Dimerization of Receptor Protein-Tyrosine Phosphatase alpha in living cells |
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| Authors: | Leon GJ Tertoolen Christophe Blanchetot Guoqiang Jiang John Overvoorde Theodorus WJ Gadella Jr Tony Hunter Jeroen den Hertog |
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| Affiliation: | (1) Hubrecht Laboratory, Netherlands Institute for Developmental Biology, Utrecht, The Netherlands;(2) Molecular Biology and Virology Laboratory, The Salk Institute for Biological Studies, La Jolla, USA;(3) Merck Research Laboratory, , Rahway, USA;(4) Laboratory for Molecular Biology, Wageningen University, Wageningen, The Netherlands |
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| Abstract: | Background Dimerization is an important regulatory mechanism of single membrane-spanning receptors. For instance, activation of receptor protein-tyrosine kinases (RPTKs) involves dimerization. Structural, functional and biochemical studies suggested that the enzymatic counterparts of RPTKs, the receptor protein-tyrosine phosphatases (RPTPs), are inhibited by dimerization, but whether RPTPs actually dimerize in living cells remained to be determined. |
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