β2‐Chimaerin binds to EphA receptors and regulates cell migration
- 21 March 2009
- journal article
- Published by Wiley in FEBS Letters
- Vol. 583 (8), 1237-1242
- https://doi.org/10.1016/j.febslet.2009.03.032
Abstract
Ephrins and Eph receptors have key roles in regulation of cell migration during development. We found that the RacGAP β2-chimaerin (chimerin) bound to EphA2 and EphA4 and inactivated Rac1 in response to ephrinA1 stimulation. EphA4 bound to β2-chimaerin through its kinase domain and promoted binding of Rac1 to β2-chimaerin. In addition, knockdown of endogenous β2-chimaerin blocked ephrinA1-induced suppression of cell migration. These results suggest that β2-chimaerin is activated by EphA receptors and mediates the EphA receptor-dependent regulation of cell migration.Structured summaryMINT-7013428: EphA1 (uniprotkb:Q60750) physically interacts (MI:0218) with Chimaerin beta 2 (uniprotkb:Q80XD1-2) and EphA4 (uniprotkb:O08542) by anti tag coimmunoprecipitation (MI:0007)MINT-7013515: Chimaerin beta 2 (uniprotkb:Q80XD1-2) physically interacts (MI:0218) with Rac1 (uniprotkb:P63001) by anti tag coimmunoprecipitation (MI:0007)MINT-7013410: EphA1 (uniprotkb:Q60750) physically interacts (MI:0218) with Chimaerin beta 1 (uniprotkb:Q80XD1-1) and EphA4 (uniprotkb:O08542) by anti tag coimmunoprecipitation (MI:0007)MINT-7013503: Chimaerin beta 1 (uniprotkb:Q80XD1-1) physically interacts (MI:0218) with EphA4 (uniprotkb:O08542) by anti tag coimmunoprecipitation (MI:0007)MINT-7013472: Chimaerin beta 2 (uniprotkb:Q80XD1-2) physically interacts (MI:0218) with EphA2 (uniprotkb:O43921) by anti tag coimmunoprecipitation (MI:0007)MINT-7013450: EphA1 (uniprotkb:Q60750) physically interacts (MI:0218) with EphA2 (uniprotkb:O43921) and Chimaerin beta 2 (uniprotkb:P52757-1) by anti tag coimmunoprecipitation (MI:0007)MINT-7013491: Chimaerin beta 2 (uniprotkb:Q80XD1-2) physically interacts (MI:0218) with EphA4 (uniprotkb:O08542) by anti tag coimmunoprecipitation (MI:0007Keywords
This publication has 18 references indexed in Scilit:
- Identification of an Autoinhibitory Mechanism That Restricts C1 Domain-mediated Activation of the Rac-GAP α2-ChimaerinJournal of Biological Chemistry, 2008
- Role of chimaerins, a group of Rac-specific GTPase activating proteins, in T-cell receptor signalingCellular Signalling, 2008
- α2-Chimaerin interacts with EphA4 and regulates EphA4-dependent growth cone collapseProceedings of the National Academy of Sciences of the United States of America, 2007
- α2-Chimaerin Is an Essential EphA4 Effector in the Assembly of Neuronal Locomotor CircuitsNeuron, 2007
- Phospholipase Cγ/diacylglycerol-dependent activation of β2-chimaerin restricts EGF-induced Rac signalingThe EMBO Journal, 2006
- Role of the ephrin and Eph receptor tyrosine kinase families in angiogenesis and development of the cardiovascular systemThe Journal of Pathology, 2006
- Diverse Roles of Eph Receptors and Ephrins in the Regulation of Cell Migration and Tissue AssemblyDevelopmental Cell, 2004
- Structural Mechanism for Lipid Activation of the Rac-Specific GAP, β2-ChimaerinCell, 2004
- Phorbol Esters and Related Analogs Regulate the Subcellular Localization of β2-Chimaerin, a Non-protein Kinase C Phorbol Ester ReceptorPublished by Elsevier BV ,2001
- Kinase-Dependent and Kinase-Independent Functions of EphA4 Receptors in Major Axon Tract Formation In VivoNeuron, 2001