Regulation of O-Linked N-Acetyl Glucosamine Transferase (OGT) through E6 Stimulation of the Ubiquitin Ligase Activity of E6AP.

Cell Line Cell Line, Tumor HEK293 Cells HeLa Cells Humans N-Acetylglucosaminyltransferases / metabolism Oncogene Proteins, Viral / metabolism Papillomaviridae / metabolism Proteasome Endopeptidase Complex / metabolism Ubiquitin / metabolism Ubiquitin-Protein Ligases / metabolism Ubiquitination / physiology
E6 E6AP O-GlcNAc O-GlcNAcylation OGT human papillomavirus ubiquitin ubiquitination

Journal

International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791

Informations de publication

Date de publication:
24 Sep 2021
Historique:
received: 29 07 2021
revised: 17 09 2021
accepted: 21 09 2021
entrez: 13 10 2021
pubmed: 14 10 2021
medline: 3 11 2021
Statut: epublish

Résumé

Glycosyltransferase OGT catalyzes the conjugation of O-linked β-D-N-acetylglucosamine (O-GlcNAc) to Ser and Thr residues of the cellular proteins and regulates many key processes in the cell. Here, we report the identification of OGT as a ubiquitination target of HECT-type E3 ubiquitin (UB) ligase E6AP, whose overexpression in HEK293 cells would induce the degradation of OGT. We also found that the expression of E6AP in HeLa cells with the endogenous expression of the E6 protein of the human papillomavirus (HPV) would accelerate OGT degradation by the proteasome and suppress O-GlcNAc modification of OGT substrates in the cell. Overall, our study establishes a new mechanism of OGT regulation by the ubiquitin-proteasome system (UPS) that mediates the crosstalk between protein ubiquitination and O-GlcNAcylation pathways underlying diverse cellular processes.

Identifiants

DOI: 10.3390/ijms221910286 PMID: 34638625 PMC: PMC8508608
pubmed: 34638625
pii: ijms221910286
doi: 10.3390/ijms221910286
pmc: PMC8508608
pii:
doi:

Substances chimiques

Oncogene Proteins, Viral 0
Ubiquitin 0
UBE3A protein, human EC 2.3.2.26
Ubiquitin-Protein Ligases EC 2.3.2.27
N-Acetylglucosaminyltransferases EC 2.4.1.-
OGT protein, human EC 2.4.1.255
Proteasome Endopeptidase Complex EC 3.4.25.1

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : National Natural Science Foundation of China
ID : 31770921;31971187
Organisme : Science and Technology Commission of Shanghai Municipality Project
ID : 20JC1411200
Organisme : NIH HHS
ID : R01GM104498
Pays : United States
Organisme : National Science Foundation
ID : 1710460; 2109051

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Auteurs

Kangli Peng (K)

Engineering Research Center of Cell and Therapeutic Antibody, Ministry of Education, School of Pharmacy, Shanghai Jiao Tong University, Shanghai 200240, China.
Department of Chemistry, Center for Diagnostics and Therapeutics, Georgia State University, Atlanta, GA 30303, USA.
ORCID: 0000-0003-1361-2340

Ruochuan Liu (R)

Department of Chemistry, Center for Diagnostics and Therapeutics, Georgia State University, Atlanta, GA 30303, USA.

Caiwei Jia (C)

Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai 100864, China.

Yiyang Wang (Y)

Department of Pathophysiology, School of Medicine, Jinan University, Guangzhou 510632, China.

Geon H Jeong (GH)

Department of Chemistry, Center for Diagnostics and Therapeutics, Georgia State University, Atlanta, GA 30303, USA.

Li Zhou (L)

Department of Chemistry, Center for Diagnostics and Therapeutics, Georgia State University, Atlanta, GA 30303, USA.

Ronggui Hu (R)

Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai 100864, China.

Hiroaki Kiyokawa (H)

Department of Pharmacology, Northwestern University, Chicago, IL 60611, USA.
ORCID: 0000-0002-7942-6455

Jun Yin (J)

Department of Chemistry, Center for Diagnostics and Therapeutics, Georgia State University, Atlanta, GA 30303, USA.

Bo Zhao (B)

Engineering Research Center of Cell and Therapeutic Antibody, Ministry of Education, School of Pharmacy, Shanghai Jiao Tong University, Shanghai 200240, China.
ORCID: 0000-0001-7188-5959

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Classifications MeSH

Recherchemedicale.com › Cellules › Cellules cultivées › Lignée cellulaire › Regulation of O-Linked N-Acetyl Glucosamine...
Recherchemedicale.com › Cellules › Cellules cultivées › Cellules cancéreuses en culture › Lignée cellulaire tumorale › Regulation of O-Linked N-Acetyl Glucosamine...
Recherchemedicale.com › Cellules › Cellules épithéliales › Cellules HEK293 › Regulation of O-Linked N-Acetyl Glucosamine...
Recherchemedicale.com › Cellules › Cellules épithéliales › Cellules HeLa › Regulation of O-Linked N-Acetyl Glucosamine...
Recherchemedicale.com › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Regulation of O-Linked N-Acetyl Glucosamine...
Recherchemedicale.com › Enzymes et coenzymes › Enzymes › Transferases › Glycosyltransferase › N-acetylhexosaminyltransferase › N-acetylglucosaminyltransferase › Regulation of O-Linked N-Acetyl Glucosamine...
Recherchemedicale.com › Acides aminés, peptides et protéines › Protéines › Protéines virales › Protéines des oncogènes viraux › Regulation of O-Linked N-Acetyl Glucosamine...
Recherchemedicale.com › Virus › Virus oncogènes › Virus tumoraux à ADN › Papillomaviridae › Regulation of O-Linked N-Acetyl Glucosamine...
Recherchemedicale.com › Enzymes et coenzymes › Enzymes › Complexes multienzymatiques › Proteasome endopeptidase complex › Regulation of O-Linked N-Acetyl Glucosamine...
Recherchemedicale.com › Acides aminés, peptides et protéines › Protéines › Ubiquitines › Ubiquitine › Regulation of O-Linked N-Acetyl Glucosamine...
Recherchemedicale.com › Enzymes et coenzymes › Enzymes › Ligases › Ubiquitin-protein ligase complexes › Ubiquitin-protein ligases › Regulation of O-Linked N-Acetyl Glucosamine...
Recherchemedicale.com › Phénomènes génétiques › Régulation de l'expression des gènes › Modification traductionnelle des protéines › Maturation post-traductionnelle des protéines › Ubiquitination › Regulation of O-Linked N-Acetyl Glucosamine...