hSpry2 is targeted to the ubiquitin-dependent proteasome pathway by c-Cbl

Current Biology

Volumn 13, Issue 4, 2003, Pages 308-314

  Hall, Amy B ^a,b   Jura, Natalia ^a   DaSilva, John ^a   Jang, Yeon Joo ^a   Gong, Delquin ^a   Bar Sagi, Dafna ^a  

^a STONY BROOK UNIVERSITY   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CBL PROTEIN; CBL PROTEIN, HUMAN; CYSTEINE PROTEINASE; MULTIENZYME COMPLEX; NERVE PROTEIN; ONCOPROTEIN; PROTEASOME; SPRY2 PROTEIN, RAT; TYROSINE; UBIQUITIN; UBIQUITIN PROTEIN LIGASE;

ANIMAL; ARTICLE; HUMAN; METABOLISM; PHOSPHORYLATION;

ANIMALS; CYSTEINE ENDOPEPTIDASES; HUMANS; MULTIENZYME COMPLEXES; NERVE TISSUE PROTEINS; PHOSPHORYLATION; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTO-ONCOGENE PROTEINS; PROTO-ONCOGENE PROTEINS C-CBL; TYROSINE; UBIQUITIN; UBIQUITIN-PROTEIN LIGASES;

ANIMALIA; VERTEBRATA;

EID: 0037452567     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(03)00086-1     Document Type: Article

References (21)

1. Hacohen, N., Kramer, S., Sutherland, D., Hiromi, Y., and Krasnow, M.A. (1998). sprouty encodes a novel antagonist of FGF signaling that patterns apical branching of the Drosophila airways. Cell 92, 253-263.
2. Casci, T., Vinos, J., and Freeman, M. (1999). Sprouty, an intracellular inhibitor of Ras signaling. Cell 96, 655-665.
3. Minowada, G., Jarvis, L.A., Chi, C.L., Neubuser, A., Sun, X., Hacohen, N., Krasnow, M.A., and Martin, G.R. (1999). Vertebrate Sprouty genes are induced by FGF signaling and can cause chondrodysplasia when overexpressed. Development 126, 4465-4475.
4. Tefft, J.D., Lee, M., Smith, S., Leinwand, M., Zhao, J., Bringas, P., Jr., Crowe, D.L., and Warburton, D. (1999). Conserved function of mSpry-2, a murine homolog of Drosophila sprouty, which negatively modulates respiratory organogenesis. Curr. Biol. 9, 219-222.
5. Wong, E.S., Lim, J., Low, B.C., Chen, Q., and Guy, G.R. (2001). Evidence for direct interaction between Sprouty and Cbl. J. Biol. Chem. 276, 5866-5875.
6. Schlessinger, J. (2000). Cell signaling by receptor tyrosine kinases. Cell 103, 193-200.
7. Freeman, M. (2000). Feedback control of intercellular signalling in development. Nature 408, 313-319.
8. Levkowitz, G., Waterman, H., Zamir, E., Kam, Z., Oved, S., Langdon, W.Y., Beguinot, L., Geiger, B., and Yarden, Y. (1998). c-Cbl/ Sli-1 regulates endocytic sorting and ubiquitination of the epidermal growth factor receptor. Genes Dev. 12, 3663-3674.
9. Miyake, S., Lupher, M.L., Jr., Druker, B., and Band, H. (1998). The tyrosine kinase regulator Cbl enhances the ubiquitination and degradation of the platelet-derived growth factor receptor alpha. Proc. Natl. Acad. Sci. USA 95, 7927-7932.
10. Lee, P.S., Wang, Y., Dominguez, M.G., Yeung, Y.G., Murphy, M.A., Bowtell, D.D., and Stanley, E.R. (1999). The Cbl protooncoprotein stimulates CSF-1 receptor multiubiquitination and endocytosis, and attenuates macrophage proliferation. EMBO J. 18, 3616-3628.
11. Wong, E.S., Fong, C.W., Lim, J., Yusoff, P., Low, B.C., Langdon, W.Y., and Guy, G.R. (2002). Sprouty2 attenuates epidermal growth factor receptor ubiquitylation and endocytosis, and consequently enhances Ras/ERK signalling. EMBO J. 21, 4796-4808.
12. Egan, J., Hall, A., Yatsula, B., and Bar-Sagi, D. (2002). The bimodal regulation of epidermal growth factor signaling by human Sprouty proteins. Proc. Natl. Acad. Sci. USA 99, 6041-6046.
13. Sasaki, A., Taketomi, T., Wakioka, T., Kato, R., and Yoshimura, A. (2001). Identification of a dominant negative mutant of Sprouty that potentiates fibroblast growth factor- but not epidermal growth factor-induced ERK activation. J. Biol. Chem. 276, 36804-36808.
14. Bucci, C., Parton, R., Mather, I., Stunnenberg, H., Simons, K., Hoflack, B., and Zerial, M. (1992). The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway. Cell 70, 715-728.
15. Lim, J., Wong, E.S., Ong, S.H., Yusoff, P., Low, B.C., and Guy, G.R. (2000). Sprouty proteins are targeted to membrane ruffles upon growth factor receptor tyrosine kinase activation. Identification of a novel translocation domain. J. Biol. Chem. 275, 32837-32845.
16. Weissman, A.M. (2001). Themes and variations on ubiquitylation. Nat. Rev. Mol. Cell Biol. 2, 169-178.
17. Herbst, A., and Tansey, W. (2000). HAM: a new epitope-tag for in vivo protein labeling. Mol. Biol. Rep. 27, 203-208.
18. Jehn, B., Dittert, I., Beyer, S., von der Mark, K., and Bielke, W. (2002). c-Cbl binding and ubiquitin-dependent lysosomal degradation of membrane-associated Notch1. J. Biol. Chem. 277, 8033-8040.
19. Reich, A., Sapir, A., and Shilo, B. (1999). Sprouty is a general inhibitor of receptor tyrosine kinase signaling. Development 126, 4139-4147.
20. Impagnatiello, M., Weitzer, S., Gannon, G., Compagni, A., Cotten, M., and Christofori, G. (2001). Mammalian sprouty-1 and -2 are membrane-anchored phosphoprotein inhibitors of growth factor signaling in endothelial cells. J. Cell Biol. 152, 1087-1098.
21. Gross, I., Bassit, B., Benezra, M., and Licht, J.D. (2001). Mammalian sprouty proteins inhibit cell growth and differentiation by preventing ras activation. J. Biol. Chem. 276, 46460-46468.