Identification of FAM96B as a novel prelamin A binding partner |
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Authors: | Xing-Dong Xiong Junwen Wang Huiling Zheng Xia Jing Zhenjie Liu Zhongjun Zhou Xinguang Liu |
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Affiliation: | 1. Institute of Aging Research, Guangdong Medical College, Dongguan 523808, PR China;2. Institute of Biochemistry & Molecular Biology, Guangdong Medical College, Zhanjiang 524023, PR China;3. Guangdong Provincial Key Laboratory of Medical Molecular Diagnostics, Dongguan 523808, PR China;4. Department of Biochemistry, Li Ka Shing Faculty of Medicine, The University of Hong Kong, Hong Kong, PR China |
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Abstract: | 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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Keywords: | FAM96B, family with sequence similarity 96 member B HGPS, Hutchinson&ndash Gilford progeria syndrome CIA, the cytoplasmic Fe&ndash S assembly |
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