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RTN3 inducing apoptosis is modulated by an adhesion protein CRELD1

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Abstract

Reticulon3 (RTN3), as a member of the reticulon family, is generally regarded as a novel human apoptosis-inducing protein. But the extensional role of RTN3 remains virtually unknown. Herein, we showed that cysteine rich with EGF like domains 1(CRELD1), a cell adhesion molecule played a critical role in atrioventricular septal defects and it had mutual effect with RTN3 in vitro. Furthermore, we discovered that ectopic CRELD1 could interact with ectopic or endogenous RTN3. CRELD1 bound with RTN3 so as to increase the localization of RTN3 on the plasma membrane and decreased the apoptotic activity of RTN3 moderately. Moreover, the tunicamycin-inducing cell apoptosis was partly suppressed by this kind of interaction mentioned above. These results suggested that CRELD1 could partly change the localization of RTN3 from the endoplasmic reticulum to the plasma membrane and modulate the apoptotic activity of RTN3 through binding with it.

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Acknowledgments

We thank Professor Cheryl Maslen (Oregon Health &Science University) for her kind donation of the plasmid of CRELD1. This research was supported by National Nature Sciences foundation of China (30800476) and Doctoral Fund of Ministry of Education of China (200805331129).

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Correspondence to Shuiping Zhao.

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Xiang, R., Zhao, S. RTN3 inducing apoptosis is modulated by an adhesion protein CRELD1. Mol Cell Biochem 331, 225–230 (2009). https://doi.org/10.1007/s11010-009-0163-9

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