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Mutational Analysis of Carbohydrate and Phospholipid Modifications of a Cell Adhesion Protein

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Glyco-and Cellbiology

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).

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© 1994 Springer-Verlag Berlin Heidelberg

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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

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  • 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

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