Interaction of Heat Shock Protein Cpn10 with the Cyclin E/Cdk2 Substrate Nuclear Protein Ataxia-Telangiectasia (NPAT) Is Involved in Regulating Histone Transcription*
| العنوان: | Interaction of Heat Shock Protein Cpn10 with the Cyclin E/Cdk2 Substrate Nuclear Protein Ataxia-Telangiectasia (NPAT) Is Involved in Regulating Histone Transcription* |
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| المؤلفون: | Xin Bao Wang, Xi Sheng Rao, Fei Ya Wang, Wei Fan, Yan Luo, Yi Ting Zhou, Peng Yi, Yue Shen, Dao Sheng Huang, Lei Zheng, Li Ling Zheng, Xiao Xia Cong |
| المصدر: | The Journal of Biological Chemistry |
| بيانات النشر: | American Society for Biochemistry and Molecular Biology, 2015. |
| سنة النشر: | 2015 |
| مصطلحات موضوعية: | Cyclin E, Transcription, Genetic, Amino Acid Motifs, NPAT, histone transcription, Cell Cycle Proteins, histone, Pregnancy Proteins, Biochemistry, Histones, cyclin, Two-Hybrid System Techniques, Transcriptional regulation, medicine, Chaperonin 10, Suppressor Factors, Immunologic, heat shock protein (HSP), Humans, Nuclear protein, Cell Cycle Protein, Molecular Biology, Cell Proliferation, Cell Nucleus, biology, Cpn10, Cyclin-dependent kinase 2, Cell Cycle, Cyclin-Dependent Kinase 2, Nuclear Proteins, Cell Biology, Cell cycle, Molecular biology, Cell biology, Cell nucleus, Histone, medicine.anatomical_structure, Microscopy, Fluorescence, biology.protein, Disease Progression, RNA Interference, Signal Transduction, HeLa Cells |
| الوصف: | Background: NPAT is critical for histone transcription and cell cycle progression. Results: A novel NPAT-interacting protein, Cpn10/HSPE, is critical for histone transcription and focus formation of NPAT. Conclusion: Heat shock protein Cpn10 is a novel regulator for histone transcription and cell proliferation. Significance: Our findings reveal a previously unappreciated role of heat shock protein in regulating histone transcription. Precise modulation of histone gene transcription is critical for cell cycle progression. As a direct substrate of Cyclin E/CDK2, nuclear protein ataxia-telangiectasia (NPAT) is a crucial factor in regulating histone transcription and cell cycle progression. Here we identified that Cpn10/HSPE, a 10-kDa heat shock protein, is a novel interacting partner of NPAT. A pool of Cpn10 is colocalized with NPAT foci during G1 and S phases in nuclei. Gain- and loss-of-function experiments unraveled an essential role of Cpn10 in histone transcription. A conserved DLFD motif within Cpn10 was critical for targeting NPAT and modulating histone transcription. More importantly, knockdown of Cpn10 disrupted the focus formation of both NPAT and FADD-like interleukin-1β-converting enzyme-associated huge protein without affecting Coilin-positive Cajal bodies. Finally, Cpn10 is important for S phase progression and cell proliferation. Taken together, our finding revealed a novel role of Cpn10 in the spatial regulation of NPAT signaling and disclosed a previously unappreciated link between the heat shock protein and histone transcription regulation. |
| اللغة: | English |
| تدمد: | 1083-351X 0021-9258 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::53bb1db994fc4d26947f2b7f2952a2c0Test http://europepmc.org/articles/PMC4705935Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....53bb1db994fc4d26947f2b7f2952a2c0 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 1083351X 00219258 |
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