The carbonic anhydrase domain of receptor tyrosine phosphatase β is a functional ligand for the axonal cell recognition molecule contactin

• Published in: Cell 1995-07, Vol.82 (2), p.251-260
• Main Authors: Peles, Elior, Nativ, Moshe, Campbell, Phillip L, Sakurai, Takeshi, Martinez, Ricardo, Levt, Sima, Clary, Douglas O, Schilling, James, Barnea, Gilad, Plowman, Gregory D, Grumet, Martin, Schlessinger, Joseph
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Astrocytoma; Axons - physiology; Binding Sites; Carbonic Anhydrases - chemistry; Carbonic Anhydrases - metabolism; Cell Adhesion Molecules, Neuronal; Cell Line; Cercopithecus aethiops; Cloning, Molecular; Contactins; Humans; Ligands; Membrane Proteins - biosynthesis; Membrane Proteins - metabolism; Molecular Sequence Data; Nerve Tissue Proteins - analysis; Nerve Tissue Proteins - chemistry; Nerve Tissue Proteins - metabolism; Neurites - physiology; Neurons - metabolism; Protein Binding; Protein Tyrosine Phosphatases - analysis; Protein Tyrosine Phosphatases - chemistry; Protein Tyrosine Phosphatases - metabolism; Receptor-Like Protein Tyrosine Phosphatases, Class 5; Recombinant Fusion Proteins - chemistry; Recombinant Fusion Proteins - metabolism; Tumor Cells, Cultured
• ISSN: 0092-8674; 1097-4172
• DOI: 10.1016/0092-8674(95)90312-7

Receptor-type protein tyrosine phosphatase β (RPTPβ) is expressed in the developing nervous system and contains a carbonic anhydrase (CAH) domain as well as a fibronectin type III repeat in its extracellular domain. Fusion proteins containing these domains were used to search for ligands of RPTPβ. The CAH domain bound specifically to a 140 kDa protein expressed on the surface of neuronal cells. Expression cloning in COS7 cells revealed that this protein is contactin, a GPI membrane-anchored neuronal cell recognition molecule. The CAH domain of RPTPβ induced cell adhesion and neurite growth of primary tectal neurons, and differentiation of neuroblastoma cells. These responses were blocked by antibodies against contactin, demonstrating that contactin is a neuronal receptor for RPTPβ. These experiments show that an individual domain of RPTPβ acts as a functional ligand for the neuronal receptor contactin. The interaction between contactin and RPTPβ may generate unidirectional or bidirectional signals during neural development.