Grb2 interacts with SGEF and antagonizes the ability of SGEF to enhance EGF-induced ERK1/2 activation

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• 作者：Hongtao Wang (1)
  Shanhu Li (1)
  Hailiang Li (1)
  Peng Wang (1)
  Fang Huang (1)
  Yali Zhao (1)
  Lan Yu (1)
  Guolan Luo (1)
  Xiaoqing Zhang (1)
  Jian Wang (1)
  Jianguang Zhou (1)
  
• 关键词：SGEF ; Grb2 ; EGF ; EGFR ; ERK1/2
• 刊名：Molecular and Cellular Biochemistry
• 出版年：2014
• 出版时间：April 2014
• 年：2014
• 卷：389
• 期：1-2
• 页码：239-247
• 全文大小：1,288 KB
• 参考文献：1. Jorissen RN, Walker F, Pouliot N, Garrett TP, Ward CW, Burgess AW (2003) Epidermal growth factor receptor: mechanisms of activation and signalling. Exp Cell Res 284:31鈥?3 CrossRef
  2. Herbst RS (2004) Review of epidermal growth factor receptor biology. Int J Radiat Oncol Biol Phys 59:21鈥?6 CrossRef
  3. Yarden Y, Sliwkowski MX (2001) Untangling the ErbB signalling network. Nat Rev Mol Cell Biol 2:127鈥?37 CrossRef
  4. Olayioye MA, Neve RM, Lane HA, Hynes NE (2000) The ErbB signaling network: receptor heterodimerization in development and cancer. EMBO J 19:3159鈥?167 CrossRef
  5. Schlessinger J (2000) Cell signaling by receptor tyrosine kinases. Cell 103:211鈥?25 CrossRef
  6. Batzer AG, Rotin D, Urena JM, Skolnik EY, Schlessinger J (1994) Hierarchy of binding sites for Grb2 and Shc on the epidermal growth factor receptor. Mol Cell Biol 14:5192鈥?201
  7. Chardin P, Camonis JH, Gale NW, van Aelst L, Schlessinger J, Wigler MH, Bar-Sagi D (1993) Human Sos1: a guanine nucleotide exchange factor for Ras that binds to GRB2. Science 260:1338鈥?343 CrossRef
  8. Li N, Batzer A, Daly R, Yajnik V, Skolnik E, Chardin P, Bar-Sagi D, Margolis B, Schlessinger J (1993) Guanine-nucleotide-releasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling. Nature 363:85鈥?8 CrossRef
  9. Robinson MJ, Cobb MH (1997) Mitogen-activated protein kinase pathways. Curr Opin Cell Biol 9:180鈥?86 CrossRef
  10. Wang H, Li S, Li H, Li C, Guan K, Luo G, Yu L, Wu R, Zhang X, Wang J, Zhou J (2013) SGEF enhances EGFR stability through delayed EGFR trafficking from early to late endosomes. Carcinogenesis 34:1976鈥?983 CrossRef
  11. Wang H, Wu R, Yu L, Wu F, Li S, Zhao Y, Li H, Luo G, Wang J, Zhou J (2012) SGEF is overexpressed in prostate cancer and contributes to prostate cancer progression. Oncol Rep 28:1468鈥?474
  12. van Buul JD, Allingham MJ, Samson T, Meller J, Boulter E, Garcia-Mata R, Burridge K (2007) RhoG regulates endothelial apical cup assembly downstream from ICAM1 engagement and is involved in leukocyte trans-endothelial migration. J Cell Biol 178:1279鈥?293 CrossRef
  13. Patel JC, Galan JE (2006) Differential activation and function of Rho GTPases during Salmonella-host cell interactions. J Cell Biol 175:453鈥?63 CrossRef
  14. Ellerbroek SM, Wennerberg K, Arthur WT, Dunty JM, Bowman DR, DeMali KA, Der C, Burridge K (2004) SGEF, a RhoG guanine nucleotide exchange factor that stimulates macropinocytosis. Mol Biol Cell 15:3309鈥?319 CrossRef
  15. Krishna Subbaiah V, Massimi P, Boon SS, Myers MP, Sharek L, Garcia-Mata R, Banks L (2012) The invasive capacity of HPV transformed cells requires the hDlg-dependent enhancement of SGEF/RhoG activity. PLoS Pathog 8:e1002543 CrossRef
  16. Yu H, Chen JK, Feng S, Dalgarno DC, Brauer AW, Schrelber SL (1994) Structural basis for the binding of proline-rich peptides to SH3 domains. Cell 76:933鈥?45 CrossRef
  17. Mebratu Y, Tesfaigzi Y (2009) How ERK1/2 activation controls cell proliferation and cell death: is subcellular localization the answer? Cell Cycle 8:1168鈥?175 CrossRef
  18. Kao S, Jaiswal RK, Kolch W, Landreth GE (2001) Identification of the mechanisms regulating the differential activation of the mapk cascade by epidermal growth factor and nerve growth factor in PC12 cells. J Biol Chem 276:18169鈥?8177 CrossRef
  19. Marshall CJ (1995) Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation. Cell 80:179鈥?85 CrossRef
  20. Wong ES, Fong CW, Lim J, Yusoff P, Low BC, Langdon WY, Guy GR (2002) Sprouty2 attenuates epidermal growth factor receptor ubiquitylation and endocytosis, and consequently enhances Ras/ERK signalling. EMBO J 21:4796鈥?808 CrossRef
  21. Traverse S, Seedorf K, Paterson H, Marshall CJ, Cohen P, Ullrich A (1994) EGF triggers neuronal differentiation of PC12 cells that overexpress the EGF receptor. Curr Biol 4:694鈥?01 CrossRef
  22. Haglund K, Schmidt MH, Wong ES, Guy GR, Dikic I (2005) Sprouty2 acts at the Cbl/CIN85 interface to inhibit epidermal growth factor receptor downregulation. EMBO Rep 6:635鈥?41 CrossRef
  23. Ren Y, Cheng L, Rong Z, Li Z, Li Y, Zhang X, Xiong S, Hu J, Fu XY, Chang Z (2008) hSef potentiates EGF-mediated MAPK signaling through affecting EGFR trafficking and degradation. Cell Signal 20:518鈥?33 CrossRef
  24. Gan Y, Shi C, Inge L, Hibner M, Balducci J, Huang Y (2010) Differential roles of ERK and Akt pathways in regulation of EGFR-mediated signaling and motility in prostate cancer cells. Oncogene 29:4947鈥?958 CrossRef
  25. Giubellino A, Burke TR Jr, Bottaro DP (2008) Grb2 signaling in cell motility and cancer. Expert Opin Ther Targets 12:1021鈥?033 CrossRef
  
• 作者单位：Hongtao Wang (1)
  Shanhu Li (1)
  Hailiang Li (1)
  Peng Wang (1)
  Fang Huang (1)
  Yali Zhao (1)
  Lan Yu (1)
  Guolan Luo (1)
  Xiaoqing Zhang (1)
  Jian Wang (1)
  Jianguang Zhou (1)
  
  1. Laboratory of Medical Molecular Biology, Beijing Institute of Biotechnology, 27 Taiping Road, Haidian, Beijing, 100850, People鈥檚 Republic of China
  
• ISSN：1573-4919

文摘

Previously, we demonstrated that SGEF enhances EGFR stability; however, SGEF-mediated downstream signaling of EGFR is not well understood. Here, we show that SGEF enhances EGF-induced ERK1/2 activation independent of its guanine nucleotide exchange (GEF) activity. We further show that SGEF interacts with Grb2, a critical downstream transducer of EGFR. Surprisingly, we found that interaction of Grb2 to SGEF antagonizes the ability of SGEF to enhance EGF-induced ERK1/2 activation. Taken together, this study reports a novel function of SGEF that excludes GEF and also provides important insights into the complex role of Grb2 in EGFR signal transduction.