The Phosphotyrosine Interaction Domains of X11 and FE65 Bind to Distinct Sites on the YENPTY Motif of Amyloid Precursor Protein

REFERENCES

• Batzer, A. G., P. Blaikie, K. Nelson, J. Schlessinger, and B. Margolis. 1995. The phosphotyrosine interaction domain of Shc binds an LXNPXY motif on the epidermal growth factor receptor. Mol. Cell. Biol. 15:4403–4409.
   PubMedGoogle Scholar
• Batzer, A. G., D. Rotin, J. M. Urena, E. Y. Skolnik, and J. Schlessinger. 1994. Hierarchy of binding sites for Grb2 and Shc on the epidermal growth factor receptor. Mol. Cell. Biol. 14:5192–5201.
   PubMed Web of Science ®Google Scholar
• Blaikie, P., D. Immanuel, J. Wu, N. Li, V. Yajnik, and B. Margolis. 1994. A region in Shc distinct from the SH2 domain can bind tyrosine-phosphorylated growth factor receptors. J. Biol. Chem. 269:32031–32034.
   PubMed Web of Science ®Google Scholar
• Borg, J. P., J. Herz, and B. Margolis. Unpublished observations.
   Google Scholar
• Bork, P., and B. Margolis. 1995. A phosphotyrosine interaction domain. Cell 80:693–694.
   PubMed Web of Science ®Google Scholar
• Brenman, J. E., D. S. Chao, S. H. Gee, A. W. McGee, S. E. Craven, D. R. Santillano, Z. Wu, F. Huang, H. Xia, M. F. Peters, S. C. Froehner, and D. S. Bredt. 1996. Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and α1-syntrophin mediated by PDZ domains. Cell 84:757–767.
   PubMed Web of Science ®Google Scholar
• Brenman, J. E., D. S. Chao, H. Xia, K. Aldape, and D. S. Bredt. 1995. Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy. Cell 82:743–752.
   PubMed Web of Science ®Google Scholar
• Buxbaum, J. D., S. E. Gandy, P. Cichetti, M. E. Ehrlich, A. J. Czernik, R. P. Fracasso, T. V. Ramabhadran, A. J. Unterbeck, and P. Greengard. 1990. Processing of Alzheimer β/A4 amyloid precursor protein: modulation by agents that regulate protein phosphorylation. Proc. Natl. Acad. Sci. USA 87:6003–6006.
   PubMed Web of Science ®Google Scholar
• Charest, A., J. Wagner, S. Jacob, C. J. McGlade, and M. L. Tremblay. 1996. Phosphotyrosine-independent binding of SHC to the NPLH sequence of murine protein-tyrosine phosphatase-PEST. J. Biol. Chem. 271:8424–8429.
   PubMedGoogle Scholar
• Chen, C., and H. Okayama. 1987. High-efficiency transformation of mammalian cells by plasmid DNA. Mol. Cell. Biol. 7:2745–2752.
   PubMed Web of Science ®Google Scholar
• Chen, H. I., and M. Sudol. 1995. The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules. Proc. Natl. Acad. Sci. USA 92:7819–7823.
   PubMedGoogle Scholar
• Chen, W.-J., J. L. Goldstein, and M. S. Brown. 1990. NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor. J. Biol. Chem. 265:3116–3123.
   PubMed Web of Science ®Google Scholar
• Chen, Y.-H., D. Grall, A. E. Salcini, P. G. Pelicci, J. Pouyssegur, and E. Van Obberghen-Schilling. 1996. Shc adaptor proteins are key transducers of mitogenic signaling mediated by the G protein-coupled thrombin receptor. EMBO J. 15:1037–1044.
   PubMedGoogle Scholar
• Craparo, A., T. J. O’Neill, and T. A. Gustafson. 1995. Non-SH2 domains within insulin receptor substrate-1 and SHC mediate their phosphotyrosine-dependent interaction with the NPEY motif of the insulin-like growth factor I receptor. J. Biol. Chem. 270:15639–15643.
   PubMedGoogle Scholar
• Cutler, R. L., L. Liu, J. E. Damen, and G. Krystal. 1993. Multiple cytokines induce the tyrosine phosphorylation of Shc and its association with Grb2 in hemopoietic cells. J. Biol. Chem. 268:21463–21465.
   PubMed Web of Science ®Google Scholar
• De Strooper, B., L. Umans, F. Van Leuven, and H. Van Den Berghe. 1993. Study of the synthesis and secretion of normal and artificial mutants of murine amyloid precursor protein (APP): cleavage of APP occurs in a late compartment of the default secretion pathway. J. Cell Biol. 121:295–304.
   PubMed Web of Science ®Google Scholar
• Dikic, I., A. G. Batzer, P. Blaikie, A. Obermeier, A. Ullrich, J. Schlessinger, and B. Margolis. 1995. Shc binding to nerve growth factor receptor is mediated by the phosphotyrosine interaction domain. J. Biol. Chem. 270:15125–15129.
   PubMedGoogle Scholar
• Doyle, D. A., A. Lee, J. Lewis, E. Kim, M. Sheng, and R. MacKinnon. 1996. Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Cell 85:1067–1076.
   PubMed Web of Science ®Google Scholar
• Duclos, F., U. Boschert, G. Sirugo, J.-L. Mandel, R. Hen, and M. Koenig. 1993. Gene in the region of the Friedreich ataxia locus encodes a putative transmembrane protein expressed in the nervous system. Proc. Natl. Acad. Sci. USA 90:109–113.
   PubMedGoogle Scholar
• Duilio, A., N. Zambrano, A. R. Mogavero, R. Ammendola, F. Cimino, and T. Russo. 1991. A rat brain mRNA encoding a transcriptional activator homologous to the DNA binding domain of retroviral integrases. Nucleic Acids Res. 19:5269–5274.
   PubMedGoogle Scholar
• Fiore, F., N. Zambrano, G. Minopoli, V. Donini, A. Duilio, and T. Russo. 1996. The regions of the Fe65 protein homologous to the phosphotyrosine interaction/phosphotyrosine binding domain of Shc bind the intracellular domain of the Alzheimer’s amyloid precursor protein. J. Biol. Chem. 270:30853–30856.
   Google Scholar
• Glenner, G. G., and C. W. Wong. 1984. Alzheimer’s disease and Down’s syndrome: sharing of a unique cerebrovascular amyloid fibril protein. Bio-chem. Biophys. Res. Commun. 122:1131–1135.
   PubMed Web of Science ®Google Scholar
• Guo, M., L. Y. Jan, and Y. N. Jan. 1996. Control of daughter cell fates during asymmetric division: interaction of Numb and Notch. Neuron 17:27–41.
   PubMed Web of Science ®Google Scholar
• Gustafson, T., W. He, A. Craparo, C. Schaub, and T. O’Neill. 1995. Phos-photyrosine-dependent interaction of SHC and insulin receptor substrate 1 with the NPEY motif of the insulin receptor via a novel non-SH2 domain. Mol. Cell. Biol. 15:2500–2508.
   PubMed Web of Science ®Google Scholar
• Haass, C., A. Y. Hung, M. G. Schlossmacher, D. B. Teplow, and D. J. Selkoe. 1993. β-Amyloid peptide and a 3-kDa fragment are derived by distinct cellular mechanisms. J. Biol. Chem. 268:3021–3024.
   PubMed Web of Science ®Google Scholar
• He, W., T. J. O’Neill, and T. A. Gustafson. 1995. Distinct modes of interaction of SHC and IRS-1 with the insulin receptor NPEY region via non-SH2 domains. J. Biol. Chem. 270:23258–23262.
   PubMedGoogle Scholar
• Isakoff, S. J., Y.-P. Yu, Y.-C. Su, P. Blaikie, V. Yajnik, E. Rose, K. M. Weidner, M. Sachs, B. Margolis, and E. Y. Skolnik. 1996. The Shc PTB/PI domain is required for Shc tyrosine phosphorylation by the Insulin Receptor (IR) and recognizes an NPXY motif on the IR that is distinct from IRS-1 in vivo. J. Biol. Chem. 271:3959–3962.
   PubMedGoogle Scholar
• Kang, J., H.-G. Lemaire, A. Unterbeck, J. M. Salbaum, C. L. Masters, K.-H. Grzeschik, G. Multhaup, K. Beyreuther, and B. Muller-Hill. 1987. The precursor of Alzheimer’s disease amyloid A4 protein resembles a cell-surface receptor. Nature (London) 325:733–736.
   PubMed Web of Science ®Google Scholar
• Kavanaugh, W. M., and L. T. Williams. 1994. An alternative to SH2 domains for binding tyrosine-phosphorylated proteins. Science 266:1862–1865.
   PubMed Web of Science ®Google Scholar
• Koo, E. H., and S. L. Squazzo. 1994. Evidence that production and release of amyloid β-protein involves the endocytic pathway. J. Biol. Chem. 269:17386–17389.
   PubMed Web of Science ®Google Scholar
• Kornau, H.-C., L. T. Schenker, M. B. Kennedy, and P. H. Seeburg. 1995. Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95. Science 269:1737–1740.
   PubMedGoogle Scholar
• Lai, A., S. S. Sisodia, and I. S. Trowbridge. 1995. Characterization of sorting signals in the –-amyloid precursor protein cytoplasmic domain. J. Biol. Chem. 270:3565–3573.
   PubMed Web of Science ®Google Scholar
• Lev, S., H. Moreno, A. Martinez, P. Canoll, E. Peles, J. M. Musacchio, G. D. Plowman, B. Rudy, and J. Schlessinger. 1995. Protein tyrosine kinase PYK2 involved in (Ca2+)-induced regulation of ion channel and MAP kinase functions. Nature (London) 376:737–745.
   PubMed Web of Science ®Google Scholar
• Lowenstein, E. J., R. J. Daly, A. G. Batzer, W. Li, B. Margolis, R. Lammers, A. Ullrich, E. Y. Skolnik, D. Bar-Sagi, and J. Schlessinger. 1992. The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling. Cell 70:431–442.
   PubMed Web of Science ®Google Scholar
• Margolis, B., N. Li, A. Koch, M. Mohammadi, D. Hurwitz, A. Zilberstein, A. Ullrich, T. Pawson, and J. Schlessinger. 1990. The tyrosine phosphorylated carboxyterminus of the EGF receptor is a binding site for GAP and PLC-gamma. EMBO J. 9:4375–4380.
   PubMedGoogle Scholar
• Margolis, B., S. G. Rhee, S. Felder, M. Mervic, R. Lyall, A. Levitski, A. Ullrich, A. Zilberstein, and J. Schlessinger. 1989. EGF induces tyrosine phosphorylation of phospholipase C-II: a potential mechanism for EGF receptor signaling. Cell 57:1101–1107.
   PubMed Web of Science ®Google Scholar
• Margolis, B., O. Silvennoinen, F. Comoglio, C. Roonprapunt, E. Skolnik, A. Ullrich, and J. Schlessinger. 1992. High-efficiency expression/cloning of epidermal growth factor-receptor-binding proteins with Src homology 2 domains. Proc. Natl. Acad. Sci. USA 89:8894–8898.
   PubMedGoogle Scholar
• Masters, C. L., G. Simms, N. A. Weinman, G. Multhaup, B. L. McDonald, and K. Beyreuther. 1985. Amyloid plaque core protein in Alzheimer disease and Down syndrome. Proc. Natl. Acad. Sci. USA 82:4245–4249.
   PubMed Web of Science ®Google Scholar
• Norstedt, C., G. L. Caporaso, J. Thyberg, S. E. Gandy, and P. Greengard. 1993. Identification of the Alzheimer β/A4 amyloid precursor protein in clathrin-coated vesicles purified from PC12 cells. J. Biol. Chem. 268:608–612.
   PubMedGoogle Scholar
• Ooi, J., V. Yajnik, D. Immanuel, M. Gordon, J. J. Moskow, A. M. Buchberg, and B. Margolis. 1995. The cloning of Grb10 reveals a new family of SH2 domain proteins. Oncogene 10:1621–1630.
   PubMedGoogle Scholar
• Pawson, T. 1995. Protein modules and signalling networks. Nature (London) 373:573–579.
   PubMed Web of Science ®Google Scholar
• Pelicci, G., L. Lanfrancone, F. Grignani, J. McGlade, F. Cavallo, G. Forni, I. Nicoletti, T. Pawson, and P. G. Pelicci. 1992. A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction. Cell 70:93–104.
   PubMed Web of Science ®Google Scholar
• Ron, D., and H. Dressler. 1992. pGSTag: a versatile bacterial expression plasmid for enzymatic labeling of recombinant proteins. BioTechniques 13:866–869.
   PubMedGoogle Scholar
• Rozakis-Adcock, M., J. McGlade, G. Mbamalu, G. Pelicci, R. Daly, W. Li, A. Batzer, S. Thomas, J. Brugge, and P. G. Pelicci. 1992. Association of the Shc and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases. Nature (London) 360:689–692.
   PubMed Web of Science ®Google Scholar
• Sato, T., S. Irie, S. Kitada, and J. C. Reed. 1995. FAP-1: a protein tyrosine phosphatase that associates with Fas. Science 268:411–415.
   PubMed Web of Science ®Google Scholar
• Schlessinger, J. 1994. SH2/SH3 signaling proteins. Curr. Opin. Genet. Dev. 4:25–30.
   PubMedGoogle Scholar
• Simeone, A., A. Duilio, F. Fiore, D. Acampora, C. De Felice, R. Faraonio, F. Paolocci, F. Cimino, and T. Russo. 1994. Expression of the neuron-specific FE65 gene marks the development of embryo ganglionic derivatives. Dev. Neurosci. 16:53–60.
   PubMedGoogle Scholar
• Skolnik, E. Y., B. Margolis, M. Mohammadi, E. Lowenstein, R. Fischer, A. Drepps, A. Ullrich, and J. Schlessinger. 1991. Cloning of PI3 kinase-associated p85 utilizing a novel method for expression/cloning of target proteins for receptor tyrosine kinases. Cell 65:83–90.
   PubMed Web of Science ®Google Scholar
• Songyang, Z., S. E. Shoelson, J. McGlade, P. Olivier, T. Pawson, X. R. Bustelo, M. Barbacid, H. Sabe, H. Hanafusa, and T. Yi. 1994. Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav. Mol. Cell. Biol. 14:2777–2785.
   PubMed Web of Science ®Google Scholar
• Staub, O., S. Dho, P. C. Henry, J. Correa, T. Ishikawa, J. McGlade, and D. Rotin. 1996. WW domains of Nedd4 bind to the proline-rich PY motifs in the epithelial Na+ channel deleted in Liddle’s syndrome. EMBO J. 15:2371–2380.
   PubMed Web of Science ®Google Scholar
• Sudol, M., P. Bork, A. Einbond, K. Kastury, T. Druck, M. Negrini, K. Huebner, and D. Lehman. 1995. Characterization of the mammalian YAP (Yes-associated protein) gene and its role in defining a novel protein module, the WW domain. J. Biol. Chem. 24:14733–14741.
   Google Scholar
• Sudol, M., H. I. Chen, C. Bougeret, A. Einbond, and P. Bork. 1995. Characterization of a novel protein-binding module—the WW domain. FEBS Lett. 369:67–71.
   PubMed Web of Science ®Google Scholar
• Tartare-Deckert, S., D. Sawka-Verhelle, J. Murdaca, and E. Van Obberghen. 1995. Evidence for a differential interaction of SHC and IRS-1 with the IGF-IR in the yeast two-hybrid system. J. Biol. Chem. 270:23456–23460.
   PubMed Web of Science ®Google Scholar
• van der Geer, P., S. Wiley, G. D. Gish, K.-M. V. Lai, R. Stephens, M. F. White, D. Kaplan, and T. Pawson. 1996. Identification of residues that control specific binding of the Shc phosphotyrosine-binding domain to phosphotyrosine sites. Proc. Natl. Acad. Sci. USA 93:963–968.
   PubMedGoogle Scholar
• van der Geer, P., S. Wiley, V. K.-M. Lai, J. P. Olivier, G. D. Gish, R. Stephens, D. Kaplan, S. Shoelson, and T. Pawson. 1995. A conserved aminoterminal Shc domain binds to phosphotyrosine motifs in activated receptors and phosphopeptides. Curr. Biol. 5:404–412.
   PubMedGoogle Scholar
• VanderKuur, J., G. Allevato, N. Billestrup, G. Norstedt, and C. Carter-Su. 1995. Growth hormone-promoted tyrosyl phosphorylation of SHC proteins and SHC association with Grb2. J. Biol. Chem. 270:7587–7593.
   PubMed Web of Science ®Google Scholar
• Waksman, G., D. Kominos, S. C. Robertson, N. Pant, D. Baltimore, R. B. Birge, D. Cowburn, H. Hanafusa, B. J. Mayer, and M. Overduin. 1992. Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides. Nature (London) 358:646–653.
   PubMed Web of Science ®Google Scholar
• Wolf, G., T. Trüb, E. Ottinger, L. Groninga, A. Lynch, M. F. White, M. Miyazaki, J. Lee, and S. E. Shoelson. 1995. PTB domains of IRS-1 and Shc have distinct but overlapping binding specificities. J. Biol. Chem. 270:27407–27410.
   PubMedGoogle Scholar
• Yajnik, V., P. Blaikie, P. Bork, and B. Margolis. 1996. Identification of residues within the Shc phosphotyrosine binding/phosphotyrosine interaction domain crucial for phosphopeptide interaction. J. Biol. Chem. 271:1813–1816.
   PubMedGoogle Scholar
• Zhou, M.-M., K. S. Ravichandran, E. T. Olejniczak, A. M. Petros, R. P. Meadows, M. Sattler, J. E. Harlan, W. S. Wade, S. J. Burakoff, and S. W. Fesik. 1995. Structure and ligand recognition of the phosphotyrosine binding domain of Shc. Nature (London) 378:584–592.
   PubMedGoogle Scholar