Abstract
The contact site A (csA) glycoprotein is a developmentally regulated cell adhesion molecule (Beug et al. 1973; Müller and Gerisch 1978; Noegel et al. 1985). It is absent from growth-phase cells, and is maximally expressed at the aggregation stage of Dictyostelium discoideum, i.e., during transition from the state of single cells to a multicellular organism (Murray et al. 1981). According to its sequence, the csA protein consists of three regions: a large extracellular N-terminal domain, a proline-, serine-and threonine-rich sequence which resembles the hinge region of immunoglobulins, and a carboxyterminal stretch of hydrophobic amino acids (Noegel et al. 1986). The protein is cotranslationally modified by N-linked carbohydrate residues at the N-terminal domain, and by a ceramide-based phospholipid (PL) anchor (Stadler et al. 1989). The pro/ser/thr-rich stretch of the C-terminal region near to the plasma membrane is decorated with O-linked carbohydrate residues during passage of the protein through the Golgi apparatus, and the N-linked carbohydrate residues are sulfated during the passage (Hohmann et al. 1985; Hohmann et al. 1987b).
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Barth A (1992) Untersuchungen zur Funktion des Phospholipid-Ankers eines Zelladhäsions-proteins von Dictyostelium discoideum RAPER. Ph D Thesis: Univ Hamburg
Bertholdt G, Stadler J, Bozzaro S, Fichtner B, Gerisch G (1985) Carbohydrate and other epitopes of the contact site A glycoprotein of Dictyostelium discoideum as characterized by monoclonal antibodies. Cell Diff 16:187–202
Beug H, Katz FE, Gerisch G (1973) Dynamics of antigenic membrane sites relating to cell aggregation in Dictyostelium discoideum. J Cell Biol 56:647–658
Bozzaro S, Gerisch G (1978) Contact sites in aggregating cells of Polysphondylium pallidum. J Mol Biol 120:265–279
Bozzaro S, Merkl R, Gerisch G (1987) Cell adhesion: Its quantification, assay of the molecules involved, and selection of defective mutants in Dictyostelium and Polysphondylium. Methods Cell Biol 28:359–385
Chadwick CM, Ellison JE, Garrod DR (1984) Dual role for Dictyostelium contact site B in phagocytosis and developmental size regulation. Nature 307:646–647
Desbarats L, Lam TY, Wong LM, Siu C-H (1992) Identification of a unique cAMP-response element in the gene encoding the cell adhesion molecule gp80 in Dictyostelium discoideum. J Biol Chem 267:19655–19664
Faix J, Gerisch G, Noegel AA (1990) Constitutive overexpression of the contact site A glycoprotein enables growth-phase cells of Dictyostelium discoideum to aggregate. EMBO J 9:2709–2716
Faix J, Gerisch G, Noegel AA (1992) Overexpression of the csA cell adhesion molecule under its own cAMP-regulated promoter impairs morphogenesis in Dictyostelium. J Cell Sci 102:203–214
Faix J (1993) Gezielte Expression und Mutagenese des csA-Glycoproteins von Dictyostelium discoideum zur Untersuchung der strukturellen Voraussetzungen seiner Funktion als Zell-adhäsionsmolekül. Ph D Thesis, Univ Regensburg
Fang H, Higa M, Suzuki K, Aiba K, Urushihara H, Yanagisawa K (1993) Molecular cloning and characterization of two genes encoding gpl38, a cell surface glycoprotein involved in the sexual cell fusion of Dictyostelium discoideum. Dev Biol 156:201–208
Ferguson MAJ, Williams AF (1988) Cell-surface anchoring of proteins via glycosylphosphatidyl-inositol structures. Annu Rev Biochem 57:285–320
Francis D, Toda K, Merkl R, Hatfield T, Gerisch G (1985) Mutants of Polysphondylium pallidum altered in cell aggregation and in the expression of a carbohydrate epitope on cell surface glycoproteins. EMBO J 4:2525–2532
Gaillard J-L, Berche P, Frehel C, Gouin E, Cossart P (1991) Entry of L. monocytogenes into cells is mediated by internalin, a repeat protein reminiscent of surface antigens from gram- positive cocci. Cell 65:1127–1141
Gerisch G, Krelle H, Bozzaro S, Eitle E, Guggenheim R (1980) Analysis of cell adhesion in Dictyostelium and Polysphondylium by the use of Fab. In: Curtis ASG, Pitts JD (eds) Cell adhesion and motility. University Press, Cambridge, pp 293–307
Gerisch G, Weinhart U, Bertholdt G, Claviez M, Stadler J (1985) Incomplete contact site Aglycoprotein in HL220, a modB mutant of Dictyostelium discoideum. J Cell Sci 73:49–68
Gonzales-Yanes B, Mandell RB, Girard M, Henry S, Aparicio O, Gritzali M, Brown RD Jr, Erdos GW, West CM (1989) The spore coat of a fucosylation mutant in Dictyostelium discoideum. Dev Biol 133:576–587
Hohmann H-P, Gerisch G, Lee RWH, Huttner WB (1985) Cell-free sulfation of the contact site A glycoprotein of Dictyostelium discoideum and of a partially glycosylated precursor. J Biol Chem 260:13869–13878
Hohmann H-P, Bozzaro S, Merkl R, Wallraff E, Yoshida M, Weinhart U, Gerisch G (1987a) Post-translational glycosylation of the contact site A protein of Dictyostelium discoideum is important for stability but not for its function in cell adhesion. EMBO J 6:3663–3671
Hohmann H-P, Bozzaro S, Yoshida M, Merkl R, Gerisch G (1987b) Two-step glycosylation of the contact site A protein of Dictyostelium discoideum and transport of an incompletely glycosylated form to the cell surface. J Biol Chem 262:16618–16624
Knecht DA, Dimond RL, Wheeler S, Loomis WF (1984) Antigenic determinants shared by lysosomal proteins of Dictyostelium discoideum. J Biol Chem 259:10633–10640
Loomis WF, Wheeler SA, Springer WR, Barondes SH (1985) Adhesion mutants of Dictyostelium discoideum lacking the saccharide determinant recognized by two adhesion-blocking monoclonal antibodies. Dev Biol 109:111–117
Müller K, Gerisch G (1978) A specific glycoprotein as the target site of adhesion blocking Fab in aggregating Dictyostelium cells. Nature 274:445–449
Müller-Taubenberger A (1989) Sequenzierung und funktionelle Charakterisierung von ent-wicklungsregulierten Genen in Dictyostelium discoideum. Ph D Thesis, Univ Stuttgart
Müller-Taubenberger A, Westphal M, Noegel A, Gerisch G (1989) A developmentally regulated gene product from Dictyostelium discoideum shows high homology to human α-L-fu- cosidase. FEBS Lett 246:185–192
Murray BA, Yee LD, Loomis WF (1981) Immunological analysis of a glycoprotein (contact sites A) involved in intercellular adhesion of Dictyostelium discoideum. J Supramol Struct Cell Biochem 17:197–211
Murray BA, Wheeler S, Jongens T, Loomis WF (1984) Mutations affecting a surface glycoprotein, gp80, of Dictyostelium discoideum. Mol Cell Biol 4:514–519
Noegel A, Harloff C, Hirth P, Merkl R, Modersitzki M, Stadler J, Weinhart U, Westphal M, Gerisch G (1985) Probing an adhesion mutant of Dictyostelium discoideum with cDNA clones and monoclonal antibodies indicates a specific defect in the contact site A glycoprotein. EMBO J 4:3805–3810
Noegel A, Gerisch G, Stadler J, Westphal M (1986) Complete sequence and transcript regulation of a cell adhesion protein from aggregating Dictyostelium cells. EMBO J 5:1473–1476
Raper KB (1984) The Dictyostelids. University Press, Princeton, p 227 Saito T, Kumazaki T, Ochiai H (1993) A purification method and N-glycosylation sites of a 36- cysteine-containing, putative cell/cell adhesion glycoprotein gp64 of the cellular slime mold, Polysphondylium pallidum. Eur J Biochem 211:147–155
Saxe III CL, Klein P, Sun TJ, Kimmel AR, Devreotes PN (1988) Structure and expression of the cAMP cell-surface receptor. Dev Gen 9:227–235
Schopohl D, Muller-Taubenberger A, Orthen B, Hess H, Reutter W (1992) Purification and properties of a secreted and developmentally regulated a-L-fucosidase from Dictyostelium discoideum. J Biol Chem 267:2400–2405
Stadler J, Gerisch G, Bauer G, Suchanek C, Huttner WB (1983) In vivo sulfation of the contact site A glycoprotein of Dictyosteliwn discoideum. EMBO J 2:1137–1143
Stadler J, Keenan TW, Bauer G, Gerisch G (1989) The contact site A glycoprotein of Dictyosteliwn discoideum carries a phospholipid anchor of a novel type. EMBO J 8:371–377
Toda K, Bozzaro S, Lottspeich F, Merkl R, Gerisch G (1984a) Monoclonal anti-glycoprotein antibody that blocks cell adhesion in Polysphondylium pallidum. Eur J Biochem 140:73–81
Toda K, Tharanathan RN, Bozzaro S, Gerisch G (1984b) Monoclonal antibodies that block cell adhesion in Polysphondylium pallidum: reaction with L-fucose, a terminal sugar in cell-surface glycoproteins. Eur J Biochem 143:477–481
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1994 Springer-Verlag Berlin Heidelberg
About this paper
Cite this paper
Gerisch, G. et al. (1994). Mutational Analysis of Carbohydrate and Phospholipid Modifications of a Cell Adhesion Protein. In: Wieland, F., Reutter, W. (eds) Glyco-and Cellbiology. Colloquium der Gesellschaft für Biologische Chemie 22.–24. April 1993 in Mosbach/Baden, vol 44. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-78729-4_13
Download citation
DOI: https://doi.org/10.1007/978-3-642-78729-4_13
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-78731-7
Online ISBN: 978-3-642-78729-4
eBook Packages: Springer Book Archive