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  EphrinB phosphorylation and reverse signaling: regulation by Src kinases and PTP-BL phosphatase

Palmer, A., Zimmer, M., Erdmann, K. S., Eulenburg, V., Porthin, A., Heumann, R., et al. (2002). EphrinB phosphorylation and reverse signaling: regulation by Src kinases and PTP-BL phosphatase. Molecular Cell, 9(4), 725-737.

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 Creators:
Palmer, A.*1, Author              
Zimmer, M.*2, Author              
Erdmann, K. S.3, Author
Eulenburg, V.3, Author
Porthin, A.2, Author              
Heumann, R.3, Author
Deutsch, U.3, Author
Klein, R.2, Author              
*equal contribution3, Author
Affiliations:
1Research Group: Signal Transduction / Acker-Palmer, MPI of Neurobiology, Max Planck Society, ou_1113563              
2Department: Molecular Neurobiology / Klein, MPI of Neurobiology, Max Planck Society, ou_1113546              
3Ruhr Univ Bochum, D-44780 Bochum, Germany; European Mol Biol Lab, D-69117 Heidelberg, Germany; Max Planck Inst Physiol & Clin Res, WG Kerckhoff Inst, D-61231 Bad Nauheim, Germany; Max Planck Inst Vasc Biol, D-48149 Munster, Germany, ou_persistent22              

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 Abstract: Ephrins are cell surface-associated ligands for Eph receptors and are important regulators of morphogenic processes such as axon guidance and angiogenesis. Transmembrane ephrinB ligands act as "receptor-like" signaling molecules, in part mediated by tyrosine phosphorylation and by engagement with PDZ domain proteins. However, the underlying cell biology and signaling mechanisms are poorly understood. Here we show that Src family kinases (SFKs) are positive regulators of ephrinB phosphorylation and phosphotyrosine-mediated reverse signaling. EphB receptor engagement of ephrinB causes rapid recruitment of SFKs to ephrinB expression domains and transient SFK activation. With delayed kinetics, ephrinB ligands recruit the cytoplasmic PDZ domain containing protein tyrosine phosphatase PTP-BL and are dephosphorylated. Our data suggest the presence of a switch mechanism that allows a shift from phosphotyrosine/SFK-dependent signaling to PDZ-dependent signaling.

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Language(s): eng - English
 Dates: 2002-04
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 15207
ISI: 000175244400007
 Degree: -

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Title: Molecular Cell
  Alternative Title : Mol. Cell
Source Genre: Journal
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Pages: - Volume / Issue: 9 (4) Sequence Number: - Start / End Page: 725 - 737 Identifier: ISSN: 1097-2765