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Glycosylation of Nuclear and Cytoplasmic Proteins Is as Abundant and as Dynamic as Phosphorylation

  • Conference paper
Glyco-and Cellbiology

Abstract

While probing murine lymphocyte cell surfaces with bovine milk galactosyltrans-ferase, we discovered a new form of protein glycosylation in which single N-acetylglucosamine monosaccharides are O-glycosidically linked to serine or threonine moieties (O-GlcNAc) (Torres and Hart 1984). Surprisingly, O-GlcNAc is highly abundant (lymphocytes have > 1.5 × 108 molecules/cell), and is exclusively localized in nucleoplasmic and cytoplasmic compartments of the cell (Kearse and Hart 1991b). Based upon probing with galactosyltransferase (Whiteheart et al. 1989), a myriad of proteins in both the nucleus and cytoplasm are modified by O-GlcNAc. O-GlcNAc has been found in eukaryotes from yeast to man (Haltiwanger et al. 1992b; Hart et al. 1989), but has not yet been detected in prokaryotes. Identified O-GlcNAc-bearing proteins are listed in Table 1. These intracellular glycoproteins have a diverse range of functions, including transcription regulatory factors, enzymes, nuclear pore proteins, cytoskeletal proteins, and viral proteins. However, all of these glycoproteins are also phosphoproteins that form reversible multimeric complexes, depending upon their phosphorylation states, thus suggesting that O-GlcNAc may playa role in mediating/modulating regulated and reversible protein subunit interactions.

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Authors and Affiliations

  1. Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham Schools of Medicine/Dentistry, 1918 University Boulevard, AL 35294-0005, Birmingham, USA

    K. Greis

Authors
  1. G. W. Hart
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  2. W. G. Kelly
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  3. M. A. Blomberg
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  4. E. P. Roquemore
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  5. L.-Y. Dong
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  6. L. Kreppel
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  7. T.-Y. Chou
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  8. D. Snow
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  9. K. Greis
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Editor information

Editors and Affiliations

  1. Institut für Biochemie I der Universität, Universität Heidelberg, Im Neuenheimer Feld 328, D-69120, Heidelberg, Germany

    Felix Wieland

  2. Institut für Molekularbiologie und Biochemie, Freie Universität Berlin, Arnimallee 22, D-14195, Berlin, Germany

    Werner Reutter

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© 1994 Springer-Verlag Berlin Heidelberg

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Hart, G.W. et al. (1994). Glycosylation of Nuclear and Cytoplasmic Proteins Is as Abundant and as Dynamic as Phosphorylation. 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_10

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  • DOI: https://doi.org/10.1007/978-3-642-78729-4_10

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-78731-7

  • Online ISBN: 978-3-642-78729-4

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