Standard Article

Biological Regulation by Protein Phosphorylation

Proteins, Peptides and Amino Acids

  1. Clay W. Scott1,
  2. Ratan V. Bhat2,
  3. Gaochao Tian1

Published Online: 15 SEP 2006

DOI: 10.1002/3527600906.mcb.200300111

Reviews in Cell Biology and Molecular Medicine

Reviews in Cell Biology and Molecular Medicine

How to Cite

Scott, C. W., Bhat, R. V. and Tian, G. 2006. Biological Regulation by Protein Phosphorylation. Reviews in Cell Biology and Molecular Medicine. .

Author Information

  1. 1

    AstraZeneca Pharmaceuticals LP, Lead Discovery Department, Wilmington, DE, USA

  2. 2

    AstraZeneca R&D Södertälje, Department of Bioscience, Huddinge, Sweden

Publication History

  1. Published Online: 15 SEP 2006

Abstract

The biological activity of many proteins is modulated by the phosphorylation of specific sites within the protein. Protein kinases catalyze the transfer of a phosphate group to the protein, while protein phosphatases remove the phosphate group. This reversible modification is utilized by the cell to dynamically regulate proteins that are involved in almost all cellular functions. Protein phosphorylation plays a particularly prominent role in the transduction of extracellular signals. A hormone, neurotransmitter, or growth factor binds to its cell surface receptor and may directly or indirectly activate a protein kinase (or phosphatase) inside the cell, which leads to changes in the phosphorylation states of key regulatory proteins. This cascade of events ultimately results in a functional or phenotypic cellular response (e.g. contraction, release of neurotransmitter, changes in metabolism, or altered gene expression).

Keywords:

  • Protein Kinase;
  • Phosphoprotein Phosphatase;
  • Second Messenger