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Heterogeneous nuclear ribonucleoprotein K inhibits heat shock-induced transcriptional activity of heat shock factor 1.
Kim, Hee-Jung; Lee, Jae-Jin; Cho, Jin-Hwan; Jeong, Jaeho; Park, A Young; Kang, Wonmo; Lee, Kong-Joo.
Affiliation
  • Kim HJ; Graduate School of Pharmaceutical Sciences, College of Pharmacy, Ewha Womans University, Seoul 120-750, Korea.
  • Lee JJ; Graduate School of Pharmaceutical Sciences, College of Pharmacy, Ewha Womans University, Seoul 120-750, Korea.
  • Cho JH; Graduate School of Pharmaceutical Sciences, College of Pharmacy, Ewha Womans University, Seoul 120-750, Korea.
  • Jeong J; Graduate School of Pharmaceutical Sciences, College of Pharmacy, Ewha Womans University, Seoul 120-750, Korea.
  • Park AY; Graduate School of Pharmaceutical Sciences, College of Pharmacy, Ewha Womans University, Seoul 120-750, Korea.
  • Kang W; Graduate School of Pharmaceutical Sciences, College of Pharmacy, Ewha Womans University, Seoul 120-750, Korea.
  • Lee KJ; Graduate School of Pharmaceutical Sciences, College of Pharmacy, Ewha Womans University, Seoul 120-750, Korea. Electronic address: kjl@ewha.ac.kr.
J Biol Chem ; 292(31): 12801-12812, 2017 08 04.
Article in En | MEDLINE | ID: mdl-28592492
When cells are exposed to heat shock and various other stresses, heat shock factor 1 (HSF1) is activated, and the heat shock response (HSR) is elicited. To better understand the molecular regulation of the HSR, we used 2D-PAGE-based proteome analysis to screen for heat shock-induced post-translationally modified cellular proteins. Our analysis revealed that two protein spots typically present on 2D-PAGE gels and containing heterogeneous nuclear ribonucleoprotein K (hnRNP K) with trioxidized Cys132 disappeared after the heat shock treatment and reappeared during recovery, but the total amount of hnRNP K protein remained unchanged. We next tested whether hnRNP K plays a role in HSR by regulating HSF1 and found that hnRNP K inhibits HSF1 activity, resulting in reduced expression of hsp70 and hsp27 mRNAs. hnRNP K also reduced binding affinity of HSF1 to the heat shock element by directly interacting with HSF1 but did not affect HSF1 phosphorylation-dependent activation or nuclear localization. hnRNP K lost its ability to induce these effects when its Cys132 was substituted with Ser, Asp, or Glu. These findings suggest that hnRNP K inhibits transcriptional activity of HSF1 by inhibiting its binding to heat shock element and that the oxidation status of Cys132 in hnRNP K is critical for this inhibition.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Transcription Factors / Protein Processing, Post-Translational / Gene Expression Regulation / HSP70 Heat-Shock Proteins / Response Elements / Heterogeneous-Nuclear Ribonucleoprotein K / DNA-Binding Proteins / HSP27 Heat-Shock Proteins Language: En Journal: J Biol Chem Year: 2017 Type: Article

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Transcription Factors / Protein Processing, Post-Translational / Gene Expression Regulation / HSP70 Heat-Shock Proteins / Response Elements / Heterogeneous-Nuclear Ribonucleoprotein K / DNA-Binding Proteins / HSP27 Heat-Shock Proteins Language: En Journal: J Biol Chem Year: 2017 Type: Article