title: Characterizing ErbB-2-Mediated Tyrosine Phosphorylation and Activation of Plexins.
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.
authors: Institute of Pharmacology, University of Marburg, Karl-von-Frisch-Str. 1, 35043, Marburg, Germany. thomas.worzfeld@staff.uni-marburg.de.|Department of Pharmacology, Max-Planck-Institute for Heart and Lung Research, Ludwigstr. 43, 61231, Bad Nauheim, Germany. thomas.worzfeld@staff.uni-marburg.de.
authors: Thomas
authors: T
authors: Worzfeld
authors: Department of Pharmacology, Max-Planck-Institute for Heart and Lung Research, Ludwigstr. 43, 61231, Bad Nauheim, Germany. jakub.swiercz@mpi-bn.mpg.de.
authors: Jakub M
authors: JM
authors: Swiercz
mesh_terms: D015153:Blotting, Western; D015815:Cell Adhesion Molecules / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D057809:HEK293 Cells; D006801:Humans; D061986:MCF-7 Cells; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D010766:Phosphorylation; D018719:Erb-b2 Receptor Tyrosine Kinases / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D014443:Tyrosine / Q000378:metabolism*; D020742:rhoA GTP-Binding Protein / Q000378:metabolism
chemical_list: D015815:Cell Adhesion Molecules; D009419:Nerve Tissue Proteins; D018719:Erb-b2 Receptor Tyrosine Kinases; D011993:Recombinant Fusion Proteins; D014443:Tyrosine; D020742:rhoA GTP-Binding Protein; C091529:plexin
keywords: ErbB-2; Immunoblot; Immunoprecipitation; Phosphorylation; Plexin; Pulldown; RhoA; RhoC; Semaphorin; Signaling