2. Academic Validation
  3. Immediate-early response 5 (IER5) interacts with protein phosphatase 2A and regulates the phosphorylation of ribosomal protein S6 kinase and heat shock factor 1

Immediate-early response 5 (IER5) interacts with protein phosphatase 2A and regulates the phosphorylation of ribosomal protein S6 kinase and heat shock factor 1

  • FEBS Lett. 2015 Nov 30;589(23):3679-85. doi: 10.1016/j.febslet.2015.10.013.
Shotaro Kawabata 1,  Yuichiro Ishita 1,  Yukio Ishikawa 1,  Hiroshi Sakurai 2
Affiliations

Affiliations

  • 1 Division of Health Sciences, Kanazawa University Graduate School of Medical Science, 5-11-80 Kodatsuno, Kanazawa, Ishikawa 920-0942, Japan.
  • 2 Division of Health Sciences, Kanazawa University Graduate School of Medical Science, 5-11-80 Kodatsuno, Kanazawa, Ishikawa 920-0942, Japan. Electronic address: [email protected].
PMID: 26496226 DOI: 10.1016/j.febslet.2015.10.013
Abstract

Immediate-early response 5 (IER5) is a growth factor-inducible protein with homology to the N-terminus of IER2. Deletion analysis shows that a large region of IER5, including the N-terminal region, is involved in cell growth and stress resistance. The N-terminal region mediates IER5 oligomerization and binding to the B55 regulatory subunit of protein Phosphatase 2A (PP2A). IER5 physically interacts with the PP2A target proteins ribosomal protein S6 kinase (S6K) and heat shock factor 1 (HSF1), and the interactions are essential for the reduced phosphorylation of S6K and HSF1. Our data indicate that oligomeric IER5 regulates PP2A activity and cell growth.

Keywords

Heat shock factor 1; Immediate-early response 5; Phosphorylation; Protein phosphatase 2A; S6 kinase.

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