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Volumn 66, Issue 4, 2009, Pages 711-720

A complex of Shc and Ran-GTPase localises to the cell nucleus

Author keywords

FLIM; Nuclear localisation; Nuclear transport; Protein complex; Proteomics

Indexed keywords

ADAPTOR PROTEIN; GUANOSINE TRIPHOSPHATASE; HYBRID PROTEIN; NUCLEAR PROTEIN; PROTEIN NTF2; PROTEIN SHC; RAN PROTEIN; UNCLASSIFIED DRUG;

EID: 60149101603     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-009-8667-8     Document Type: Article
Times cited : (10)

References (40)
  • 1
    • 0027374486 scopus 로고
    • Identification of Trk binding sites for SHC and phosphatidylinositol 3′-kinase and formation of a multimeric signaling complex
    • Obermeier, A., Lammers, R. Wiesmuller, K. H. Jung, G. Schlessinger, J. and Ullrich, A. (1993) Identification of Trk binding sites for SHC and phosphatidylinositol 3′-kinase and formation of a multimeric signaling complex. J. Biol. Chem. 268, 963-966.
    • (1993) J. Biol. Chem , vol.268 , pp. 963-966
    • Obermeier, A.1    Lammers, R.2    Wiesmuller, K.H.3    Jung, G.4    Schlessinger, J.5    Ullrich, A.6
  • 2
    • 0028242350 scopus 로고
    • Evidence for a functional role of Shc proteins in mitogenic signaling induced by insulin, insulin-like growth factor-1, and epidermal growth factor
    • Sasaoka, T., Rose, D. W. Jhun, B. H. Saltiel, A. R. Draznin, B. and Olefsky J. M. (1994) Evidence for a functional role of Shc proteins in mitogenic signaling induced by insulin, insulin-like growth factor-1, and epidermal growth factor. J. Biol. Chem. 269, 13689-13694.
    • (1994) J. Biol. Chem , vol.269 , pp. 13689-13694
    • Sasaoka, T.1    Rose, D.W.2    Jhun, B.H.3    Saltiel, A.R.4    Draznin, B.5    Olefsky, J.M.6
  • 3
    • 0028912999 scopus 로고
    • Phosphotyrosine-dependent interaction of SHC and insulin receptor substrate 1 with the NPEY motif of the insulin receptor via a novel non-SH2domain
    • Gustafson, T. A., He, W. Craparo, A. Schaub, C. D. and O'Neill, T. J. (1995) Phosphotyrosine-dependent interaction of SHC and insulin receptor substrate 1 with the NPEY motif of the insulin receptor via a novel non-SH2domain. Mol. Cell. Biol. 15, 2500-2508.
    • (1995) Mol. Cell. Biol , vol.15 , pp. 2500-2508
    • Gustafson, T.A.1    He, W.2    Craparo, A.3    Schaub, C.D.4    O'Neill, T.J.5
  • 7
    • 0028860968 scopus 로고    scopus 로고
    • Zhou, M. M., Ravichandran, K. S., Olejniczak, E. F., Petros, A. M., Meadows, R. P., Sattler, M., Harlan, J. E., Wade, W. S., Burakoff, S. J. and Fesik, S. W. (1995) Structure and ligand recognition of the phosphotyrosine binding domain of Shc. Nature. 378, 584-592.
    • Zhou, M. M., Ravichandran, K. S., Olejniczak, E. F., Petros, A. M., Meadows, R. P., Sattler, M., Harlan, J. E., Wade, W. S., Burakoff, S. J. and Fesik, S. W. (1995) Structure and ligand recognition of the phosphotyrosine binding domain of Shc. Nature. 378, 584-592.
  • 8
    • 0033525733 scopus 로고    scopus 로고
    • Phosphotyrosine binding domains of Shc and insulin receptor substrate 1 recognize the NPXpY motif in a thermodynamically distinct manner
    • Farooq, A., Plotnikova, O., Zeng, L. and Zhou, M. M. (1999) Phosphotyrosine binding domains of Shc and insulin receptor substrate 1 recognize the NPXpY motif in a thermodynamically distinct manner. J. Biol. Chem. 274, 6114-6121.
    • (1999) J. Biol. Chem , vol.274 , pp. 6114-6121
    • Farooq, A.1    Plotnikova, O.2    Zeng, L.3    Zhou, M.M.4
  • 9
    • 0034003397 scopus 로고    scopus 로고
    • Shc associates with the IL-3 receptor beta subunit, SHIP and Gab2 following IL-3 stimulation. Contribution of Shc PTB and SH2 domains
    • Bone, H. and Welham, M. J. (2000) Shc associates with the IL-3 receptor beta subunit, SHIP and Gab2 following IL-3 stimulation. Contribution of Shc PTB and SH2 domains. Cell. Signal. 12, 183-194.
    • (2000) Cell. Signal , vol.12 , pp. 183-194
    • Bone, H.1    Welham, M.J.2
  • 10
    • 0031038795 scopus 로고    scopus 로고
    • Lorenzo, M. J., Gish, G. D., Houghton, C., Stonehouse, T. J., Pawson, T., Ponder, B. A. and Smith, D. P. (1997) RET alternate splicing influences the interaction of activated RET with the SH2 and PTB domains of Shc, and the SH2 domain of Grb2. Oncogene. 14, 763-771.
    • Lorenzo, M. J., Gish, G. D., Houghton, C., Stonehouse, T. J., Pawson, T., Ponder, B. A. and Smith, D. P. (1997) RET alternate splicing influences the interaction of activated RET with the SH2 and PTB domains of Shc, and the SH2 domain of Grb2. Oncogene. 14, 763-771.
  • 11
    • 0030293986 scopus 로고    scopus 로고
    • The Shc adaptor protein is highly phosphorylated at conserved, twin tyrosine residues (Y239/240) that mediate protein-protein interactions
    • van der Geer, P., Wiley, S., Gish, G. D. and Pawson, T. (1996) The Shc adaptor protein is highly phosphorylated at conserved, twin tyrosine residues (Y239/240) that mediate protein-protein interactions. Curr. Biol. 6, 1435-44.
    • (1996) Curr. Biol , vol.6 , pp. 1435-1444
    • van der Geer, P.1    Wiley, S.2    Gish, G.D.3    Pawson, T.4
  • 12
    • 0032542350 scopus 로고    scopus 로고
    • Liu, S. K. and McGlade, C. J. (1998) Gads is a novel SH2 and SH3 domain-containing adaptor protein that binds to tyrosine-phosphorylated Shc. Oncogene. 17, 3073-3082.
    • Liu, S. K. and McGlade, C. J. (1998) Gads is a novel SH2 and SH3 domain-containing adaptor protein that binds to tyrosine-phosphorylated Shc. Oncogene. 17, 3073-3082.
  • 14
    • 0027724634 scopus 로고
    • Interaction of Shc with the zeta chain of the T cell receptor upon T cell activation
    • Ravichandran, K. S., Lee, K. K., Songyang, Z., Cantley, L. C., Burn, P. and Burakoff, S. J. (1993) Interaction of Shc with the zeta chain of the T cell receptor upon T cell activation. Science. 262, 902-905.
    • (1993) Science , vol.262 , pp. 902-905
    • Ravichandran, K.S.1    Lee, K.K.2    Songyang, Z.3    Cantley, L.C.4    Burn, P.5    Burakoff, S.J.6
  • 15
    • 0037059799 scopus 로고    scopus 로고
    • Shc and CEACAM1 interact to regulate the mitogenic action of insulin
    • Poy, M. N., Ruch, R. J., Fernstrom, M. A., Okabayashi, Y. and Najjar, S. M. (2002) Shc and CEACAM1 interact to regulate the mitogenic action of insulin. J. Biol. Chem. 277, 1076-1084.
    • (2002) J. Biol. Chem , vol.277 , pp. 1076-1084
    • Poy, M.N.1    Ruch, R.J.2    Fernstrom, M.A.3    Okabayashi, Y.4    Najjar, S.M.5
  • 16
    • 0030910268 scopus 로고    scopus 로고
    • Interaction of the adaptor protein Shc and the adhesion molecule cadherin
    • Xu, Y., Guo, D. F., Davidson, M., Inagami, T. and Carpenter, G. (1997) Interaction of the adaptor protein Shc and the adhesion molecule cadherin. J. Biol. Chem. 272, 13463-13466.
    • (1997) J. Biol. Chem , vol.272 , pp. 13463-13466
    • Xu, Y.1    Guo, D.F.2    Davidson, M.3    Inagami, T.4    Carpenter, G.5
  • 18
    • 0036122481 scopus 로고    scopus 로고
    • Protein phosphatase 2A forms a molecular complex with Shc and regulates Shc tyrosine phosphorylation and downstream mitogenic signaling
    • Ugi, S., Imamura, T., Ricketts, W. and Olefsky J. M. (2002) Protein phosphatase 2A forms a molecular complex with Shc and regulates Shc tyrosine phosphorylation and downstream mitogenic signaling. Mol Cell Biol. 22, 2375-2387.
    • (2002) Mol Cell Biol , vol.22 , pp. 2375-2387
    • Ugi, S.1    Imamura, T.2    Ricketts, W.3    Olefsky, J.M.4
  • 19
    • 0036137605 scopus 로고    scopus 로고
    • Linkage of rapid estrogen action to MAPK activation by ERalpha-Shc association and Shc pathway activation
    • Song, R. X., McPherson, R. A., Adam, L., Bao, Y., Shupnik, M., Kumar, R. and Santen, R. J. (2002) Linkage of rapid estrogen action to MAPK activation by ERalpha-Shc association and Shc pathway activation. Mol Endocrinol. 16, 116-127.
    • (2002) Mol Endocrinol , vol.16 , pp. 116-127
    • Song, R.X.1    McPherson, R.A.2    Adam, L.3    Bao, Y.4    Shupnik, M.5    Kumar, R.6    Santen, R.J.7
  • 20
    • 0033545617 scopus 로고    scopus 로고
    • Cloning and characterization of mPAL, a novel Shc SH2 domain-binding protein expressed in proliferating cells
    • Schmandt, R., Liu, S. K. and McGlade, C. J. (1999) Cloning and characterization of mPAL, a novel Shc SH2 domain-binding protein expressed in proliferating cells. Oncogene. 18, 1867-79.
    • (1999) Oncogene , vol.18 , pp. 1867-1879
    • Schmandt, R.1    Liu, S.K.2    McGlade, C.J.3
  • 21
    • 0029988340 scopus 로고    scopus 로고
    • Phosphotyrosine-independent binding of SHC to the NPLH sequence of murine protein-tyrosine phosphatase-PEST. Evidence for extended phosphotyrosine binding/phosphotyrosine interaction domain recognition specificity
    • Charest, A, Wagner, J., Jacob, S., McGlade, C. J. and Tremblay, M. J. (1996) Phosphotyrosine-independent binding of SHC to the NPLH sequence of murine protein-tyrosine phosphatase-PEST. Evidence for extended phosphotyrosine binding/phosphotyrosine interaction domain recognition specificity. J. Biol. Chem. 271, 8424-8429.
    • (1996) J. Biol. Chem , vol.271 , pp. 8424-8429
    • Charest, A.1    Wagner, J.2    Jacob, S.3    McGlade, C.J.4    Tremblay, M.J.5
  • 22
    • 41949102314 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase epsilon regulates Shc signaling in a kinase-specific manner: Increasing coherence in tyrosine phosphatase signaling
    • Kraut-Cohen, J., Muller, W. J. and Elson, A. (2008) Protein-tyrosine phosphatase epsilon regulates Shc signaling in a kinase-specific manner: increasing coherence in tyrosine phosphatase signaling. J. Biol. Chem. 283, 4612-4621.
    • (2008) J. Biol. Chem , vol.283 , pp. 4612-4621
    • Kraut-Cohen, J.1    Muller, W.J.2    Elson, A.3
  • 23
    • 40649128513 scopus 로고    scopus 로고
    • A phosphorylation dependent mechanism controls the SH2 domain interactions of the Shc adaptor protein
    • George, R., Schuller, A. C., Harris, R. and Ladbury J.E. (2008) A phosphorylation dependent mechanism controls the SH2 domain interactions of the Shc adaptor protein. J. Mol. Biol. 377, 740-747.
    • (2008) J. Mol. Biol , vol.377 , pp. 740-747
    • George, R.1    Schuller, A.C.2    Harris, R.3    Ladbury, J.E.4
  • 24
    • 0037665155 scopus 로고    scopus 로고
    • Specificity is complex and time consuming: Mutual exclusivity in tyrosine kinase-mediated signalling
    • O'Rourke, L. and Ladbury, J. E. (2003) Specificity is complex and time consuming: Mutual exclusivity in tyrosine kinase-mediated signalling. Acc. Chem. Res. 36, 410-416.
    • (2003) Acc. Chem. Res , vol.36 , pp. 410-416
    • O'Rourke, L.1    Ladbury, J.E.2
  • 25
  • 27
    • 0347087425 scopus 로고    scopus 로고
    • A cryptic targeting signal induces isoform-specific localization of p46Shc to mitochondria
    • Ventura, A., Maccarana, M., Raker, V. A. and Pelicci, P.G. (2004) A cryptic targeting signal induces isoform-specific localization of p46Shc to mitochondria. J. Biol. Chem. 279, 2299-2306.
    • (2004) J. Biol. Chem , vol.279 , pp. 2299-2306
    • Ventura, A.1    Maccarana, M.2    Raker, V.A.3    Pelicci, P.G.4
  • 30
    • 0025217198 scopus 로고
    • Direct cloning of leucine zipper proteins: Jun binds cooperatively to the CRE with CRE-BP1
    • Macgregor, P. F., Abate, C. and Curran, T. (1990) Direct cloning of leucine zipper proteins: Jun binds cooperatively to the CRE with CRE-BP1. Oncogene. 5, 451-458.
    • (1990) Oncogene , vol.5 , pp. 451-458
    • Macgregor, P.F.1    Abate, C.2    Curran, T.3
  • 32
    • 34548627531 scopus 로고    scopus 로고
    • Structural biology of nucleocytoplasmic transport
    • Cook, A., Bono, F., Jinek, M. and Conti, E. (2007) Structural biology of nucleocytoplasmic transport. Annu. Rev. Biochem. 76, 647-671.
    • (2007) Annu. Rev. Biochem , vol.76 , pp. 647-671
    • Cook, A.1    Bono, F.2    Jinek, M.3    Conti, E.4
  • 33
    • 33847176295 scopus 로고    scopus 로고
    • Molecular mechanism of the nuclear protein import cycle
    • Stewart, M. (2007) Molecular mechanism of the nuclear protein import cycle. Nat Rev. Mol. Cell. Biol. 8, 195-208.
    • (2007) Nat Rev. Mol. Cell. Biol , vol.8 , pp. 195-208
    • Stewart, M.1
  • 34
    • 42149128181 scopus 로고    scopus 로고
    • High expression of Ran GTPase is associated with local invasion and metastasis of human clear cell renal cell carcinoma
    • Abe, H., Kamai, H., Shirataki, M., Oyama, T., Arai, K. and Yoshida, K. (2008) High expression of Ran GTPase is associated with local invasion and metastasis of human clear cell renal cell carcinoma. Int. J. Cancer. 122, 2391-2397.
    • (2008) Int. J. Cancer , vol.122 , pp. 2391-2397
    • Abe, H.1    Kamai, H.2    Shirataki, M.3    Oyama, T.4    Arai, K.5    Yoshida, K.6
  • 35
    • 40949124863 scopus 로고    scopus 로고
    • Tumor cell dependence on Ran-GTP-directed mitosis
    • Xia, F., Lee, C.W. and Altieri, D.C. (2008) Tumor cell dependence on Ran-GTP-directed mitosis. Cancer Res. 68, 1826-33.
    • (2008) Cancer Res , vol.68 , pp. 1826-1833
    • Xia, F.1    Lee, C.W.2    Altieri, D.C.3
  • 36
    • 23044516594 scopus 로고    scopus 로고
    • Proteomic analysis of redox- and ErbB2-dependent changes in mammary luminal epithelial cells using cysteine- and lysine-labelling two-dimensional difference gel electrophoresis
    • Chan, H. L., Gharbi, S., Gaffney, P. R., Cramer, R., Waterfield, M. D. and Timms, J.F. (2005) Proteomic analysis of redox- and ErbB2-dependent changes in mammary luminal epithelial cells using cysteine- and lysine-labelling two-dimensional difference gel electrophoresis. Proteomics. 5, 2908-2926
    • (2005) Proteomics , vol.5 , pp. 2908-2926
    • Chan, H.L.1    Gharbi, S.2    Gaffney, P.R.3    Cramer, R.4    Waterfield, M.D.5    Timms, J.F.6
  • 37
    • 0032479322 scopus 로고    scopus 로고
    • Colony stimulating factor-1 stimulates the formation of multimeric cytosolic complexes of signaling proteins and cytoskeletal components in macrophages
    • Yee-Young, Y., Yun, W., Einstein, D. B., Lee, P. S. W. and Stanley, E. R. (1998) Colony stimulating factor-1 stimulates the formation of multimeric cytosolic complexes of signaling proteins and cytoskeletal components in macrophages. J. Biol. Chem. 273, 17128-17137.
    • (1998) J. Biol. Chem , vol.273 , pp. 17128-17137
    • Yee-Young, Y.1    Yun, W.2    Einstein, D.B.3    Lee, P.S.W.4    Stanley, E.R.5
  • 38
    • 46249129455 scopus 로고    scopus 로고
    • Extracellular point mutations in FGFR2 elicit unexpected changes in intracellular signalling
    • Ahmed, Z., Schüller, A. C., Suhling, K., Tregidgo, C. and Ladbury, J. E. (2008) Extracellular point mutations in FGFR2 elicit unexpected changes in intracellular signalling. Biochem. J. 413, 37-49.
    • (2008) Biochem. J , vol.413 , pp. 37-49
    • Ahmed, Z.1    Schüller, A.C.2    Suhling, K.3    Tregidgo, C.4    Ladbury, J.E.5
  • 39
    • 1042278767 scopus 로고    scopus 로고
    • Nuclear transport and cancer: From mechanism to intervention
    • Kau, T. R., Way, J. C. and Silver, P. A. (2004) Nuclear transport and cancer: from mechanism to intervention. Nat. Rev. Cancer. 4, 106-117.
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 106-117
    • Kau, T.R.1    Way, J.C.2    Silver, P.A.3
  • 40
    • 0029798506 scopus 로고    scopus 로고
    • Nucleotide-specific interaction of Ran/TC4 with nuclear transport factors NTF2 and p97
    • Paschal, B. M., Delphin, C. and Gerace, L. (1996) Nucleotide-specific interaction of Ran/TC4 with nuclear transport factors NTF2 and p97. Proc. Natl. Acad. Sci. USA. 93. (1996), pp. s7679-7683.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93
    • Paschal, B.M.1    Delphin, C.2    Gerace, L.3


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