IL-4 signaling is regulated through the recruitment of phosphatases, kinases, and SOCS proteins to the receptor complex

Cold Spring Harb Symp Quant Biol. 1999:64:405-16. doi: 10.1101/sqb.1999.64.405.
No abstract available

Publication types

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

MeSH terms

  • Animals
  • Carrier Proteins / metabolism
  • Humans
  • Insulin Receptor Substrate Proteins
  • Interleukin-4 / metabolism*
  • Intracellular Signaling Peptides and Proteins*
  • Macromolecular Substances
  • Models, Biological
  • Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases
  • Phosphoproteins / metabolism
  • Phosphoric Monoester Hydrolases / metabolism
  • Phosphotransferases / metabolism
  • Protein Serine-Threonine Kinases
  • Proto-Oncogene Proteins / metabolism
  • Proto-Oncogene Proteins c-pim-1
  • Receptors, Interleukin-4 / chemistry
  • Receptors, Interleukin-4 / metabolism*
  • Repressor Proteins*
  • STAT6 Transcription Factor
  • Signal Transduction / physiology*
  • Suppressor of Cytokine Signaling 1 Protein
  • Suppressor of Cytokine Signaling Proteins
  • Trans-Activators / metabolism

Substances

  • Carrier Proteins
  • IRS2 protein, human
  • Insulin Receptor Substrate Proteins
  • Intracellular Signaling Peptides and Proteins
  • Macromolecular Substances
  • Phosphoproteins
  • Proto-Oncogene Proteins
  • Receptors, Interleukin-4
  • Repressor Proteins
  • SOCS1 protein, human
  • STAT6 Transcription Factor
  • STAT6 protein, human
  • Suppressor of Cytokine Signaling 1 Protein
  • Suppressor of Cytokine Signaling Proteins
  • Trans-Activators
  • Interleukin-4
  • Phosphotransferases
  • Protein Serine-Threonine Kinases
  • Proto-Oncogene Proteins c-pim-1
  • proto-oncogene proteins pim
  • Phosphoric Monoester Hydrolases
  • INPPL1 protein, human
  • Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases