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Molecular Chaperone Heat Shock Protein 90 Stabilizes Nucleolin to Maintain mRNA Level in Mitosis
Author(s) -
HUNG JanJong
Publication year - 2011
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.25.1_supplement.519.4
Heat shock protein 90(Hsp90) is important for the folding of numbers proteins. Our previous study reveals that Hsp90 can stabilize the Sp1 by modulating its phosphorylation during mitosis. Herein we use the proteomics to probe the Hsp90 interact proteins. Nucleolin is one of these proteins interacted with Sp1 during mitosis. To clarify the effect of Hsp90 in nucleolin in mitosis found that nucleolin level is inhibited after geldanamycin, inhibitor of Hsp90, treatment through the inhibition of the nucleolin phosphorylation by CDK1. Due to nucleolin with the function in increasing RNA stability, we did the cDNA array with or without GA treatment during mitosis to screen the mRNA level affected by Hsp90. Data indicates that about 200 mRNAs are protected by Hsp90 in mitosis. After RNA immunoprecipitation assay reveals that 60 mRNAs of the 200 mRNAs could recruit nucleolin to the 3′UTR to increase the RNA stability. Taken together, Hsp90 as a chaperone is very important for the mitotic progression smoothly.