Control of glycogen synthase by hierarchal protein phosphorylation

Research output: Contribution to journalArticle

181 Citations (Scopus)

Abstract

Protein phosphorylation is one of the most common mechanisms for controlling protein function. We now know that most phosphoproteins contain multiple phosphorylation sites and that these sites are often located in clusters. From the study of the enzyme glycogen synthase, one mechanism for the formation of phosphorylation clusters has been discovered that involves the concerted action of two or more protein kinases. One protein kinase, the primary kinase, introduces a phosphate group that is a requirement for the action of another, secondary, protein kinase. Thus the multiple phosphorylation occurs in a hierarchal fashion. This mechanism, which is critical for the phosphorylation of glycogen synthase, is likely to be a much more widespread phenome non.

Original languageEnglish
Pages (from-to)2961-2968
Number of pages8
JournalFASEB Journal
Volume4
Issue number12
StatePublished - 1990

Fingerprint

glycogen (starch) synthase
Glycogen Synthase
Phosphorylation
protein phosphorylation
phosphorylation
protein kinases
Protein Kinases
Proteins
phosphoproteins
Phosphoproteins
phosphotransferases (kinases)
phosphates
Phosphotransferases
Phosphates
enzymes
Enzymes
proteins

Keywords

  • Glycogen metabolism
  • Isozyme
  • Mutagenesis
  • Phosphoprotein
  • Phosphorylation site
  • Protein kinase
  • Synthetic peptides

ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Cell Biology

Cite this

Control of glycogen synthase by hierarchal protein phosphorylation. / Roach, Peter.

In: FASEB Journal, Vol. 4, No. 12, 1990, p. 2961-2968.

Research output: Contribution to journalArticle

@article{0e47fb1199494f97bce871077a5a4b91,
title = "Control of glycogen synthase by hierarchal protein phosphorylation",
abstract = "Protein phosphorylation is one of the most common mechanisms for controlling protein function. We now know that most phosphoproteins contain multiple phosphorylation sites and that these sites are often located in clusters. From the study of the enzyme glycogen synthase, one mechanism for the formation of phosphorylation clusters has been discovered that involves the concerted action of two or more protein kinases. One protein kinase, the primary kinase, introduces a phosphate group that is a requirement for the action of another, secondary, protein kinase. Thus the multiple phosphorylation occurs in a hierarchal fashion. This mechanism, which is critical for the phosphorylation of glycogen synthase, is likely to be a much more widespread phenome non.",
keywords = "Glycogen metabolism, Isozyme, Mutagenesis, Phosphoprotein, Phosphorylation site, Protein kinase, Synthetic peptides",
author = "Peter Roach",
year = "1990",
language = "English",
volume = "4",
pages = "2961--2968",
journal = "FASEB Journal",
issn = "0892-6638",
publisher = "FASEB",
number = "12",

}

TY - JOUR

T1 - Control of glycogen synthase by hierarchal protein phosphorylation

AU - Roach, Peter

PY - 1990

Y1 - 1990

N2 - Protein phosphorylation is one of the most common mechanisms for controlling protein function. We now know that most phosphoproteins contain multiple phosphorylation sites and that these sites are often located in clusters. From the study of the enzyme glycogen synthase, one mechanism for the formation of phosphorylation clusters has been discovered that involves the concerted action of two or more protein kinases. One protein kinase, the primary kinase, introduces a phosphate group that is a requirement for the action of another, secondary, protein kinase. Thus the multiple phosphorylation occurs in a hierarchal fashion. This mechanism, which is critical for the phosphorylation of glycogen synthase, is likely to be a much more widespread phenome non.

AB - Protein phosphorylation is one of the most common mechanisms for controlling protein function. We now know that most phosphoproteins contain multiple phosphorylation sites and that these sites are often located in clusters. From the study of the enzyme glycogen synthase, one mechanism for the formation of phosphorylation clusters has been discovered that involves the concerted action of two or more protein kinases. One protein kinase, the primary kinase, introduces a phosphate group that is a requirement for the action of another, secondary, protein kinase. Thus the multiple phosphorylation occurs in a hierarchal fashion. This mechanism, which is critical for the phosphorylation of glycogen synthase, is likely to be a much more widespread phenome non.

KW - Glycogen metabolism

KW - Isozyme

KW - Mutagenesis

KW - Phosphoprotein

KW - Phosphorylation site

KW - Protein kinase

KW - Synthetic peptides

UR - http://www.scopus.com/inward/record.url?scp=0025202408&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025202408&partnerID=8YFLogxK

M3 - Article

C2 - 2168324

AN - SCOPUS:0025202408

VL - 4

SP - 2961

EP - 2968

JO - FASEB Journal

JF - FASEB Journal

SN - 0892-6638

IS - 12

ER -