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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

EphrinA5-EphA7 Complex Induces Apoptotic Cell Death Via TNFR1

Haeryung Lee, Eunjeong Park, Yujin Kim, and Soochul Park

Department of Biological Science, Sookmyung Women's University, Seoul 140-742, Korea

Received: February 27, 2013; Revised: March 14, 2013; Accepted: March 14, 2013

Abstract

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

Article

Research Article

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.

EphrinA5-EphA7 Complex Induces Apoptotic Cell Death Via TNFR1

Haeryung Lee, Eunjeong Park, Yujin Kim, and Soochul Park

Department of Biological Science, Sookmyung Women's University, Seoul 140-742, Korea

Received: February 27, 2013; Revised: March 14, 2013; Accepted: March 14, 2013

Abstract

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
Mar 31, 2023 Vol.46 No.3, pp. 131~189
COVER PICTURE
The physiologically important cytoprotective signaling in normal cells (background area in turquoise) mediated by NRF2 (blue chain) is often hijacked by cancer cells (red ball) in the tumor microenvironment (yellow area). However, the differential roles of NRF2 throughout the multistage carcinogenesis remains largely unresolved (white-colored overlapping misty areas).

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