The Hedgehog-inducible ubiquitin ligase subunit WSB-1 modulates thyroid hormone activation and PTHrP secretion in the developing growth plate

Nature Cell Biology

Volumn 7, Issue 7, 2005, Pages 698-705

  Dentice, Monica ^a   Bandyopadhyay, Amitabha ^b   Gereben, Balázs ^c   Callebaut, Isabelle ^d   Christoffolete, Marcelo A ^a   Kim, Brian W ^a   Nissim, Sahar ^b   Mornon, Jean Paul ^d   Zavacki, Ann Marie ^a   Zeöld, Anikó ^c   Capelo, Luciane P ^a   Curcio Morelli, Cyntia ^a   Ribeiro, Rogério ^a   Harney, John W ^a   Tabin, Clifford J ^b   Bianco, Antonio C ^a  

^a BRIGHAM AND WOMEN S HOSPITAL   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

^c INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

^d SORBONNE UNIVERSITÉ   (France)

Author keywords

[No Author keywords available]

Indexed keywords

PARATHYROID HORMONE RELATED PROTEIN; SONIC HEDGEHOG PROTEIN; SUPPRESSOR OF CYTOKINE SIGNALING; THYROXINE DEIODINASE; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; WSB 1 PROTEIN;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; BONE DEVELOPMENT; CARTILAGE CELL; CATALYSIS; CELL DIFFERENTIATION; CHICK EMBRYO; COMPLEX FORMATION; CONTROLLED STUDY; EMBRYO; EMBRYO DEVELOPMENT; EMBRYONIC STRUCTURES; ENZYME SUBUNIT; GROWTH PLATE; HORMONE ACTION; METABOLIC DISORDER; MODULATION; MOLECULAR INTERACTION; MOLECULAR RECOGNITION; NEGATIVE FEEDBACK; NONHUMAN; PRIORITY JOURNAL; PROTEIN SECRETION; REGULATORY MECHANISM; SIGNAL TRANSDUCTION; TIBIA; UBIQUITINATION;

AMINO ACID SEQUENCE; ANIMALS; BETA-TRANSDUCIN REPEAT-CONTAINING PROTEINS; BINDING SITES; CELL DIFFERENTIATION; CHICK EMBRYO; CHONDROCYTES; GENE EXPRESSION; GROWTH PLATE; HEDGEHOG PROTEINS; HUMANS; IMMUNOPRECIPITATION; IN SITU HYBRIDIZATION; IODIDE PEROXIDASE; MICE; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PARATHYROID HORMONE-RELATED PROTEIN; PROTEIN BINDING; PROTEIN SUBUNITS; PROTEINS; RNA INTERFERENCE; SEQUENCE HOMOLOGY, AMINO ACID; THYROID HORMONES; TIBIA; TRANS-ACTIVATORS; TRANSCRIPTION FACTORS; TRANSFECTION; TWO-HYBRID SYSTEM TECHNIQUES; UBIQUITIN; UBIQUITIN-PROTEIN LIGASES;

ANIMALIA; ERINACEIDAE;

EID: 22144499549     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb1272     Document Type: Article

References (35)

1. Bianco, A. C., Salvatore, D., Gereben, B., Berry, M. J. & Larsen, P. R. Biochemistry, cellular and molecular biology and physiological roles of the iodothyronine selenodeiodinases. Endocr. Rev. 23, 38-89 (2002).
2. Weissman, A. M. Themes and variations on ubiquitylation. Nature Rev. Mol. Cell Biol. 2, 169-178 (2001).
3. Hampton, R. Y. ER-associated degradation in protein quality control and cellular regulation. Curr. Opin. Cell Biol. 14, 476-482 (2002).
4. Steinsapir, J., Harney, J. & Larsen, P. R. Type 2 iodothyronine deiodinase in rat pituitary tumor cells is inactivated in proteasomes. J. Clin. Invest. 102, 1895-1899 (1998).
5. Gereben, B., Goncalves, C., Harney, J. W., Larsen, P. R. & Bianco, A. C. Selective proteolysis of human type 2 deiodinase: a novel ubiquitin-proteasomal mediated mechanism for regulation of hormone activation. Mol. Endocrinol. 14, 1697-1708 (2000).
6. Curcio-Morelli, C. et al. Deubiquitination of type 2 iodothyronine deiodinase by pVHL-interacting deubiquitinating enzymes regulates thyroid hormone activation. J. Clin. Invest. 112, 189-196 (2003).
7. Hilton, D. J. et al. Twenty proteins containing a C-terminal SOCS box form five structural classes. Proc. Natl Acad. Sci. USA 95, 114-119 (1998).
8. Vasiliauskas, D., Hancock, S. & Stern, C. D. SWiP-1: novel SOCS box containing WD-protein regulated by signalling centres and by Shh during development. Mech. Dev. 82, 79-94 (1999).
9. Callebaut, I. et al. Deciphering protein sequence information through hydrophobic cluster analysis (HCA): current status and perspectives. Cell. Mol. Life Sci. 53, 621-645 (1997).
10. Orlicky, S., Tang, X., Wiliems, A., Tyers, M. & Sicheri, F. Structural basis for phosphodependent substrate selection and orientation by the SCFCdc4 ubiquitin ligase. Cell 112, 243-256 (2003).
11. Maniatis, T. A ubiquitin ligase complex essential for the NF-κB, Wnt/Wingless, and Hedgehog signaling pathways. Genes Dev. 13, 505-510 (1999).
12. 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).
13. Schulman, B. A. et al. Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2 complex. Nature 408, 381-386 (2000).
14. Kamura, T. et al. 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. Genes Dev. 12, 3872-3881 (1998).
15. Solomon, V., Lecker, S. H. & Goldberg, A. L. The N-end rule pathway catalyzes a major fraction of the protein degradation in skeletal muscle. J. Biol. Chem. 273, 25216-25222 (1998).
16. Kamura, T. et al. Muf1, a novel Elongin BC-interacting leucine-rich repeat protein that can assemble with Cul5 and Rbx1 to reconstitute a ubiquitin ligase. J. Biol. Chem. 276, 29748-29753 (2001).
17. Zheng, N. et al. Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex. Nature 416, 703-709 (2002).
18. Hamilton, K. S., Ellison, M. J. & Shaw, G. S. Identification of the ubiquitin interfacial residues in a ubiquitin-E2 covalent complex. J. Biomol. NMR 18, 319-327 (2000).
19. Min, J. H. et al. Structure of an HIF-1α-pVHL complex: hydroxyproline recognition in signaling. Science 296, 1886-1889 (2002).
20. Wu, G. et al. Structure of a β-TrCP1-Skp1-β-catenin complex: destruction motif binding and lysine specificity of the SCF(β-TrCP1) ubiquitin ligase. Mol. Cell 11, 1445-1456 (2003).
21. Zheng, N., Wang, P., Jeffrey, P. D. & Pavletich, N. P. Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases. Cell 102, 533-539 (2000).
22. Cook, W. J., Martin, P. D., Edwards, B. F., Yamazaki, R. K. & Chau, V. Crystal structure of a class I ubiquitin conjugating enzyme (Ubc7) from Saccharomyces cerevisiae at 2.9 angstroms resolution. Biochemistry 36, 1621-1627 (1997).
23. Biederer, T., Volkwein, C. & Sommer, T. Role of Cue1p in ubiquitination and degradation at the ER surface Science 278, 1806-1809 (1997).
24. Sommer, T. & Jentsch, S. A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum. Nature 365, 176-179 (1993).
25. Kim, B. W. et al. ER-associated degradation of the human type 2 iodothyronine deiodinase (D2) is mediated via an association between mammalian UBC7 and the carboxyl region of D2. Mol. Endocrinol. 17, 2603-2612 (2003).
26. Botero, D. et al. Ubc6p and Ubc7p are required for normal and substrate-induced endoplasmic reticulum-associated degradation of the human selenoprotein type 2 iodothyronine monodeiodinase. Mol. Endocrinol. 16, 1999-2007 (2002).
27. Callebaut, I. et al. The iodothyronine selenodeiodinases are thioredoxin-fold family proteins containing a glycoside hydrolase-clan GH-A-like structure. J. Biol. Chem. 278, 36887-36896 (2003).
28. Curcio-Morelli, C. et al. In vivo dimerization of types 1, 2, and 3 iodothyronine selenodeiodinases. Endocrinology 144, 3438-3443 (2003).
29. Kronenberg, H. M. Developmental regulation of the growth plate. Nature 423, 332-336 (2003).
30. Vortkamp, A. et al. Regulation of rate of cartilage differentiation by Indian hedgehog and PTH-related protein. Science 273, 613-622 (1996).
31. St-Jacques, B., Hammerschmidt, M. & McMahon, A. P. Indian hedgehog signaling regulates proliferation and differentiation of chondrocytes and is essential for bone formation. Genes Dev. 13, 2072-2086 (1999).
32. Long, F., Zhang, X. M., Karp, S., Yang, Y. & McMahon, A. P. Genetic manipulation of hedgehog signaling in the endochondral skeleton reveals a direct role in the regulation of chondrocyte proliferation. Development 128, 5099-5108 (2001).
33. Stevens, D. A. et al. Thyroid hormones regulate hypertrophic chondrocyte differentiation and expression of parathyroid hormone-related peptide and its receptor during endochondral bone formation. J. Bone Miner. Res. 15, 2431-2442 (2000).
34. Robson, H., Siebler, T., Stevens, D. A., Shalet, S. M. & Williams, G. R. Thyroid hormone acts directly on growth plate chondrocytes to promote hypertrophic differentiation and inhibit clonal expansion and cell proliferation. Endocrinology 141, 3887-3897 (2000).
35. Boussif, O. et al. A versatile vector for gene and oligonucleotide transfer into cells in culture and in vivo: polyethylenimine. Proc. Natl Acad. Sci. USA 92, 7297-7301 (1995).