Nutrient regulation of cancer cells by o-glcnacylation

Xin Liu; Gerald Warren Hart

doi:10.1007/978-4-431-55939-9_6

Nutrient regulation of cancer cells by o-glcnacylation

Xin Liu, Gerald Warren Hart

School of Medicine

Research output: Chapter in Book/Report/Conference proceeding › Chapter

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.

Original language	English (US)
Title of host publication	Glycosignals in Cancer: Mechanisms of Malignant Phenotypes
Publisher	Springer Japan
Pages	95-108
Number of pages	14
ISBN (Print)	9784431559399, 9784431559375
DOIs	https://doi.org/10.1007/978-4-431-55939-9_6
State	Published - Jan 1 2016

Keywords

Cancer
Nutrients
O-glcnac
O-glcnac transferase
O-glcnacase
Oga
Ogt

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)
Medicine(all)

Access to Document

10.1007/978-4-431-55939-9_6

Cite this

@inbook{cd348e57b05443f780947b89bf1c4de7,

title = "Nutrient regulation of cancer cells by o-glcnacylation",

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{\textquoteright}s disease, diabetes, and cancer. In this chapter, we present an overview of O-GlcNAcylation in different kinds of cancer.",

keywords = "Cancer, Nutrients, O-glcnac, O-glcnac transferase, O-glcnacase, Oga, Ogt",

author = "Xin Liu and Hart, {Gerald Warren}",

year = "2016",

month = jan,

day = "1",

doi = "10.1007/978-4-431-55939-9_6",

language = "English (US)",

isbn = "9784431559399",

pages = "95--108",

booktitle = "Glycosignals in Cancer: Mechanisms of Malignant Phenotypes",

publisher = "Springer Japan",

}

TY - CHAP

T1 - Nutrient regulation of cancer cells by o-glcnacylation

AU - Liu, Xin

AU - Hart, Gerald Warren

PY - 2016/1/1

Y1 - 2016/1/1

N2 - 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.

AB - 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.

KW - Cancer

KW - Nutrients

KW - O-glcnac

KW - O-glcnac transferase

KW - O-glcnacase

KW - Oga

KW - Ogt

UR - http://www.scopus.com/inward/record.url?scp=84960472843&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84960472843&partnerID=8YFLogxK

U2 - 10.1007/978-4-431-55939-9_6

DO - 10.1007/978-4-431-55939-9_6

M3 - Chapter

AN - SCOPUS:84960472843

SN - 9784431559399

SN - 9784431559375

SP - 95

EP - 108

BT - Glycosignals in Cancer: Mechanisms of Malignant Phenotypes

PB - Springer Japan

ER -

Nutrient regulation of cancer cells by o-glcnacylation

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this