Identification of FAM96B as a novel prelamin A binding partner.

Identification of FAM96B as a novel prelamin A binding partner.
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鉴定 FAM96B 作为新型前核纤层蛋白 A 结合伴侣。

DOI:
10.1016/j.bbrc.2013.08.099
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发表时间:
2013-10
期刊:
Biochem Biophys Res Commun
影响因子:
--
通讯作者:
Liu, Xinguang
Liu, Xinguang
中科院分区:
其他
文献类型:
--
作者:
Xiong, Xing-Dong;Wang, Junwen;Zheng, Huiling;Jing, Xia;Liu, Zhenjie;Zhou, Zhongjun;Liu, Xinguang

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前体蛋白A积累导致核异常,损害核功能,并最终促进细胞衰老。然而,前层蛋白A如何促进细胞衰老的潜在机制仍然知之甚少。在这里,我们进行了酵母双杂交筛选使用人骨骼肌cDNA文库,以寻找prelamin A的结合伴侣,并确定FAM 96 B作为prelamin A的结合伴侣。通过GST下拉和免疫共沉淀实验证实了FAM 96 B与前层蛋白A的相互作用。此外,通过荧光共聚焦显微镜进行的共定位实验显示,FAM 96 B与前层蛋白A在HEK-293细胞中共定位。综上所述,我们的数据表明FAM 96 B和prelamin A之间的物理相互作用,这可能为prelamin A在早衰中的机制提供一些线索。
Prelamin A accumulation causes nuclear abnormalities, impairs nuclear functions, and eventually promotes cellular senescence. However, the underlying mechanism of how prelamin A promotes cellular senescence is still poorly understood. Here we carried out a yeast two-hybrid screen using a human skeletal muscle cDNA library to search for prelamin A binding partners, and identified FAM96B as a prelamin A binding partner. The interaction of FAM96B with prelamin A was confirmed by GST pull-down and co-immunoprecipitation experiments. Furthermore, co-localization experiments by fluorescent confocal microscopy revealed that FAM96B colocalized with prelamin A in HEK-293 cells. Taken together, our data demonstrated the physical interaction between FAM96B and prelamin A, which may provide some clues to the mechanisms of prelamin A in premature aging.
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