Beta2-chimaerin binds to EphA receptors and regulates cell migration.
Ephrins and Eph receptors have key roles in regulation of cell migration during development. We found that the RacGAP beta2-chimaerin (chimerin) bound to EphA2 and EphA4 and inactivated Rac1 in response to ephrinA1 stimulation. EphA4 bound to beta2-chimaerin through its kinase domain and promoted binding of Rac1 to beta2-chimaerin. In addition, knockdown of endogenous beta2-chimaerin blocked ephrinA1-induced suppression of cell migration. These results suggest that beta2-chimaerin is activated by EphA receptors and mediates the EphA receptor-dependent regulation of cell migration.
Takeuchi
Shingo
S
Laboratory of Molecular Neurobiology, Graduate School of Biostudies, Kyoto University, Yoshidakonoe-cho, Sakyo-ku, Kyoto 606-8501, Japan.
Yamaki
Nao
N
Iwasato
Takuji
T
Negishi
Manabu
M
Katoh
Hironori
H
D000818:Animals; D001483:Base Sequence; D002460:Cell Line; D002465:Cell Movement; D017931:DNA Primers; D006801:Humans; D009363:Neoplasm Proteins / Q000378:metabolism*; D011485:Protein Binding; D036081:Receptors, Eph Family / Q000378:metabolism*
D017931:DNA Primers; D009363:Neoplasm Proteins; C079844:beta-chimaerin; D036081:Receptors, Eph Family