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a b s t r a c tEphrins and Eph receptors have key roles in regulation of cell migration during development. We found that the RacGAP b2-chimaerin (chimerin) bound to EphA2 and EphA4 and inactivated Rac1 in response to ephrinA1 stimulation. EphA4 bound to b2-chimaerin through its kinase domain and promoted binding of Rac1 to b2-chimaerin. In addition, knockdown of endogenous b2-chimaerin blocked ephrinA1-induced suppression of cell migration. These results suggest that b2-chimaerin is activated by EphA receptors and mediates the EphA receptor-dependent regulation of cell migration. Structured summary:MINT-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:0007)