Receptor protein tyrosine phosphatase alpha activates pp60c-src and is involved in neuronal differentiation
den Hertog, J.; Pals, C.E.; Peppelenbosch, M.P.; Tertoolen, L.G.; de Laat, S.W.; Kruijer, W.
EMBO Journal 12(10): 3789-3798
1993
ISSN/ISBN: 0261-4189 PMID: 7691597 Document Number: 421890
Here we report that protein tyrosine phosphatases (PTPases), like their enzymatic counterpart the protein tyrosine kinases, can play an important role in cell differentiation. Expression of the transmembrane PTPase receptor protein tyrosine phosphatase alpha (RPTP-alpha) is transiently enhanced during neuronal differentiation of embryonal carcinoma (EC) and neuroblastoma cells. Retinoic acid induces wild type P19 cells to differentiate into endoderm- and mesoderm-like cells. By contrast, retinoic acid treatment leads to neuronal differentiation of P19 cells, ectopically expressing functional RPTP-alpha, as illustrated by their ability to generate action potentials. Endogenous pp60-c-src kinase activity is enhanced in the RPTP-alpha-transfected cells, which may be due to direct dephosphorylation of the regulatory Tyr residue at position 527 in pp60-c-src by RPTP-alpha. Our results demonstrate that RPTP-alpha is involved in neuronal differentiation and imply a role for pp60-c-src in the differentiation process.