Biosynthesis of glycosyl-phosphatidylinositol protein snchors in African trypanosomes

Kenneth G. Milne, Robert A. Field, Michael A. J. Ferguson

    Research output: Chapter in Book/Report/Conference proceedingConference contribution

    Abstract

    Covalent linkage to a glycosyl-phosphatidylinositol (GPI) has been widely recognised as a mode of anchoring proteins to eukaryotic cell surfaces (Ferguson and Williams, 1988; Low, 1989; Thomas et al., 1990; Cross, 1990; Ferguson, 1991). The GPI anchor can be thought of as an alternative to the hydrophobic transmembrane polypeptide domain for membrane protein anchorage. There is no clear correlation between the occurrence of a GPI anchor and protein function, examples of GPI anchored proteins include, protozoal coat proteins, hydrolases, differentiation antigens, adhesion molecules and receptors (Fig. 1). The basic structure of GPI anchors is conserved between different eukaryotes (Ferguson et al., 1988; Homans et al., 1988; Roberts et al., 1988; Schneider et al., 1990; Guther et al., 1992; Deeg et al., 1992), suggestive of a shared biosynthetic pathway.
    Original languageEnglish
    Title of host publicationNew developments in lipid—protein interactions and receptor function
    EditorsK. W. A. Wirtz, L. Packer, J. A. Gustafsson, A. E. Evangelopoulos, J. P. Changeux
    Place of PublicationNew York
    PublisherPlenum Press
    Pages275-286
    Number of pages12
    ISBN (Electronic)9781461528609
    ISBN (Print)9781461362395
    DOIs
    Publication statusPublished - 1993
    EventNATO Advanced Study Institute on New Developments in Lipid-Protein Interactions and Receptor Function Conference - Spetsai, Greece
    Duration: 16 Aug 199227 Aug 1992
    http://www.worldcat.org/title/new-developments-in-lipid-protein-interactions-and-receptor-function-proceedings-of-a-nato-advanced-study-institute-on-new-developments-in-lipid-proteinand-receptor-function-held-august-16-27-1992-in-spetsai-greece/oclc/311928225

    Publication series

    NameNATO ASI series. Series A: Life sciences
    Volume246

    Conference

    ConferenceNATO Advanced Study Institute on New Developments in Lipid-Protein Interactions and Receptor Function Conference
    CountryGreece
    CitySpetsai
    Period16/08/9227/08/92
    Internet address

    Fingerprint

    Protein
    Africa
    Adhesion
    Linkage
    Membrane
    Pathway
    Anchoring

    Cite this

    Milne, K. G., Field, R. A., & Ferguson, M. A. J. (1993). Biosynthesis of glycosyl-phosphatidylinositol protein snchors in African trypanosomes. In K. W. A. Wirtz, L. Packer, J. A. Gustafsson, A. E. Evangelopoulos, & J. P. Changeux (Eds.), New developments in lipid—protein interactions and receptor function (pp. 275-286). (NATO ASI series. Series A: Life sciences; Vol. 246). New York: Plenum Press. https://doi.org/10.1007/978-1-4615-2860-9_26
    Milne, Kenneth G. ; Field, Robert A. ; Ferguson, Michael A. J. / Biosynthesis of glycosyl-phosphatidylinositol protein snchors in African trypanosomes. New developments in lipid—protein interactions and receptor function . editor / K. W. A. Wirtz ; L. Packer ; J. A. Gustafsson ; A. E. Evangelopoulos ; J. P. Changeux. New York : Plenum Press, 1993. pp. 275-286 (NATO ASI series. Series A: Life sciences).
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    title = "Biosynthesis of glycosyl-phosphatidylinositol protein snchors in African trypanosomes",
    abstract = "Covalent linkage to a glycosyl-phosphatidylinositol (GPI) has been widely recognised as a mode of anchoring proteins to eukaryotic cell surfaces (Ferguson and Williams, 1988; Low, 1989; Thomas et al., 1990; Cross, 1990; Ferguson, 1991). The GPI anchor can be thought of as an alternative to the hydrophobic transmembrane polypeptide domain for membrane protein anchorage. There is no clear correlation between the occurrence of a GPI anchor and protein function, examples of GPI anchored proteins include, protozoal coat proteins, hydrolases, differentiation antigens, adhesion molecules and receptors (Fig. 1). The basic structure of GPI anchors is conserved between different eukaryotes (Ferguson et al., 1988; Homans et al., 1988; Roberts et al., 1988; Schneider et al., 1990; Guther et al., 1992; Deeg et al., 1992), suggestive of a shared biosynthetic pathway.",
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    year = "1993",
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    isbn = "9781461362395",
    series = "NATO ASI series. Series A: Life sciences",
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    Milne, KG, Field, RA & Ferguson, MAJ 1993, Biosynthesis of glycosyl-phosphatidylinositol protein snchors in African trypanosomes. in KWA Wirtz, L Packer, JA Gustafsson, AE Evangelopoulos & JP Changeux (eds), New developments in lipid—protein interactions and receptor function . NATO ASI series. Series A: Life sciences, vol. 246, Plenum Press, New York, pp. 275-286, NATO Advanced Study Institute on New Developments in Lipid-Protein Interactions and Receptor Function Conference, Spetsai, Greece, 16/08/92. https://doi.org/10.1007/978-1-4615-2860-9_26

    Biosynthesis of glycosyl-phosphatidylinositol protein snchors in African trypanosomes. / Milne, Kenneth G.; Field, Robert A.; Ferguson, Michael A. J.

    New developments in lipid—protein interactions and receptor function . ed. / K. W. A. Wirtz; L. Packer; J. A. Gustafsson; A. E. Evangelopoulos; J. P. Changeux. New York : Plenum Press, 1993. p. 275-286 (NATO ASI series. Series A: Life sciences; Vol. 246).

    Research output: Chapter in Book/Report/Conference proceedingConference contribution

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    T1 - Biosynthesis of glycosyl-phosphatidylinositol protein snchors in African trypanosomes

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    AU - Field, Robert A.

    AU - Ferguson, Michael A. J.

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    N2 - Covalent linkage to a glycosyl-phosphatidylinositol (GPI) has been widely recognised as a mode of anchoring proteins to eukaryotic cell surfaces (Ferguson and Williams, 1988; Low, 1989; Thomas et al., 1990; Cross, 1990; Ferguson, 1991). The GPI anchor can be thought of as an alternative to the hydrophobic transmembrane polypeptide domain for membrane protein anchorage. There is no clear correlation between the occurrence of a GPI anchor and protein function, examples of GPI anchored proteins include, protozoal coat proteins, hydrolases, differentiation antigens, adhesion molecules and receptors (Fig. 1). The basic structure of GPI anchors is conserved between different eukaryotes (Ferguson et al., 1988; Homans et al., 1988; Roberts et al., 1988; Schneider et al., 1990; Guther et al., 1992; Deeg et al., 1992), suggestive of a shared biosynthetic pathway.

    AB - Covalent linkage to a glycosyl-phosphatidylinositol (GPI) has been widely recognised as a mode of anchoring proteins to eukaryotic cell surfaces (Ferguson and Williams, 1988; Low, 1989; Thomas et al., 1990; Cross, 1990; Ferguson, 1991). The GPI anchor can be thought of as an alternative to the hydrophobic transmembrane polypeptide domain for membrane protein anchorage. There is no clear correlation between the occurrence of a GPI anchor and protein function, examples of GPI anchored proteins include, protozoal coat proteins, hydrolases, differentiation antigens, adhesion molecules and receptors (Fig. 1). The basic structure of GPI anchors is conserved between different eukaryotes (Ferguson et al., 1988; Homans et al., 1988; Roberts et al., 1988; Schneider et al., 1990; Guther et al., 1992; Deeg et al., 1992), suggestive of a shared biosynthetic pathway.

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    T3 - NATO ASI series. Series A: Life sciences

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    A2 - Wirtz, K. W. A.

    A2 - Packer, L.

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    Milne KG, Field RA, Ferguson MAJ. Biosynthesis of glycosyl-phosphatidylinositol protein snchors in African trypanosomes. In Wirtz KWA, Packer L, Gustafsson JA, Evangelopoulos AE, Changeux JP, editors, New developments in lipid—protein interactions and receptor function . New York: Plenum Press. 1993. p. 275-286. (NATO ASI series. Series A: Life sciences). https://doi.org/10.1007/978-1-4615-2860-9_26