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Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone.

The OLE pathway of yeast regulates the level of the ER-bound enzyme Delta9-fatty acid desaturase OLE1, thereby controlling membrane fluidity. A central component of this regulon is the transcription factor SPT23, a homolog of mammalian NF-kappaB. SPT23 is synthesized as an inactive, ER membrane-anchored precursor that is activated by regulated ubiquitin/proteasome-dependent processing (RUP). We now show that SPT23 dimerizes prior to processing and that the processed molecule, p90, retains its ubiquitin modification and initially remains tethered to its unprocessed, membrane-bound SPT23 partner. Subsequently, p90 is liberated from its partner for nuclear targeting by the activity of the chaperone-like CDC48(UFD1/NPL4) complex. Remarkably, this enzyme binds preferentially ubiquitinated substrates, suggesting that CDC48(UFD1/NPL4) is qualified to selectively remove ubiquitin conjugates from protein complexes.

Pubmed ID: 11733065

Authors

  • Rape M
  • Hoppe T
  • Gorr I
  • Kalocay M
  • Richly H
  • Jentsch S

Journal

Cell

Publication Data

November 30, 2001

Associated Grants

None

Mesh Terms

  • Active Transport, Cell Nucleus
  • Adenosine Triphosphatases
  • Cell Cycle Proteins
  • Cell Membrane
  • Dimerization
  • Fatty Acid Desaturases
  • Fungal Proteins
  • Genes, Reporter
  • Macromolecular Substances
  • Membrane Proteins
  • Models, Biological
  • Molecular Chaperones
  • Nuclear Pore Complex Proteins
  • Nuclear Proteins
  • Nucleocytoplasmic Transport Proteins
  • Protein Binding
  • Protein Precursors
  • Protein Processing, Post-Translational
  • Protein Structure, Tertiary
  • Proteins
  • Saccharomyces cerevisiae Proteins
  • Trans-Activators
  • Transcription Factors
  • Two-Hybrid System Techniques
  • Ubiquitin
  • Yeasts