Protein Regulation in Signal Transduction

Cold Spring Harb Perspect Biol. 2016 Jun 1;8(6):a005918. doi: 10.1101/cshperspect.a005918.

Abstract

SUMMARYCells must respond to a diverse, complex, and ever-changing mix of signals, using a fairly limited set of parts. Changes in protein level, protein localization, protein activity, and protein-protein interactions are critical aspects of signal transduction, allowing cells to respond highly specifically to a nearly limitless set of cues and also to vary the sensitivity, duration, and dynamics of the response. Signal-dependent changes in levels of gene expression and protein synthesis play an important role in regulation of protein levels, whereas posttranslational modifications of proteins regulate their degradation, localization, and functional interactions. Protein ubiquitylation, for example, can direct proteins to the proteasome for degradation or provide a signal that regulates their interactions and/or location within the cell. Similarly, protein phosphorylation by specific kinases is a key mechanism for augmenting protein activity and relaying signals to other proteins that possess domains that recognize the phosphorylated residues.

Publication types

  • Review

MeSH terms

  • Allosteric Site
  • Amino Acid Motifs
  • Animals
  • Cell Membrane / metabolism
  • GTP Phosphohydrolases / metabolism
  • Gene Expression Regulation
  • Humans
  • Lipids / chemistry
  • Models, Theoretical
  • Phosphorylation*
  • Proteasome Endopeptidase Complex / metabolism
  • Protein Binding*
  • Protein Domains
  • Protein Interaction Mapping
  • Protein Processing, Post-Translational*
  • Signal Transduction / physiology*
  • Transcription Factors / metabolism
  • Ubiquitination

Substances

  • Lipids
  • Transcription Factors
  • Proteasome Endopeptidase Complex
  • GTP Phosphohydrolases