Multi-ligand interactions with receptor-like protein tyrosine phosphatase beta: implications for intercellular signaling.
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.
Peles
E
E
Dept of Molecular Cell Biology, Weizmann Institute of Science, Rehovot, Israel. peles@wiccmail.weizmann.ac.il
Schlessinger
J
J
Grumet
M
M
D000818:Animals; D002450:Cell Communication; D005109:Extracellular Matrix / Q000378:metabolism; D006801:Humans; D008024:Ligands; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000378:metabolism*; D009420:Nervous System / Q000166:cytology / Q000378:metabolism; D019006:Neural Cell Adhesion Molecules / Q000378:metabolism; D017027:Protein Tyrosine Phosphatases / Q000737:chemistry / Q000378:metabolism*; D054633:Receptor-Like Protein Tyrosine Phosphatases, Class 5; D015398:Signal Transduction
D008024:Ligands; D009419:Nerve Tissue Proteins; D019006:Neural Cell Adhesion Molecules; C516895:PTPRZ1 protein, human; D017027:Protein Tyrosine Phosphatases; D054633:Receptor-Like Protein Tyrosine Phosphatases, Class 5