Multi-ligand interactions with receptor-like protein tyrosine phosphatase β: implications for intercellular signaling
E Peles, J Schlessinger, M Grumet - Trends in biochemical sciences, 1998 - cell.com
E Peles, J Schlessinger, M Grumet
Trends in biochemical sciences, 1998•cell.comReceptor-like protein tyrosine phosphatase β (RPTPβ) 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.
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.
Abstract
Receptor-like protein tyrosine phosphatase β (RPTPβ) 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.
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