Protein phosphorylation on tyrosine residues is an important cell signaling mechanism that is regulated by the antagonistic activities of the protein-tyrosine kinases (PTKs) and protein-tyrosine phosphatases (PTPs). We are interested in the function of PTPs in development and cell signaling. Using biochemical and cell biological approaches, we found that the proto-typical RPTPalpha is regulated by dimerization, oxidation and phosphorylation. The zebrafish is used to elucidate the role of PTPs and PTKs in early vertebrate development. Recently, we found that several PTKs and PTPs are essential for normal convergence and extension cell movements in gastrulation.
About the research
Jopling, C., van Geemen, D., den Hertog, J. (2007) Shp2 knock down and Noonan/LEOPARD mutant Shp2 induced gastrulation cell movement defects in zebrafish. PLoS Genet. 3: e225.
Jopling, C., den Hertog, J. (2005) Fyn/Yes and non-canonical Wnt signaling converge on RhoA in vertebrate gastrulation cell movements. EMBO Rep. 6: 426 – 431.
van der Wijk, T., Blanchetot, C., Overvoorde, J., den Hertog, J. (2003) Redox-regulated rotational coupling of receptor protein-tyrosine phosphatase alpha dimers. J. Biol. Chem. 278: 13968-13974.
Blanchetot, C., Tertoolen, L.G.J., den Hertog, J. (2002) Regulation of receptor protein tyrosine phosphatase alpha by oxidative stress. EMBO J. 21: 493-503.
den Hertog, J., Pals, C.E.G.M., Peppelenbosch, M.P., Tertoolen, L.G.J., de Laat, S.W., Kruijer, W. (1993) Receptor protein-tyrosine phosphatase alpha activates pp60c-src and is involved in neuronal differentiation. EMBO J. 12: 3789-3798.
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