Structure of native oligomeric Sprouty2 by electron microscopy and its property of electroconductivity

Biochemical and Biophysical Research Communications

Volumn 439, Issue 3, 2013, Pages 351-356

  Chen, Feng Jung ^a,b   Lee, Kuan Wei ^a   Lai, Chun Chieh ^a   Lee, Sue Ping ^c   Shen, Hsiao Hsuian ^a   Tsai, Shu Ping ^c   Liu, Bang Hung ^a   Wang, Ling Mei ^d   Liou, Gunn Guang ^a,e  

^a NATIONAL HEALTH RESEARCH INSTITUTES   (Taiwan)

^b NATIONAL CHIAO TUNG UNIVERSITY   (Taiwan)

^c INSTITUTE OF MOLECULAR BIOLOGY   (Taiwan)

^d INDUSTRIAL TECHNOLOGY RESEARCH INSTITUTE   (Taiwan)

^e CHINA MEDICAL UNIVERSITY   (Taiwan)

Author keywords

BIAcore surface plasmon resonance (BIAcore SPR); Electroconductivity; Electron microscopy single particle reconstruction (EM SPR); Energy dispersive spectrum (EDS); Sprouty2 (Spry2)

Indexed keywords

OLIGOMER; SILICON; SPROUTY PROTEIN; SPROUTY2 PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL STRUCTURE; CONTROLLED STUDY; DISPERSION; ELECTRIC RESISTANCE; ELECTRON MICROSCOPY; ENERGY; ENERGY TRANSFER; NONHUMAN; PRIORITY JOURNAL; SIGNAL TRANSDUCTION; SURFACE PLASMON RESONANCE;

BIACORE SURFACE PLASMON RESONANCE (BIACORE SPR); ELECTROCONDUCTIVITY; ELECTRON MICROSCOPY SINGLE PARTICLE RECONSTRUCTION (EM SPR); ENERGY DISPERSIVE SPECTRUM (EDS); SPROUTY2 (SPRY2);

ANIMALS; ELECTRIC CONDUCTIVITY; HUMANS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; IRON; MEMBRANE PROTEINS; MICROSCOPY, ELECTRON; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SILICON;

EID: 84884588983     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.08.083     Document Type: Article

References (28)

1. Bache K.G., Slagsvold T., Stenmark H. Defective downregulation of receptor tyrosine kinases in cancer. EMBO J. 2004, 23:2707-2712.
2. Haglund K., Di Fiore P.P., Dilic I. Distinct monoubiquitin signals in receptor endocytosis. Trends Biochem. Sci. 2003, 28:598-603.
3. Haglund K., Sigismund S., Szymkiewicz I., Di Fiore P.P., Dikic I. Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation. Nat. Cell Biol. 2003, 5:461-466.
4. Ishida M., Ichihara M., Mii S., Jijiwa M., Asai N., Enomoto A., Kato T., Majima A., Ping J., Murakumo Y., Takahashi M. Sprouty2 regulates growth and differentiation of human neuroblastoma cells through RET tyrosine kinase. Cancer Sci. 2007, 98:815-821.
5. Mason J.M., Morrison D.J., Basson M.A., Licht J.D. Sprouty protein: multifaceted negative-feedback regulators of receptor tyrosine kinase signaling. Trends Cell Biol. 2006, 16:45-54.
6. Schiller M.R. Coupling receptor tyrosine kinases to Rho GTPaess-GEFs what's the link. Cell Signal. 2006, 18:1834-1843.
7. Schreiber S.L., Bernstein B.E. Signaling network model of chromatin. Cell 2002, 111:771-778.
8. McKay M.M., Morrison D.K. Integrating signals from RTKs to ERK/MAPK. Oncogene 2007, 26:3113-3121.
9. Mason J.M., Morrison D.J., Bassit B., Dimri M., Band H., Licht J.D., Gross I. Tyrosin phosphorylation of Sprouty proteins regulates their ability to inhibit growth factor signaling: a dual feedback loop. Mol. Bio. Cell 2004, 15:2176-2188.
10. Wong E.S., Lim J., Low B.C., Chen Q., Guy G.R. Evidence for direct interaction between Sprouty and Cbl. J. Biol. Chem. 2001, 276:5866-5875.
11. Haglund K., Schmide M.H., Wong E.S., Guy G.R., Dikic I. Sprouty2 acts at the Cbl/CIN85 interface to inhibit epidermal growth factor receptor downregulation. EMBO Rep. 2005, 6:635-641.
12. Hall A.B., Jura N., DaSilva J., Jang Y.J., Gong D., Bar-Sagi D. HSpry2 is targeted to the ubiquitin-dependent proteasome pathway by c-Cbl. Curr. Biol. 2003, 13:308-314.
13. Mason J.M., Morrison D.J., Bassit B., Dimri M., Band H., Licht J.D., Gross I. Tyrosine phosphorylation of Sprouty proteins regulates their ability to inhibit growth factor signaling: a dual feedback loop. Mol. Biol. Cell 2004, 15:2176-2188.
14. Nadeau R.J., Toher J.L., Yang X., Kovalenko D., Friesel R. Regulation of Sprouty2 stability by mammalian seven-in-absentia homolog 2. J. Cell. Biochem. 2007, 100:151-160.
15. Qi J., Nakayama K., Gaitonde S., Goydos J.S., Krajewski S., Eroshkin A., Bar-Sagi D., Bowtell D., Ronai Z. The ubiquitin ligase Siah2 regulates tumorigenesis and metastasis by HIF-dependent and -independent pathways. Proc. Natl. Acad. Sci. USA 2008, 105:16713-16718.
16. Edwin F., Anderson K., Patel T.B. HECT domain-containing E3 ubiquitin ligase Nedd4 interacts with and ubiquitinates Sprouty2. J. Biol. Chem. 2010, 285:255-264.
17. Minowada G., Jarvis L.A., Chi C.L., Neubuser A., Sun X., Hacohen N., Krasnow M.A., Martin G.R. Vertebrate Sprouty genes are induced by FGF signaling and can cause chondrodysplasia when overexpressed. Development 1999, 126:4465-4475.
18. McKie A.B., Douglas D.A., Olijslagers S., Graham J., Omar M.M., Heer R., Gnanapragasam V.J., Robson C.N., Leung H.Y. Epigenetic inactivation of the human sprouty2 (hSPRY2) homologue in prostate cancer. Oncogene 2005, 24:2166-2174.
19. Frank M.J., Dawson D.W., Bensinger S.J., Hong J.S., Knosp W.M., Xu L., Balatoni C.E., Allen E.L., Shen R.R., Bar-Sagi D., Martin G.R., Teitell M.A. Expression of sprouty2 inhibits B-cell proliferation and is epigenetically silenced in mouse and human B-cell lymphomas. Blood 2009, 113:2478-2487.
20. Liou G.-G., Tanny J.C., Kruger R.G., Walz T., Moazed D. Assembly of the SIR complex and its regulation by o-acetyl-ADP-ribose, a product of NAD-dependent histone deacetylation. Cell 2005, 121:515-527.
21. Radermacher M., Wagenknecht T., Verschoor A., Frank F. Three-dimensional reconstruction from a single-exposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli. J. Microsc. 1987, 146:113-136.
22. Frank F., Radermacher M., Penczek P., Zhu J., Li Y., Ladjadj M., Leith A. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 1996, 116:190-199.
23. Wu X., Alexander P.B., He Y., Kikkawa M., Vogel P.D., McKnight S.L. Mammalin sprout proteins assemble into large monodisperse particles having the properties of intracellular nanobatteries. Proc. Natl. Acad. Sci. USA 2005, 102:14058-14062.
24. Ma J.F., Tamai K., Yamaji N., Mitani N., Konishi S., Katsuhara M., Ishiguro M., Murata Y., Yano M. A silicon transporter in rice. Nature 2006, 440:688-691.
25. Ma J.F., Yamaji N., Mitani N., Tamai K., Konishi S., Fujiwara T., Katsuhara M., Yano M. An efflux transporter of silicon in rice. Nature 2007, 448:209-212.
26. Chiba Y., Mitani N., Yamaji N., Ma J.F. HvLsi1 is a silicon influx transporter in barley. Plant J. 2009, 57:810-818.
27. Mitani N., Chiba Y., Yamaji N., Ma J.F. Identification and characterization of maize and barley Lsi2-Like silicon efflux transporters reveals a distinct silicon uptake system from that in rice. Plant Cell 2009, 21:2133-2142.
28. Mitani N., Yamaji N., Ago Y., Iwasaki K., Ma J.F. Isolation and functional characterization of an influx silicon transporter in two pumpkin cultivars contrasting in silicon accumulation. Plant J. 2011, 66:231-240.