurer, E. Weidt, C. Puranakanitstha, C. Neuhaus, et al. (2000)
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A. D. Perera, E. V. Kleymenova, and C. L. Walker (2000)
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Identification and Characterization of Elongin A2, a New Member of the Elongin Family of Transcription Elongation Factors, Specifically Expressed in the Testis.
T. Aso, K. Yamazaki, K. Amimoto, A. Kuroiwa, H. Higashi, Y. Matsuda, S. Kitajima, and M. Hatakeyama (2000)
J. Biol. Chem. 275, 6546-6552
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Identification of the von Hippel-Lindau tumor-suppressor protein as part of an active E3 ubiquitin ligase complex.
K. Iwai, K. Yamanaka, T. Kamura, N. Minato, R. C. Conaway, J. W. Conaway, R. D. Klausner, and A. Pause (1999)
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von Hippel-Lindau Protein Induces Hypoxia-regulated Arrest of Tyrosine Hydroxylase Transcript Elongation in Pheochromocytoma Cells.
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M. V. Botuyan, C. M. Koth, G. Mer, A. Chakrabartty, J. W. Conaway, R. C. Conaway, A. M. Edwards, C. H. Arrowsmith, and W. J. Chazin (1999)
PNAS 96, 9033-9038
   Abstract »    Full Text »    PDF »
The von Hippel-Lindau tumor suppressor protein is a component of an E3 ubiquitin-protein ligase activity.
J. Lisztwan, G. Imbert, C. Wirbelauer, M. Gstaiger, and W. Krek (1999)
Genes & Dev. 13, 1822-1833
   Abstract »    Full Text »
Physical Interaction and Functional Antagonism between the RNA Polymerase II Elongation Factor ELL and p53.
N. Shinobu, T. Maeda, T. Aso, T. Ito, T. Kondo, K. Koike, and M. Hatakeyama (1999)
J. Biol. Chem. 274, 17003-17010
   Abstract »    Full Text »    PDF »
Conjugation of the ubiquitin-like protein NEDD8 to cullin-2 is linked to von Hippel-Lindau tumor suppressor function.
D. Liakopoulos, T. Busgen, A. Brychzy, S. Jentsch, and A. Pause (1999)
PNAS 96, 5510-5515
   Abstract »    Full Text »    PDF »
The Elongin B Ubiquitin Homology Domain. IDENTIFICATION OF ELONGIN B SEQUENCES IMPORTANT FOR INTERACTION WITH ELONGIN C.
C. S. Brower, A. Shilatifard, T. Mather, T. Kamura, Y. Takagi, D. Haque, A. Treharne, S. I. Foundling, J. W. Conaway, and R. C. Conaway (1999)
J. Biol. Chem. 274, 13629-13636
   Abstract »    Full Text »    PDF »
The conserved SOCS box motif in suppressors of cytokine signaling binds to elongins B and C and may couple bound proteins to proteasomal degradation.
J.-G. Zhang, A. Farley, S. E. Nicholson, T. A. Willson, L. M. Zugaro, R. J. Simpson, R. L. Moritz, D. Cary, R. Richardson, G. Hausmann, et al. (1999)
PNAS 96, 2071-2076
   Abstract »    Full Text »    PDF »
Protective Function of von Hippel-Lindau Protein against Impaired Protein Processing in Renal Carcinoma Cells.
M. Gorospe, J. M. Egan, B. Zbar, M. Lerman, L. Geil, I. Kuzmin, and N. J. Holbrook (1999)
Mol. Cell. Biol. 19, 1289-1300
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Transcription-Dependent Nuclear-Cytoplasmic Trafficking Is Required for the Function of the von Hippel-Lindau Tumor Suppressor Protein.
S. Lee, M. Neumann, R. Stearman, R. Stauber, A. Pause, G. N. Pavlakis, and R. D. Klausner (1999)
Mol. Cell. Biol. 19, 1486-1497
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The Elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras, WD-40 repeat, and ankyrin repeat families.
T. Kamura, S. Sato, D. Haque, L. Liu, W. G. Kaelin Jr., R. C. Conaway, and J. W. Conaway (1998)
Genes & Dev. 12, 3872-3881
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Down-regulation of transmembrane carbonic anhydrases in renal cell carcinoma cell lines by wild-type von Hippel-Lindau transgenes.
S. V. Ivanov, I. Kuzmin, M.-H. Wei, S. Pack, L. Geil, B. E. Johnson, E. J. Stanbridge, and M. I. Lerman (1998)
PNAS 95, 12596-12601
   Abstract »    Full Text »    PDF »
Mechanism of Action of RNA Polymerase II Elongation Factor Elongin. MAXIMAL STIMULATION OF ELONGATION REQUIRES CONVERSION OF THE EARLY ELONGATION COMPLEX TO AN ELONGIN-ACTIVABLE FORM.
R. J. Moreland, J. S. Hanas, J. W. Conaway, and R. C. Conaway (1998)
J. Biol. Chem. 273, 26610-26617
   Abstract »    Full Text »    PDF »
pVHL19 is a biologically active product of the von Hippel-Lindau gene arising from internal translation initiation.
O. Iliopoulos, M. Ohh, and W. G. Kaelin Jr. (1998)
PNAS 95, 11661-11666
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A second major native von Hippel-Lindau gene product, initiated from an internal translation start site, functions as a tumor suppressor.
A. Schoenfeld, E. J. Davidowitz, and R. D. Burk (1998)
PNAS 95, 8817-8822
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Up-Regulation of Vascular Endothelial Growth Factor in Stromal Cells of Hemangioblastomas Is Correlated with Up-Regulation of the Transcription Factor HRF/HIF-2{alpha}.
I. Flamme, M. Krieg, and K. H. Plate (1998)
Am. J. Pathol. 153, 25-29
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Overexpression of the MEN/ELL Protein, an RNA Polymerase II Elongation Factor, Results in Transformation of Rat1 Cells with Dependence on the Lysine-rich Region.
Y. Kanda, K. Mitani, M. Kurokawa, T. Yamagata, Y. Yazaki, and H. Hirai (1998)
J. Biol. Chem. 273, 5248-5252
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The von Hippel-Lindau tumor suppressor gene is required for cell cycle exit upon serum withdrawal.
A. Pause, S. Lee, K. M. Lonergan, and R. D. Klausner (1998)
PNAS 95, 993-998
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Regulation of Hypoxia-Inducible mRNAs by the von Hippel-Lindau Tumor Suppressor Protein Requires Binding to Complexes Containing Elongins B/C and Cul2.
K. M. Lonergan, O. Iliopoulos, M. Ohh, T. Kamura, R. C. Conaway, J. W. Conaway, and W. G. Kaelin Jr. (1998)
Mol. Cell. Biol. 18, 732-741
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Identification of Elongin C Sequences Required for Interaction with the von Hippel-Lindau Tumor Suppressor Protein.
Y. Takagi, A. Pause, R. C. Conaway, and J. W. Conaway (1997)
J. Biol. Chem. 272, 27444-27449
   Abstract »    Full Text »    PDF »


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