NIH VideoCast - The split personality of human O-GlcNAc transferase

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The split personality of human O-GlcNAc transferase

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Air date:	Tuesday, April 18, 2017, 3:00:00 PM Time displayed is Eastern Time, Washington DC Local
Views:	Total views: 366 (129 Live, 237 On-demand)
Category:	WALS - Wednesday Afternoon Lectures
Runtime:	01:07:39
Closed captioning:	Check box to display CC outside of the video Note: You can drag the captioning window around and resize it
Description:	NIH Director’s Wednesday Afternoon Lecture Series O-GlcNAc Transferase (OGT) is a glycosyltransferase essential for the viability of most multicellular organisms, including mammals. It catalyzes the attachment of N-acetylglucosamine (GlcNAc) to serines and threonines of nuclear and cytoplasmic proteins, resulting in changes in protein localization, stability, and interactions. Protein O-GlcNAc levels are responsive to cellular glucose concentration, and chronically elevated O-GlcNAc levels are observed in both cancer and diabetes and are associated with widespread changes in gene expression. While the importance of OGT in the biology of multicellular organisms is clear, the molecular mechanisms underlying its effects remain poorly understood. Recently, OGT was reported to catalyze another post-translational modification: the cleavage of the essential cell-cycle regulator host cell factor 1 (HCF-1). Cleavage is required for proper HCF-1 function. Dr. Walker's laboratory has been working on the chemistry of OGT in order to lay the groundwork for exploring its biology. For her lecture, Dr. Walker will talk about her lab's structural work on OGT and describe what we have learned about the mechanism of O-GlcNAcylation and HCF-1 cleavage. She will also describe the development of cell-permeable OGT inhibitors and show how they bind to the enzyme. Finally, she will touch on how her lab's biochemical studies have provided information that may allow us to address a key question: Why is OGT essential for the viability of all dividing mammalian cells?

NLM Title:	The split personality of human o-GlcNAc transferase / Suzanne Walker, Ph.D., Professor of Microbiology and Immunobiology, Harvard Medical School.
Author:	Walker, Suzanne. National Institutes of Health (U.S.),
Publisher:
Abstract:	(CIT): NIH Director's Wednesday Afternoon Lecture Series. O-GlcNAc Transferase (OGT) is a glycosyltransferase essential for the viability of most multicellular organisms, including mammals. It catalyzes the attachment of N-acetylglucosamine (GlcNAc) to serines and threonines of nuclear and cytoplasmic proteins, resulting in changes in protein localization, stability, and interactions. Protein O-GlcNAc levels are responsive to cellular glucose concentration, and chronically elevated O-GlcNAc levels are observed in both cancer and diabetes and are associated with widespread changes in gene expression. While the importance of OGT in the biology of multicellular organisms is clear, the molecular mechanisms underlying its effects remain poorly understood. Recently, OGT was reported to catalyze another post-translational modification: the cleavage of the essential cell-cycle regulator host cell factor 1 (HCF-1). Cleavage is required for proper HCF-1 function. Dr. Walker's laboratory has been working on the chemistry of OGT in order to lay the groundwork for exploring its biology. For her lecture, Dr. Walker will talk about her lab's structural work on OGT and describe what we have learned about the mechanism of O-GlcNAcylation and HCF-1 cleavage. She will also describe the development of cell-permeable OGT inhibitors and show how they bind to the enzyme. Finally, she will touch on how her lab's biochemical studies have provided information that may allow us to address a key question: Why is OGT essential for the viability of all dividing mammalian cells?.
Subjects:	Cell Division Host Cell Factor C1 N-Acetylglucosaminyltransferases
Publication Types:	Lecture Webcast

NLM Classification:	QU 141
NLM ID:	101705358
CIT Live ID:	22141
Permanent link:	https://videocast.nih.gov/watch=22141

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