Protein aspartate phosphatases control the output of two-component signal transduction systems

Trends Genet. 1996 Mar;12(3):97-101. doi: 10.1016/0168-9525(96)81420-x.


Phosphorylation or dephosphorylation of an aspartate regulates the output activity of the response regulator of two-component signaling systems. Signal input in these systems is dependent on signal-transducing kinases, which can respond to a variety of signal ligands and, in some cases, to small phosphorylated metabolic intermediates. The kinase component of many two-component signaling systems also displays a response regulator-phosphate phosphatase activity that inactivates the response regulator in response to signals. Newly discovered kinase-independent phosphatases allow additional signals to influence the extent of response-regulator phosphorylation. Such phosphatases are prevalent in signal transduction systems controlling complex processes, such as the initiation of development in microorganisms.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • ATP-Binding Cassette Transporters*
  • Amino Acid Sequence
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Escherichia coli Proteins*
  • Histidine Kinase
  • Models, Biological
  • Models, Molecular
  • Molecular Sequence Data
  • Phosphoprotein Phosphatases / chemistry
  • Phosphoprotein Phosphatases / genetics
  • Phosphoprotein Phosphatases / metabolism*
  • Protein Kinases / genetics
  • Protein Kinases / metabolism
  • Signal Transduction / genetics
  • Signal Transduction / physiology*


  • ATP-Binding Cassette Transporters
  • Bacterial Proteins
  • Escherichia coli Proteins
  • modF protein, E coli
  • rapA protein, Bacillus subtilis
  • Protein Kinases
  • Histidine Kinase
  • rapB protein, Bacillus subtilis
  • Phosphoprotein Phosphatases