Heat Shock Protein 90 Stabilizes Nucleolin to Increase mRNA Stability in Mitosis *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 286, Issue: 51, Page: 43816-43829
2011
- 32Citations
- 25Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations32
- Citation Indexes32
- 32
- CrossRef29
- Captures25
- Readers25
- 25
Article Description
Most studies on heat shock protein 90 (Hsp90) have focused on the involvement of Hsp90 in the interphase, whereas the role of this protein in the nucleus during mitosis remains largely unclear. In this study, we found that the level of the acetylated form of Hsp90 decreased dramatically during mitosis, which indicates more chaperone activity during mitosis. We thus probed proteins that interacted with Hsp90 by liquid chromatography/mass spectrometry (LC/MS) and found that nucleolin was one of those interacting proteins during mitosis. The nucleolin level decreased upon geldanamycin treatment, and Hsp90 maintained the cyclin-dependent kinase 1 (CDK1) activity to phosphorylate nucleolin at Thr-641/707. Mutation of Thr-641/707 resulted in the destabilization of nucleolin in mitosis. We globally screened the level of mitotic mRNAs and found that 229 mRNAs decreased during mitosis in the presence of geldanamycin. Furthermore, a bioinformatics tool and an RNA immunoprecipitation assay found that 16 mRNAs, including cadherin and Bcl-xl, were stabilized through the recruitment of nucleolin to the 3′-untranslated regions (3′-UTRs) of those genes. Overall, strong correlations exist between the up-regulation of Hsp90, nucleolin, and the mRNAs related to tumorigenesis of the lung. Our findings thus indicate that nucleolin stabilized by Hsp90 contributes to the lung tumorigenesis by increasing the level of many tumor-related mRNAs during mitosis.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925820684769; http://dx.doi.org/10.1074/jbc.m111.310979; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=83755168831&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/21998300; https://linkinghub.elsevier.com/retrieve/pii/S0021925820684769; http://www.jbc.org/lookup/doi/10.1074/jbc.M111.310979; https://syndication.highwire.org/content/doi/10.1074/jbc.M111.310979; https://dx.doi.org/10.1074/jbc.m111.310979; http://www.jbc.org/article/S0021925820684769/abstract; http://www.jbc.org/article/S0021925820684769/fulltext; http://www.jbc.org/article/S0021925820684769/pdf; https://www.jbc.org/article/S0021-9258(20)68476-9/abstract; http://www.jbc.org/cgi/doi/10.1074/jbc.M111.310979; http://www.jbc.org/content/286/51/43816.abstract; http://www.jbc.org/content/286/51/43816.full; http://www.jbc.org/content/286/51/43816.full.pdf; http://www.jbc.org/content/286/51/43816; https://www.jbc.org/content/286/51/43816
Elsevier BV
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