Post-translational Regulation of FNIP1 Creates a Rheostat for the Molecular Chaperone Hsp90

Rebecca A. Sager, Mark R. Woodford, Sarah J. Backe, Alan M. Makedon, Alexander J. Baker-Williams, Bryanna T. DiGregorio, David R. Loiselle, Timothy A. Haystead, Natasha E. Zachara, Chrisostomos Prodromou, Dimitra Bourboulia, Laura S. Schmidt, W. Marston Linehan, Gennady Bratslavsky, Mehdi Mollapour

Research output: Contribution to journalArticlepeer-review

Abstract

Sager et al. show that casein-kinase-2-mediated sequential phosphorylation of the co-chaperone FNIP1 leads to incremental inhibition of Hsp90 ATPase activity and gradual activation of both kinase and non-kinase clients. O-GlcNAcylation antagonizes phosphorylation of FNIP1, preventing its interaction with Hsp90, and consequently promotes FNIP1 ubiquitination and proteasomal degradation.

Original languageEnglish (US)
Pages (from-to)1344-1356.e5
JournalCell Reports
Volume26
Issue number5
DOIs
StatePublished - Jan 29 2019

Keywords

  • BHD
  • Birt-Hogg-Dubé syndrome
  • FNIP1
  • Hsp90
  • O-GlcNAcylation
  • PP5
  • co-chaperone
  • folliculin-interacting protein 1
  • heat shock protein 90
  • serine/threonine protein phosphatase 5

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Fingerprint Dive into the research topics of 'Post-translational Regulation of FNIP1 Creates a Rheostat for the Molecular Chaperone Hsp90'. Together they form a unique fingerprint.

Cite this