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EphA Receptors Form a Complex with Caspase-8 to Induce Apoptotic Cell Death

Authors
Lee, HaeryungPark, SunjungKang, Young-SookPark, Soochul
Issue Date
Apr-2015
Publisher
KOREAN SOC MOLECULAR & CELLULAR BIOLOGY
Keywords
apoptosis; caspase-8; EphA
Citation
MOLECULES AND CELLS, v.38, no.4, pp 349 - 355
Pages
7
Journal Title
MOLECULES AND CELLS
Volume
38
Number
4
Start Page
349
End Page
355
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/10597
DOI
10.14348/molcells.2015.2279
ISSN
1016-8478
0219-1032
Abstract
EphA7 has been implicated in the regulation of apoptotic cell death in neural epithelial cells. In this report, we provide evidence that EphA7 interacts with caspase-8 to induce apoptotic cell signaling. First, a pull-down assay using biotinylated ephrinA5-Fc showed that EphA7 coprecipitated with wild type caspase-8 or catalytically inactive caspase-8 mutant. Second, co-transfection of EphA7 with caspase-8 significantly increased the number of cleaved caspase-3 positive apoptotic cells under an experimental condition where transfection of EphA7 or caspase-8 alone did not affect cell viability or apoptosis. EphA4 also had a causative role in inducing apoptotic cell death with caspase-8, whereas EphA8 did not. Third, caspase-8 catalytic activity was essential for the apoptotic signaling cascade, whereas tyrosine kinase activity of the EphA4 receptor was not. Interestingly, we found that kinase-inactive EphA4 was well co-localized at the plasma membrane with catalytically inactive caspase-8, suggesting that an interaction between these mutant proteins was more stable. Finally, we observed that the extracellular region of the EphA7 receptor was critical for interacting with caspase-8, whereas the cytoplasmic region of EphA7 was not. Therefore, we propose that Eph receptors physically associate with a transmembrane protein to form an apoptotic signaling complex and that this unidentified receptor-like protein acts as a biochemical linker between the Eph receptor and caspase-8.
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이과대학 (생명시스템학부)
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