Regulatory functions of protein multisite phosphorylation

Thomas Soderling

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

In recent years it has become apparent that an increasing number of proteins can be phosphorylated at several different sites. In this article protein multisite phosphorylation is discussed with reference to the enzymes glycogen synthase, pyruvate dehydrogenase, and phosphorylase kinase. Each of these enzymes contains three or more different phosphorylation sites on one or more subunits. Activation and inactivation of the enzymes appear to correlate quite well with phosphorylation of a few key sites on the protein. The other phosphorylation sites may influence other kinetic properties of the enzymes or regulate the rates of dephosphorylation of the key sites by the appropriate phosphatase. Thus, multisite phosphorylation may represent an important mechanism for regulating several functions of complex proteins.

Original languageEnglish (US)
Pages (from-to)157-179
Number of pages23
JournalMolecular and Cellular Endocrinology
Volume16
Issue number3
DOIs
StatePublished - 1979
Externally publishedYes

Fingerprint

Phosphorylation
Enzymes
Proteins
Phosphorylase Kinase
Glycogen Synthase
Enzyme Activation
Phosphoric Monoester Hydrolases
Chemical activation
Kinetics

ASJC Scopus subject areas

  • Endocrinology
  • Endocrinology, Diabetes and Metabolism

Cite this

Regulatory functions of protein multisite phosphorylation. / Soderling, Thomas.

In: Molecular and Cellular Endocrinology, Vol. 16, No. 3, 1979, p. 157-179.

Research output: Contribution to journalArticle

Soderling, Thomas. / Regulatory functions of protein multisite phosphorylation. In: Molecular and Cellular Endocrinology. 1979 ; Vol. 16, No. 3. pp. 157-179.
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