NDLI: Altered Golgi Localization of Core 2 β-1,6-N-Acetylglucosaminyltransferase Leads to Decreased Synthesis of Branched O-Glycans

Content Provider	Journal of Biological Chemistry (JBC)
Author	Skrincosky, David Kain, Renate El-Battari, Assou Exner, Markus Kerjaschki, Dontscho Fukuda, Minoru
Abstract	Mucin type O-glycans with core 2 branches are distinct from nonbranched O-glycans, and the amount of core 2 branched O-glycans changes dramatically during T cell differentiation. This oligosaccharide is synthesized only when core 2 β-1,6-N-acetylglucosaminyltransferase (C2GnT) is present, and the expression of this glycosyltransferase is highly regulated. To understand how O-glycan synthesis is regulated by the orderly appearance of glycosyltransferases that form core 2 branched O-glycans, the subcellular localization of C2GnT was determined by using antibodies generated that are specific to C2GnT. The studies using confocal light microscopy demonstrated that C2GnT was localized mainly in cis tomedial-cisternae of the Golgi. We then converted C2GnT to atrans-Golgi enzyme by replacing its Golgi retention signal with that of α-2,6-sialyltransferase, which resides intrans-Golgi. Chinese hamster ovary cells expressing wild type C2GnT and the chimeric C2GnT were then subjected to oligosaccharide analysis. The results obtained clearly indicate that the conversion of C2GnT into a trans-Golgi enzyme resulted in a substantial decrease of core 2 branched oligosaccharides.These results, taken together, strongly suggest that the predominance of core 2 branched oligosaccharides in those cells expressing C2GnT is due to the fact that C2GnT is located earlier in the Golgi than α-2,3-sialyltransferase that competes with C2GnT for the common substrate. Furthermore, alteration of Golgi localization renders the chimeric C2GnT much less efficient in synthesizing core 2 branched oligosaccharides, indicating the critical role of orderly subcellular localization of glycosyltransferases.
Related Links	http://www.jbc.org/content/272/36/22695.abstract
Ending Page	22702
Starting Page	22695
Page Count	8
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	36
Volume Number	272
DOI	10.1074/jbc.272.36.22695
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	1997-09-05
Access Restriction	Open
Subject Keyword	CARBOHYDRATES, LIPIDS, AND OTHER NATURAL PRODUCTS
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Tissue-specific Regulation of Mouse Core 2 β-1,6-N-Acetylglucosaminyltransferase

Synthesis of Poly-N-acetyllactosamine in Core 2 Branched O-Glycans THE REQUIREMENT OF NOVEL β-1,4-GALACTOSYLTRANSFERASE IV AND β-1,3-N-ACETYLGLUCOSAMINYLTRANSFERASE

Molecular Cloning and Expression of a Novel β-1,6-N-Acetylglucosaminyltransferase That Forms Core 2, Core 4, and I Branches

Biosynthesis ofO-N-Acetylglucosamine-linked Glycans inTrypanosoma cruzi CHARACTERIZATION OF THE NOVEL URIDINE DIPHOSPHO-N-ACETYLGLUCOSAMINE:POLYPEPTIDE N-ACETYLGLUCOSAMINYLTRANSFERASE-CATALYZING FORMATION OFN-ACETYLGLUCOSAMINE α1→O-THREONINE

Biosynthesis of Branched Polylactosaminoglycans EMBRYONAL CARCINOMA CELLS EXPRESS MIDCHAIN β1,6-N-ACETYLGLUCOSAMINYLTRANSFERASE ACTIVITY THAT GENERATES BRANCHES TO PREFORMED LINEAR BACKBONES

Expression of a differentiation antigen and poly-N-acetyllactosaminyl O-glycans directed by a cloned core 2 beta-1,6-N-acetylglucosaminyltransferase.

Molecular Cloning and Expression of cDNA Encoding the Rat UDP-N-Acetylglucosamine:α-6-D-Mannoside β-1,2-N-Acetylglucosaminyltransferase II

Transforming Growth Factor β Up-regulates Expression of the N-Acetylglucosaminyltransferase V Gene in Mouse Melanoma Cells

Circular Dichroic Spectroscopy of N-Acetylglucosaminyltransferase V and Its Substrate Interactions

Altered Golgi Localization of Core 2 β-1,6-N-Acetylglucosaminyltransferase Leads to Decreased Synthesis of Branched O-Glycans

Similar Documents

Tissue-specific Regulation of Mouse Core 2 β-1,6-N-Acetylglucosaminyltransferase

Synthesis of Poly-N-acetyllactosamine in Core 2 Branched O-Glycans THE REQUIREMENT OF NOVEL β-1,4-GALACTOSYLTRANSFERASE IV AND β-1,3-N-ACETYLGLUCOSAMINYLTRANSFERASE

Molecular Cloning and Expression of a Novel β-1,6-N-Acetylglucosaminyltransferase That Forms Core 2, Core 4, and I Branches

Biosynthesis ofO-N-Acetylglucosamine-linked Glycans inTrypanosoma cruzi CHARACTERIZATION OF THE NOVEL URIDINE DIPHOSPHO-N-ACETYLGLUCOSAMINE:POLYPEPTIDE N-ACETYLGLUCOSAMINYLTRANSFERASE-CATALYZING FORMATION OFN-ACETYLGLUCOSAMINE α1→O-THREONINE

Biosynthesis of Branched Polylactosaminoglycans EMBRYONAL CARCINOMA CELLS EXPRESS MIDCHAIN β1,6-N-ACETYLGLUCOSAMINYLTRANSFERASE ACTIVITY THAT GENERATES BRANCHES TO PREFORMED LINEAR BACKBONES

Expression of a differentiation antigen and poly-N-acetyllactosaminyl O-glycans directed by a cloned core 2 beta-1,6-N-acetylglucosaminyltransferase.

Molecular Cloning and Expression of cDNA Encoding the Rat UDP-N-Acetylglucosamine:α-6-D-Mannoside β-1,2-N-Acetylglucosaminyltransferase II

Transforming Growth Factor β Up-regulates Expression of the N-Acetylglucosaminyltransferase V Gene in Mouse Melanoma Cells

Circular Dichroic Spectroscopy of N-Acetylglucosaminyltransferase V and Its Substrate Interactions

Altered Golgi Localization of Core 2 β-1,6-N-Acetylglucosaminyltransferase Leads to Decreased Synthesis of Branched O-Glycans