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Related Experiment Videos

Structural insights into the p97-Ufd1-Npl4 complex.

Valerie E Pye1, Fabienne Beuron, Catherine A Keetch

  • 1Division of Molecular Biosciences, Faculty of Natural Sciences, Imperial College London, London SW7 2AZ, United Kingdom.

Proceedings of the National Academy of Sciences of the United States of America
|January 5, 2007
PubMed
Summary
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The Ufd1-Npl4 complex, a key partner of p97/VCP ATPase, has a distinct structure and interacts with p97 differently than p47. This structural difference explains their varied roles in cellular processes.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Cell Biology

Background:

  • p97/VCP (also known as Cdc48 in yeast) is a crucial AAA+ ATPase involved in numerous cellular functions.
  • It interacts with adaptor proteins like p47 and the Ufd1-Npl4 complex to mediate diverse pathways.
  • The Ufd1-Npl4 complex is essential for endoplasmic reticulum-associated degradation and mitotic spindle disassembly.

Purpose of the Study:

  • To elucidate the structural characteristics of the Ufd1-Npl4 complex.
  • To investigate the interaction between the Ufd1-Npl4 complex and p97.
  • To compare the structural and stoichiometric differences between p97-Ufd1-Npl4 and p97-p47 complexes.

Main Methods:

  • Electron microscopy (EM)
  • Biophysical techniques

Related Experiment Videos

Main Results:

  • The Ufd1-Npl4 heterodimer exhibits an elongated, bilobed structure (approx. 80 x 30 Å).
  • One Ufd1-Npl4 heterodimer binds to one p97 hexamer, forming the p97-Ufd1-Npl4 complex.
  • This complex forms via interaction at the N-D1 plane periphery of the p97 hexamer.

Conclusions:

  • The p97-Ufd1-Npl4 complex displays distinct stoichiometry, symmetry, and quaternary arrangement compared to the p97-p47 complex.
  • These structural differences underlie the specific cellular functions mediated by each p97-adaptor complex.
  • The findings provide insights into how p97 cooperates with different cofactors in various cellular pathways.