Multi-ligand interactions with receptor-like protein tyrosine phosphatase beta: implications for intercellular signaling

Trends Biochem Sci. 1998 Apr;23(4):121-4. doi: 10.1016/s0968-0004(98)01195-5.

Abstract

Receptor-like protein tyrosine phosphatase beta (RPTP beta) shows structural and functional similarity to cell adhesion molecules (CAMs). It binds to several neuronal CAMs and extracellular matrix (ECM) proteins that combine to form cell-recognition complexes. Here, the authors discuss the implications of such complexes for intercellular signaling, and the regulation of RPTP activity by cell-cell and cell-ECM contact.

Publication types

  • Review

MeSH terms

  • Animals
  • Cell Communication
  • Extracellular Matrix / metabolism
  • Humans
  • Ligands
  • Nerve Tissue Proteins / chemistry
  • Nerve Tissue Proteins / metabolism*
  • Nervous System / cytology
  • Nervous System / metabolism
  • Neural Cell Adhesion Molecules / metabolism
  • Protein Tyrosine Phosphatases / chemistry
  • Protein Tyrosine Phosphatases / metabolism*
  • Receptor-Like Protein Tyrosine Phosphatases, Class 5
  • Signal Transduction

Substances

  • Ligands
  • Nerve Tissue Proteins
  • Neural Cell Adhesion Molecules
  • PTPRZ1 protein, human
  • Protein Tyrosine Phosphatases
  • Receptor-Like Protein Tyrosine Phosphatases, Class 5