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Characterizing ErbB-2-Mediated Tyrosine Phosphorylation and Activation of Plexins
Thomas Worzfeld1,2, Jakub M Swiercz3
1Institute of Pharmacology, University of Marburg, Karl-von-Frisch-Str. 1, 35043, Marburg, Germany. thomas.worzfeld@staff.uni-marburg.de.
Abstract:
Plexins comprise a family of transmembrane receptors for semaphorins. Plexins of the B- and D-subfamily interact with the receptor tyrosine kinase ErbB-2, and this interaction has been shown to be functionally relevant for various biological processes including tumor metastasis and bone formation. Binding of semaphorins to B- and D-subfamily plexins results in the activation of ErbB-2, which in turn phosphorylates these plexins. This phosphorylation triggers the activation of the small GTPases RhoA and RhoC downstream of B-subfamily plexins. Here we describe a methodology that allows the analysis of ErbB-2-mediated plexin phosphorylation and signaling.
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