Truncations of the C-terminal cytoplasmic domain of MG160, a medial Golgi sialoglycoprotein, result in its partial transport to the plasma membrane and filopodia

Journal of Cell Science

Volumn 111, Issue 2, 1998, Pages 249-260

  Gonatas, Jacqueline O ^a   Chen, You Jun ^a   Stieber, Anna ^a   Mourelatos, Zisimos ^a   Gonatas, Nicholas K ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

E selectin ligand; Filopodia; Golgi; MG160 isoform; Plasma membrane; Sialoglycoprotein

Indexed keywords

FIBROBLAST GROWTH FACTOR RECEPTOR; SIALOGLYCOPROTEIN;

ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL MEMBRANE; CELLULAR DISTRIBUTION; CHO CELL; DNA TRANSFECTION; GOLGI COMPLEX; INTRACELLULAR TRANSPORT; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROCESSING; PROTEIN TRANSPORT;

AMINO ACIDS; ANIMALS; ANTIBODIES; ARGININE; BINDING SITES; BIOLOGICAL TRANSPORT; BIOTIN; CELL MEMBRANE; CHO CELLS; CRICETINAE; CULTURE MEDIA; CYTOPLASM; FEMALE; GOLGI APPARATUS; HUMANS; IMMUNOENZYME TECHNIQUES; MICROSCOPY, IMMUNOELECTRON; PRECIPITIN TESTS; PROTEIN PROCESSING, POST-TRANSLATIONAL; RABBITS; RATS; RECEPTORS, CELL SURFACE; RECEPTORS, FIBROBLAST GROWTH FACTOR; SEQUENCE DELETION; SIALOGLYCOPROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; SUCCINIMIDES; TRANSFECTION;

ANIMALIA; CRICETINAE; CRICETULUS GRISEUS;

EID: 0031906491     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (44)

1. Avrameas, S. and Ternynek, T. (1969) The cross-linking of proteins with glutaraldehyde and its use for the preparation of immunoadsorbents. Immunochemistry 6, 53-66.
2. Avrameas, S. and Temynck, T. (1971). Peroxidase-labelled antibody and Fab conjugates with enhanced intracellular penetration. Immunolchemistry 8, 1175-1179.
3. Banting, G. and Ponnambalam, S. (1997). TGN38 and its orthologues: roles in post-vesicle formation and maintenance of TGN morphology. Biochim. Biophys. Acta 1355, 209-217.
4. Bos, K., Wraight, C. and Stanley, K.K. (1993). TGN38 is maintained in the trans-Golgi network by a tyrosine-containing motif in the cytoplasmic domain. EMBO J. 12, 2219-2228.
5. Brown, WJ. and Farquhar, M.G. (1989). Immunoperoxidase methods for the localization of antigens in cultured cells and tissue sections by electron microscopy. In Methods in Cell Biology. vol. 31 (ed. A. M. Tartakotf). pp. 553-569. Academic Press.
6. Burrus, L.W. and Olwin, B.B. (1989). Isolation of a receptor specific for acidic fibroblast growth factor from embryonic chick. J. Biol. Chem. 264, 18647-18653.
7. Burrus, L.W., Zuber, M.E., Lueddecke, B.A. and Olwin, B.B. (1992) Identification of a cysteine-rich receptor for fibroblast growth factors Mol. Cell Biol. 12, 5600-5609.
8. Chen, Y.-J. and Gonatas, N.K. (1997). The Golgi Sialoglycoprotein MG160. expressed in Pichia pastoris does not require complex carbohydrates and sialic acid for secretion and Basic Fibroblast Growth Factor binding. Biochem. Biophss. Res. Comm. 234, 68-72.
9. Croul, S., Mezitis, S.G.E., Stieber, A., Chen, Y., Gonatas, J.O., Goud, B. and Gonatas, N.K. (1990). Immunocytochemical visualization of the Golgi apparatus in several species, including human and tissues with an antiserum against MG-160, a sialoglycoprotein of the rat Golgi apparatus. J. Histochem. Cytochem. 38, 957-963.
10. Fieser, L.F. and Fieser, M. (1956). Organic Chemistry. 3rd edition, p. 420. Reinhold, NY.
11. Gonatas, J.O., Mezitis, S.G.E., Stieber, A., Fleischer, B. and Gonatas, N.K. (1989). MG-160: a novel sialoglycoprotein of the medial cisternae of the Golgi apparatus. J. Biol. Chem. 264, 546-653.
12. Gonatas, J.O., Mourelatos, Z., Stieber, A., Lane, W.S., Brosius, J. and Gonatas, N.K. (1995). MG-160, a membrane sialoglycoprotein of the medial cisternae of the rat Golgi appartus, binds basic fibroblast growth factor and exhibits a high level of sequence identity to a chicken tibroblast growth factor receptor. J. Cell Sci. 108, 457-467
13. Graham, C.R. and Karnovsky, M.I. (1966). The early stages of absorption of injected horseradish peroxidase in the proximal tubules of mouse kidney: ultrastructural cytochemistry by a new technique. J. Histochem. Cytochem. 14, 291-303.
14. Green, N., Alexander, A., Olson, S., Alexander, T.M., Shinnick, J.G., Sutcliffe and Lerner, R.A. (1982) Immunogenic structure of the influenza virus hemagglutinm. Cell 28, 477-487.
15. Humphrey, J.S., Peters, P.J., Yuan, L.C. and Bonifacino, J.S. (1993) Localization of TGN38 to the trans-Golgi network: Involvement of a cytoplasmic tyrosine-containing sequence. J. Cell Biol. 120, 1123-1135.
16. Huttenlocher A., Sandborg, R. R. and Horwitz, A.F. (1995). Adhesion in cell migration. Curr. Opin. Cell Biol. 7, 697-706.
17. Johnston, P.A., Stieber, A. and Gonatas, N.K. (1994). A hypothesis on the traffic of MGI60. a medial Golgi sialoglycoprotein, from the trans-Golgi network to the Golgi cisternae J. Cell Sci. 107, 529-537.
18. Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
19. Lehninger, A.L., Nelson, D.L. and Cox, M.M. (1993) Principles in Biochemistry. 2nd edition, p. 116. Worth, New York.
20. Lopez, L.C., Maillet, C.M., Oleszkowicz, K. and Shur, B. (1989). Cell surface and Golgi pools of β-1.4-Galactosyltransferase are differentially regulated during embryonal carcinoma cell differentiation. Mol. Cell Biol. 9, 2370-2377
21. Louvard, D., Reggio, H. and Warren, G. (1982). Antibodies to the Golgi complex and the endoplasmic reticulum. J. Cell Biol. 92, 92-107.
22. Machamer, C.K. (1993). Targeting and retention of Golgi membrane proteins. Curr. Opin. Cell Biol. 5, 606-612.
23. McLean, I.W. and Nakane, P.K. (1974) Periodate-lysine-paraformaldehyde fixative. A new fixative for immunoelectron microscopy. J. Histochem. Cytochem. 22, 1077-1083.
24. Mourelatos, Z., Gonatas, J.O., Nycum, L.M., Gonatas, N.K. and Bieget, J.A. (1995). Assignment of the GLGI gene for MG-160. a Fibroblast Growth Factor and E-Selectin binding Membrane Sialoglycoprotein of the Golgi Apparatus to Chromosome 16q22-q23 by Fluorescence in Situ Hybridization. Genomics 28, 354-355.
25. Mourelatos, Z., Gonatas, J.O., Cinato, E. and Gonatas, N.K. (1996). Cloning and Sequence Analysis of the Human MGI60, a Fibroblast Growth Factor and E-Selectin binding membrane sialoglycoprotein of the Golgi apparatus. DNA Cell Biol. 15, 1121-1128.
26. Munro, S. (1991). Sequences within and adjacent to the transmembrane segment of α-2.6-sialyltransferase specify Golgi retention. EMBO J. 10, 3577-3588.
27. Munro, S. (1995). An investigation of the role of transmembrane domains in Golgi protein retention EMBO J. 14, 4695-4704.
28. Nakamura, N., Kabouille, C., Watson, R., Nilsson, T., Hui, N., Slusarewicz, P., Kreis, T.E. and Warren, G. (1995). Characterization of a cis-Golgi matrix protein, GM 130. J. Cell Biol. 131, 1715-1726.
29. Nilsson, T. and Warren, G. (1994). Retention and retrieval in the endoplasmic reticulum and the Golgi apparatus. Curr. Opin. Cell Biol. 6, 517-521.
30. Ponnambalam, S., Rabouille, C., Luzio, J.P., Nilsson, T. and Warren, G. (1994). The TGN38 glycoprotein contains two non-overlapping signals that mediate localisation to the Trans-Golgi network. J. Cell Biol. 125, 253-267.
31. Rajagopalan, S., Xu, V. and Brenner, M.B. (1994). Retention of unassembled components of integral membrane proteins by Calnexin. Science. 263, 387-390.
32. Shur, B.D. (1993). Glycosyltransferases as cell adhesion molecules. Curr. Opin. Cell Biol. 5, 854-863.
33. Slusarewicz, P., Nilsson, T., Hui, N., Watson, R. and Warren, G. (1994) Isolation of matrix that binds medial Golgi enzymes J. Cell Biol. 124, 405-413.
34. Smalheiser, N.R. (1996). Proteins in unexpected locations. Mol. Biol. Cell 7, 1003-1014.
35. Steegmaier, M., Levinovitz, A., Isenmann, S., Borges, K., Lenter, M., Kocher, H.P., Kleuser, B. and Vestweber, D. (1995). The E-selectin-ligand ESL-1 is a variant of a receptor for fibroblast growth factor. Nature 373, 615-620.
36. Steegmaier, M., Borges, E., Berger, J., Schwarz, H. and Vestweber, D. (1997). The E-selectin-ligand ESL-1 is located in the Golgi as well as on microvilli on the cell surface. J. Cell Sci. 110, 687-694.
37. Stieber, A., Mourelatos, Z., Chen, Y-J, Le Douarin, N. and Gonatas, N.K. (1995). MGI60, a membrane protein of the Golgi apparatus which is homologous to a fibroblast growth factor receptor and to a ligand for E-selectin. is found only in the Golgi apparatus and appears early in chicken embryo development. Exp. Cell Res. 219, 562-570.
38. Strous G.J. (1986). Golgi and secreted galactosyltransferase. CRC Crii. Rev. Biochem. 21, 119-151.
39. Weisz, O.A., Swift, A.M. and Machamer, C.K. (1993). Oligomenzation of a membrane protein correlates with its retention in the Golgi complex. J. Cell Biol. 122, 1185-1196.
40. Wigler, M., Silverstein, S., Lee, L-S, Pellicer, A., Cheng, Y.-C. and Axel, R. (1977). Transfer of purified herpes virus thymidine kinase gene to cultured mouse cells. Cell 11, 223-232.
41. Wong, S.H. and Hong, W. (1993). The SYQRL sequence in the cytoplastmic domain of TGN38 plays a major role in Trans-Golgi Netwotk localization. J. Biol. Chem. 268, 22853-22862.
42. Youakim, A., Dubois, D.H. and Shur, B.D. (1994). Localization of the long form of β-1.4-galactosyltransferase to the plasma membrane and Golgi complex of 3T3 and F9 cells by immunotluorescence confocal microscopy. Proc. Nat. Acad. Sci. USA 91, 10913-10917.
43. Zhou, Z., Zuber, M.E., Burrus, L. and Olwin, B.B. (1997) Identification and characterization of a Fibroblast Growth Factor (FGF) binding domain in the cysteine-rich EGF Receptor J. Biol. Chem. 272, 5167-5174.
44. Zuber, M.E., Zhou, Z., Burrus, L.W. and Olwin, B.B. (1997). Cysteine-rich EGF receptor regulates intracellular EGF-1 and EGF-2 levels J. Cell. Physiol. 170, 217-227.