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

Palmer, A; Zimmer, M; Erdmann, KS; Eulenburg, V; Porthin, A; Heumann, R; Deutsch, U; Klein, R (2002). EphrinB phosphorylation and reverse signaling: regulation by Src kinases and PTP-BL phosphatase. Molecular cell, 4(9), pp. 725-37. Cambridge, Mass.: Cell Press 10.1016/S1097-2765(02)00488-4

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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.

Item Type:	Journal Article (Original Article)
Division/Institute:	04 Faculty of Medicine > Pre-clinic Human Medicine > Theodor Kocher Institute
UniBE Contributor:	Deutsch, Urban
ISSN:	1097-2765
ISBN:	11983165
Publisher:	Cell Press
Language:	English
Submitter:	Factscience Import
Date Deposited:	04 Oct 2013 14:52
Last Modified:	05 Dec 2022 14:16
Publisher DOI:	10.1016/S1097-2765(02)00488-4
PubMed ID:	11983165
Web of Science ID:	000175244400007
URI:	https://boris.unibe.ch/id/eprint/22222 (FactScience: 32298)