Mol. Cells 2013; 35(5): 450-455
Published online May 3, 2013
https://doi.org/10.1007/s10059-013-0072-3
© The Korean Society for Molecular and Cellular Biology
A previous study showed that the EphA7 receptor regu-lates apoptotic cell death during early brain development. In this study, we provide evidence that the EphA7 receptor interacts with death receptors such as tumor necrosis factor receptor 1 (TNFR1) to decrease cell viability. We showed that ephrinA5 stimulates EphA7 to activate the TNFR1-mediated apoptotic signaling pathway. In addition, a pull-down assay using biotinylated ephrinA5-Fc revealed that ephrinA5-EphA7 complexes recruit TNFR1 to form a multi-protein complex. Immunocytochemical staining ana-lysis showed that EphA7 was co-localized with TNFR1 on the cell surface when cells were incubated with ephrinA5 at low temperatures. Finally, both the internalization motif and death domain of TNFR1 was important for inter-acting with an intracytoplasmic region of EphA7; this interaction was essential for inducing the apoptotic signaling cascade. This result suggests that a distinct multi-protein complex comprising ephrinA5, EphA7, and TNFR1 may constitute a platform for inducing caspase-dependent apoptotic cell death.
Keywords apoptosis, ephrinA5, EphA7, TNFR1
Mol. Cells 2013; 35(5): 450-455
Published online May 31, 2013 https://doi.org/10.1007/s10059-013-0072-3
Copyright © The Korean Society for Molecular and Cellular Biology.
Haeryung Lee, Eunjeong Park, Yujin Kim, and Soochul Park
Department of Biological Science, Sookmyung Women's University, Seoul 140-742, Korea
A previous study showed that the EphA7 receptor regu-lates apoptotic cell death during early brain development. In this study, we provide evidence that the EphA7 receptor interacts with death receptors such as tumor necrosis factor receptor 1 (TNFR1) to decrease cell viability. We showed that ephrinA5 stimulates EphA7 to activate the TNFR1-mediated apoptotic signaling pathway. In addition, a pull-down assay using biotinylated ephrinA5-Fc revealed that ephrinA5-EphA7 complexes recruit TNFR1 to form a multi-protein complex. Immunocytochemical staining ana-lysis showed that EphA7 was co-localized with TNFR1 on the cell surface when cells were incubated with ephrinA5 at low temperatures. Finally, both the internalization motif and death domain of TNFR1 was important for inter-acting with an intracytoplasmic region of EphA7; this interaction was essential for inducing the apoptotic signaling cascade. This result suggests that a distinct multi-protein complex comprising ephrinA5, EphA7, and TNFR1 may constitute a platform for inducing caspase-dependent apoptotic cell death.
Keywords: apoptosis, ephrinA5, EphA7, TNFR1
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