Nutrient regulation of signaling and transcription

In the early 1980s, while using purified glycosyltransferases to probe glycan structures on surfaces of living cells in the murine immune system, we discovered a novel form of serine/threonine protein glycosylation (O-linked β-GlcNAc; O-GlcNAc) that occurs on thousands of proteins within the nucleus...

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Bibliographic Details
Published inThe Journal of biological chemistry Vol. 294; no. 7; pp. 2211 - 2231
Main Author Hart, Gerald W.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 15.02.2019
American Society for Biochemistry and Molecular Biology
Subjects
Aging - metabolism
Aging - pathology
Alzheimer's disease
Animals
ASBMB Award
Caenorhabditis elegans - metabolism
Caenorhabditis elegans Proteins - metabolism
cancer
Chronic Disease
Cytoskeleton - metabolism
Cytoskeleton - pathology
diabetes
Diabetes Mellitus - metabolism
Diabetes Mellitus - pathology
Glycosylation
Humans
kinases
Mice
Mitochondria - metabolism
Mitochondria - pathology
N-Acetylglucosaminyltransferases - metabolism
Neoplasm Proteins - metabolism
Neoplasms - metabolism
Neoplasms - pathology
neurodegeneration
Neurodegenerative Diseases - metabolism
Neurodegenerative Diseases - pathology
Nutrients - metabolism
O-GlcNAcase
O-GlcNAcylation
O-linked N-acetylglucosamine (O-GlcNAc)
O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT)
Phosphorylation
Signal Transduction
Transcription, Genetic
O-linked N-acetylglucosamine (O-GlcNAc)
kinases
O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT)
neurodegeneration
O-GlcNAcase
O-GlcNAcylation
cancer
phosphorylation
diabetes
Alzheimer's disease
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Abstract In the early 1980s, while using purified glycosyltransferases to probe glycan structures on surfaces of living cells in the murine immune system, we discovered a novel form of serine/threonine protein glycosylation (O-linked β-GlcNAc; O-GlcNAc) that occurs on thousands of proteins within the nucleus, cytoplasm, and mitochondria. Prior to this discovery, it was dogma that protein glycosylation was restricted to the luminal compartments of the secretory pathway and on extracellular domains of membrane and secretory proteins. Work in the last 3 decades from several laboratories has shown that O-GlcNAc cycling serves as a nutrient sensor to regulate signaling, transcription, mitochondrial activity, and cytoskeletal functions. O-GlcNAc also has extensive cross-talk with phosphorylation, not only at the same or proximal sites on polypeptides, but also by regulating each other’s enzymes that catalyze cycling of the modifications. O-GlcNAc is generally not elongated or modified. It cycles on and off polypeptides in a time scale similar to phosphorylation, and both the enzyme that adds O-GlcNAc, the O-GlcNAc transferase (OGT), and the enzyme that removes O-GlcNAc, O-GlcNAcase (OGA), are highly conserved from C. elegans to humans. Both O-GlcNAc cycling enzymes are essential in mammals and plants. Due to O-GlcNAc’s fundamental roles as a nutrient and stress sensor, it plays an important role in the etiologies of chronic diseases of aging, including diabetes, cancer, and neurodegenerative disease. This review will present an overview of our current understanding of O-GlcNAc’s regulation, functions, and roles in chronic diseases of aging.
AbstractList In the early 1980s, while using purified glycosyltransferases to probe glycan structures on surfaces of living cells in the murine immune system, we discovered a novel form of serine/threonine protein glycosylation ( -linked β-GlcNAc; -GlcNAc) that occurs on thousands of proteins within the nucleus, cytoplasm, and mitochondria. Prior to this discovery, it was dogma that protein glycosylation was restricted to the luminal compartments of the secretory pathway and on extracellular domains of membrane and secretory proteins. Work in the last 3 decades from several laboratories has shown that -GlcNAc cycling serves as a nutrient sensor to regulate signaling, transcription, mitochondrial activity, and cytoskeletal functions. -GlcNAc also has extensive cross-talk with phosphorylation, not only at the same or proximal sites on polypeptides, but also by regulating each other's enzymes that catalyze cycling of the modifications. -GlcNAc is generally not elongated or modified. It cycles on and off polypeptides in a time scale similar to phosphorylation, and both the enzyme that adds -GlcNAc, the -GlcNAc transferase (OGT), and the enzyme that removes -GlcNAc, -GlcNAcase (OGA), are highly conserved from to humans. Both -GlcNAc cycling enzymes are essential in mammals and plants. Due to -GlcNAc's fundamental roles as a nutrient and stress sensor, it plays an important role in the etiologies of chronic diseases of aging, including diabetes, cancer, and neurodegenerative disease. This review will present an overview of our current understanding of -GlcNAc's regulation, functions, and roles in chronic diseases of aging.
In the early 1980s, while using purified glycosyltransferases to probe glycan structures on surfaces of living cells in the murine immune system, we discovered a novel form of serine/threonine protein glycosylation (O-linked β-GlcNAc; O-GlcNAc) that occurs on thousands of proteins within the nucleus, cytoplasm, and mitochondria. Prior to this discovery, it was dogma that protein glycosylation was restricted to the luminal compartments of the secretory pathway and on extracellular domains of membrane and secretory proteins. Work in the last 3 decades from several laboratories has shown that O-GlcNAc cycling serves as a nutrient sensor to regulate signaling, transcription, mitochondrial activity, and cytoskeletal functions. O-GlcNAc also has extensive cross-talk with phosphorylation, not only at the same or proximal sites on polypeptides, but also by regulating each other's enzymes that catalyze cycling of the modifications. O-GlcNAc is generally not elongated or modified. It cycles on and off polypeptides in a time scale similar to phosphorylation, and both the enzyme that adds O-GlcNAc, the O-GlcNAc transferase (OGT), and the enzyme that removes O-GlcNAc, O-GlcNAcase (OGA), are highly conserved from C. elegans to humans. Both O-GlcNAc cycling enzymes are essential in mammals and plants. Due to O-GlcNAc's fundamental roles as a nutrient and stress sensor, it plays an important role in the etiologies of chronic diseases of aging, including diabetes, cancer, and neurodegenerative disease. This review will present an overview of our current understanding of O-GlcNAc's regulation, functions, and roles in chronic diseases of aging.In the early 1980s, while using purified glycosyltransferases to probe glycan structures on surfaces of living cells in the murine immune system, we discovered a novel form of serine/threonine protein glycosylation (O-linked β-GlcNAc; O-GlcNAc) that occurs on thousands of proteins within the nucleus, cytoplasm, and mitochondria. Prior to this discovery, it was dogma that protein glycosylation was restricted to the luminal compartments of the secretory pathway and on extracellular domains of membrane and secretory proteins. Work in the last 3 decades from several laboratories has shown that O-GlcNAc cycling serves as a nutrient sensor to regulate signaling, transcription, mitochondrial activity, and cytoskeletal functions. O-GlcNAc also has extensive cross-talk with phosphorylation, not only at the same or proximal sites on polypeptides, but also by regulating each other's enzymes that catalyze cycling of the modifications. O-GlcNAc is generally not elongated or modified. It cycles on and off polypeptides in a time scale similar to phosphorylation, and both the enzyme that adds O-GlcNAc, the O-GlcNAc transferase (OGT), and the enzyme that removes O-GlcNAc, O-GlcNAcase (OGA), are highly conserved from C. elegans to humans. Both O-GlcNAc cycling enzymes are essential in mammals and plants. Due to O-GlcNAc's fundamental roles as a nutrient and stress sensor, it plays an important role in the etiologies of chronic diseases of aging, including diabetes, cancer, and neurodegenerative disease. This review will present an overview of our current understanding of O-GlcNAc's regulation, functions, and roles in chronic diseases of aging.
In the early 1980s, while using purified glycosyltransferases to probe glycan structures on surfaces of living cells in the murine immune system, we discovered a novel form of serine/threonine protein glycosylation (O-linked β-GlcNAc; O-GlcNAc) that occurs on thousands of proteins within the nucleus, cytoplasm, and mitochondria. Prior to this discovery, it was dogma that protein glycosylation was restricted to the luminal compartments of the secretory pathway and on extracellular domains of membrane and secretory proteins. Work in the last 3 decades from several laboratories has shown that O-GlcNAc cycling serves as a nutrient sensor to regulate signaling, transcription, mitochondrial activity, and cytoskeletal functions. O-GlcNAc also has extensive cross-talk with phosphorylation, not only at the same or proximal sites on polypeptides, but also by regulating each other’s enzymes that catalyze cycling of the modifications. O-GlcNAc is generally not elongated or modified. It cycles on and off polypeptides in a time scale similar to phosphorylation, and both the enzyme that adds O-GlcNAc, the O-GlcNAc transferase (OGT), and the enzyme that removes O-GlcNAc, O-GlcNAcase (OGA), are highly conserved from C. elegans to humans. Both O-GlcNAc cycling enzymes are essential in mammals and plants. Due to O-GlcNAc’s fundamental roles as a nutrient and stress sensor, it plays an important role in the etiologies of chronic diseases of aging, including diabetes, cancer, and neurodegenerative disease. This review will present an overview of our current understanding of O-GlcNAc’s regulation, functions, and roles in chronic diseases of aging.
In the early 1980s, while using purified glycosyltransferases to probe glycan structures on surfaces of living cells in the murine immune system, we discovered a novel form of serine/threonine protein glycosylation ( O -linked β-GlcNAc; O -GlcNAc) that occurs on thousands of proteins within the nucleus, cytoplasm, and mitochondria. Prior to this discovery, it was dogma that protein glycosylation was restricted to the luminal compartments of the secretory pathway and on extracellular domains of membrane and secretory proteins. Work in the last 3 decades from several laboratories has shown that O -GlcNAc cycling serves as a nutrient sensor to regulate signaling, transcription, mitochondrial activity, and cytoskeletal functions. O -GlcNAc also has extensive cross-talk with phosphorylation, not only at the same or proximal sites on polypeptides, but also by regulating each other's enzymes that catalyze cycling of the modifications. O -GlcNAc is generally not elongated or modified. It cycles on and off polypeptides in a time scale similar to phosphorylation, and both the enzyme that adds O -GlcNAc, the O -GlcNAc transferase (OGT), and the enzyme that removes O -GlcNAc, O -GlcNAcase (OGA), are highly conserved from C. elegans to humans. Both O -GlcNAc cycling enzymes are essential in mammals and plants. Due to O -GlcNAc's fundamental roles as a nutrient and stress sensor, it plays an important role in the etiologies of chronic diseases of aging, including diabetes, cancer, and neurodegenerative disease. This review will present an overview of our current understanding of O -GlcNAc's regulation, functions, and roles in chronic diseases of aging.
Author Hart, Gerald W.
Author_xml – sequence: 1
  givenname: Gerald W.
  surname: Hart
  fullname: Hart, Gerald W.
  email: gerald.hart@uga.edu
  organization: From the Complex Carbohydrate Research Center and Biochemistry and Molecular Biology Department, University of Georgia, Athens, Georgia 30602
BackLink https://www.ncbi.nlm.nih.gov/pubmed/30626734$$D View this record in MEDLINE/PubMed
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Keywords O-linked N-acetylglucosamine (O-GlcNAc)
kinases
O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT)
neurodegeneration
O-GlcNAcase
O-GlcNAcylation
cancer
phosphorylation
diabetes
Alzheimer's disease
Language English
License This is an open access article under the CC BY license.
2019 Hart.
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Snippet In the early 1980s, while using purified glycosyltransferases to probe glycan structures on surfaces of living cells in the murine immune system, we discovered...
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SubjectTerms Aging - metabolism
Aging - pathology
Alzheimer's disease
Animals
ASBMB Award
Caenorhabditis elegans - metabolism
Caenorhabditis elegans Proteins - metabolism
cancer
Chronic Disease
Cytoskeleton - metabolism
Cytoskeleton - pathology
diabetes
Diabetes Mellitus - metabolism
Diabetes Mellitus - pathology
Glycosylation
Humans
kinases
Mice
Mitochondria - metabolism
Mitochondria - pathology
N-Acetylglucosaminyltransferases - metabolism
Neoplasm Proteins - metabolism
Neoplasms - metabolism
Neoplasms - pathology
neurodegeneration
Neurodegenerative Diseases - metabolism
Neurodegenerative Diseases - pathology
Nutrients - metabolism
O-GlcNAcase
O-GlcNAcylation
O-linked N-acetylglucosamine (O-GlcNAc)
O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT)
Phosphorylation
Signal Transduction
Transcription, Genetic
Title Nutrient regulation of signaling and transcription
URI https://dx.doi.org/10.1074/jbc.AW119.003226
https://www.ncbi.nlm.nih.gov/pubmed/30626734
https://www.proquest.com/docview/2179355061
https://pubmed.ncbi.nlm.nih.gov/PMC6378989
Volume 294
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