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Nutrient Regulation of Cancer Cells by O-GlcNAcylation

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Glycosignals in Cancer: Mechanisms of Malignant Phenotypes

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Abstract

O-linked β-N-acetylglucosamine (O-GlcNAc) is a ubiquitous and dynamic posttranslational modification that occurs on serine/threonine residues of nuclear and cytoplasmic proteins. This modification is regulated by O-GlcNAc transferase (OGT), which attaches O-GlcNAc to proteins and O-GlcNAcase (OGA), which removes O-GlcNAc. O-GlcNAc serves as a nutrient sensor to regulate virtually all cellular processes, as well as playing roles in various diseases, including Alzheimer’s disease, diabetes, and cancer. In this chapter, we present an overview of O-GlcNAcylation in different kinds of cancer.

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Authors and Affiliations

  1. Department of Biological Chemistry, School of Medicine, Johns Hopkins University, WBSB515, 725N. Wolfe St., Baltimore, MD, 21205, USA

    Xin Liu & Gerald W. Hart

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  1. Xin Liu
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  2. Gerald W. Hart
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Correspondence to Gerald W. Hart .

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  1. Biomedical Sciences, Chubu University, Kasugai, Japan

    Koichi Furukawa

  2. Glycobiology Unit, Sanford-Burnham Med Res Inst, La Jolla, California, USA

    Minoru Fukuda

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Liu, X., Hart, G.W. (2016). Nutrient Regulation of Cancer Cells by O-GlcNAcylation. In: Furukawa, K., Fukuda, M. (eds) Glycosignals in Cancer: Mechanisms of Malignant Phenotypes . Springer, Tokyo. https://doi.org/10.1007/978-4-431-55939-9_6

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