Regulation of glycosyltransferases in ganglioside biosynthesis by phosphorylation and dephosphorylation

Robert K Yu, Erhard Bieberich

Research output: Contribution to journalReview article

14 Citations (Scopus)

Abstract

The biosynthesis of gangliosides is known to be under strict metabolic control. One level of control is through post-translational modification of the glycosyltransferases responsible for their biosynthesis. Thus, the activities of several sialyltransferases have been demonstrated to be downregulated by the action of protein kinase C (PKC) in cell-free and intact cell systems. This modulatory effect can be reversed at least in part by the action of membrane-bound phosphatases. In contrast, the activity of N-acetylgalactosaminyltransferase can be upregulated by the action of protein kinase A (PKA) in cultured cells. In addition, studies from several laboratories have demonstrated that phosphorylation of certain glycosyltransferases can affect their intracellular processing and translocation. Thus, modulation of glycosyltransferases by phosphorylation and dephosphorylation should represent an important regulatory mechanism for ganglioside biosynthesis.

Original languageEnglish (US)
Pages (from-to)19-24
Number of pages6
JournalMolecular and Cellular Endocrinology
Volume177
Issue number1-2
DOIs
StatePublished - May 25 2001

Fingerprint

Glycosyltransferases
Phosphorylation
Gangliosides
Biosynthesis
N-Acetylgalactosaminyltransferases
Sialyltransferases
Cell-Free System
Post Translational Protein Processing
Cyclic AMP-Dependent Protein Kinases
Phosphoric Monoester Hydrolases
Protein Kinase C
Cultured Cells
Down-Regulation
Cells
Modulation
Membranes
Processing

Keywords

  • Dephosphorylation
  • Ganglioside
  • Glycosyltransferase
  • Phosphorylation
  • Protein kinase A
  • Protein kinase C
  • Sialyltransferase

ASJC Scopus subject areas

  • Endocrinology
  • Endocrinology, Diabetes and Metabolism

Cite this

Regulation of glycosyltransferases in ganglioside biosynthesis by phosphorylation and dephosphorylation. / Yu, Robert K; Bieberich, Erhard.

In: Molecular and Cellular Endocrinology, Vol. 177, No. 1-2, 25.05.2001, p. 19-24.

Research output: Contribution to journalReview article

@article{fb0f92fcae4749fb97d84a48a9e9af51,
title = "Regulation of glycosyltransferases in ganglioside biosynthesis by phosphorylation and dephosphorylation",
abstract = "The biosynthesis of gangliosides is known to be under strict metabolic control. One level of control is through post-translational modification of the glycosyltransferases responsible for their biosynthesis. Thus, the activities of several sialyltransferases have been demonstrated to be downregulated by the action of protein kinase C (PKC) in cell-free and intact cell systems. This modulatory effect can be reversed at least in part by the action of membrane-bound phosphatases. In contrast, the activity of N-acetylgalactosaminyltransferase can be upregulated by the action of protein kinase A (PKA) in cultured cells. In addition, studies from several laboratories have demonstrated that phosphorylation of certain glycosyltransferases can affect their intracellular processing and translocation. Thus, modulation of glycosyltransferases by phosphorylation and dephosphorylation should represent an important regulatory mechanism for ganglioside biosynthesis.",
keywords = "Dephosphorylation, Ganglioside, Glycosyltransferase, Phosphorylation, Protein kinase A, Protein kinase C, Sialyltransferase",
author = "Yu, {Robert K} and Erhard Bieberich",
year = "2001",
month = "5",
day = "25",
doi = "10.1016/S0303-7207(01)00457-9",
language = "English (US)",
volume = "177",
pages = "19--24",
journal = "Molecular and Cellular Endocrinology",
issn = "0303-7207",
publisher = "Elsevier Ireland Ltd",
number = "1-2",

}

TY - JOUR

T1 - Regulation of glycosyltransferases in ganglioside biosynthesis by phosphorylation and dephosphorylation

AU - Yu, Robert K

AU - Bieberich, Erhard

PY - 2001/5/25

Y1 - 2001/5/25

N2 - The biosynthesis of gangliosides is known to be under strict metabolic control. One level of control is through post-translational modification of the glycosyltransferases responsible for their biosynthesis. Thus, the activities of several sialyltransferases have been demonstrated to be downregulated by the action of protein kinase C (PKC) in cell-free and intact cell systems. This modulatory effect can be reversed at least in part by the action of membrane-bound phosphatases. In contrast, the activity of N-acetylgalactosaminyltransferase can be upregulated by the action of protein kinase A (PKA) in cultured cells. In addition, studies from several laboratories have demonstrated that phosphorylation of certain glycosyltransferases can affect their intracellular processing and translocation. Thus, modulation of glycosyltransferases by phosphorylation and dephosphorylation should represent an important regulatory mechanism for ganglioside biosynthesis.

AB - The biosynthesis of gangliosides is known to be under strict metabolic control. One level of control is through post-translational modification of the glycosyltransferases responsible for their biosynthesis. Thus, the activities of several sialyltransferases have been demonstrated to be downregulated by the action of protein kinase C (PKC) in cell-free and intact cell systems. This modulatory effect can be reversed at least in part by the action of membrane-bound phosphatases. In contrast, the activity of N-acetylgalactosaminyltransferase can be upregulated by the action of protein kinase A (PKA) in cultured cells. In addition, studies from several laboratories have demonstrated that phosphorylation of certain glycosyltransferases can affect their intracellular processing and translocation. Thus, modulation of glycosyltransferases by phosphorylation and dephosphorylation should represent an important regulatory mechanism for ganglioside biosynthesis.

KW - Dephosphorylation

KW - Ganglioside

KW - Glycosyltransferase

KW - Phosphorylation

KW - Protein kinase A

KW - Protein kinase C

KW - Sialyltransferase

UR - http://www.scopus.com/inward/record.url?scp=0035946992&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035946992&partnerID=8YFLogxK

U2 - 10.1016/S0303-7207(01)00457-9

DO - 10.1016/S0303-7207(01)00457-9

M3 - Review article

VL - 177

SP - 19

EP - 24

JO - Molecular and Cellular Endocrinology

JF - Molecular and Cellular Endocrinology

SN - 0303-7207

IS - 1-2

ER -