Abstract
// Xinling Zhang 1 , Yuchao Gu 2 , Wengong Yu 2 and Hui Liang 1 1 The Institute of Human Nutrition, Medical College of Qingdao University, Qingdao 266021, China 2 Key Laboratory of Marine Drugs, Chinese Ministry of Education, Key Laboratory of Glycoscience and Glycotechnology of Shandong Province; School of Medicine and Pharmacy, Ocean University of China, Qingdao 266003, China Correspondence to: Hui Liang, email: ajgqdfy@163.com Xinling Zhang, email: ruoxi_67@163.com Keywords: OGT; O-GlcNAcylation; expression; protein stability; activity Received: June 14, 2017 Accepted: November 03, 2017 Published: January 02, 2018 ABSTRACT O-GlcNAc Transferase (OGT) resides in both cytosolic and nuclear compartments and catalyzes O-GlcNAcylation of myriad proteins. Numerous excellent reviews concerning roles of OGT in organismal and cellular physiology have exist, and aberrant OGT and protein O-GlcNAcylation have been implicated in progression and metastasis of different cancer types. Thus, understanding the regulation mechanisms of OGT and O-GlcNAcylation in tumor cells and their difference compared to non-tumor cells may elucidate new mechanisms related to tumor generation and development, could provide a new marker to diagnosis and prognosis in patients with cancer and indicate a new target to cancer chemotherapy. While it has become evident that OGT plays critical roles in cancers, it remains unclear how they are deregulated. This review provides an overview of our current knowledge about the known/potential regulation of OGT, and also discusses the inhibition of OGT as a potential novel therapeutic target for cancer treatment.
Highlights
O-GlcNAcylation is the covalent connection of O-GlcNAc sugars to serine or threonine residues of nuclear and cytoplasmic proteins in metazoans [1,2,3,4,5]
Given the myriad functions concerned with O-GlcNAcylation, it is exceedingly reasonable that this posttranslational modification plays a fundamental role in the etiology of tumors [6, 14, 26,27,28]
Deregulation of O-GlcNAcylation is an event detected in a variety of cancer types and this aberrant O-GlcNAcylation is conducive to tumorigenesis, cell proliferation, invasion and metastasis, and resists to therapy
Summary
O-GlcNAcylation is the covalent connection of O-GlcNAc sugars to serine or threonine residues of nuclear and cytoplasmic proteins in metazoans [1,2,3,4,5].
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