The Cdc48 unfoldase prepares well-folded protein substrates for degradation by the 26S proteasome View Full Text


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Article Info

DATE

2019-12

AUTHORS

Michal M. Olszewski, Cameron Williams, Ken C. Dong, Andreas Martin

ABSTRACT

Cdc48/p97 is an essential and highly conserved AAA+ ATPase that uses its protein-unfoldase activity to extract ubiquitinated polypeptides from macromolecular complexes and membranes. This motor has also been implicated in protein-degradation pathways, yet its exact role in acting upstream of the 26S proteasome remains elusive. Ubiquitinated proteins destined for degradation by the proteasome require an unstructured initiation region to engage with the proteasomal translocation machinery, and Cdc48 was proposed to generate these unfolded segments, yet direct evidence has been missing. Here, we used an in vitro reconstituted system to demonstrate the collaboration of Cdc48 and the 26S proteasome from S. cerevisiae in degrading ubiquitinated, well-folded proteins that lack unstructured segments. Our data indicate that a critical role for Cdc48 in the ubiquitin-proteasome system is to create flexible initiation regions in compact substrates that otherwise would be refractory to engagement and degradation by the proteasome. More... »

PAGES

29

References to SciGraph publications

  • 2013-10. Reconstitution of the 26S proteasome reveals functional asymmetries in its AAA+ unfoldase in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 2014-03. Structure of the Rpn11–Rpn8 dimer reveals mechanisms of substrate deubiquitination during proteasomal degradation in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 2002-09. A cryptic protease couples deubiquitination and degradation by the proteasome in NATURE
  • 2011-09. Rad23 escapes degradation because it lacks a proteasome initiation region in NATURE COMMUNICATIONS
  • 2015-09. Ubp6 deubiquitinase controls conformational dynamics and substrate degradation of the 26S proteasome in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 2018-12. Ub-ProT reveals global length and composition of protein ubiquitylation in cells in NATURE COMMUNICATIONS
  • 2012-07. Rational design of true monomeric and bright photoactivatable fluorescent proteins in NATURE METHODS
  • 2015-07. Cdc48-independent proteasomal degradation coincides with a reduced need for ubiquitylation in SCIENTIFIC REPORTS
  • 2011-03. Defining the geometry of the two-component proteasome degron in NATURE CHEMICAL BIOLOGY
  • 2013-07. Conformational switching of the 26S proteasome enables substrate degradation in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 2014-02. Single-molecule evaluation of fluorescent protein photoactivation efficiency using an in vivo nanotemplate in NATURE METHODS
  • 2009-11. Targeting proteins for degradation in NATURE CHEMICAL BIOLOGY
  • 2012-02. Complete subunit architecture of the proteasome regulatory particle in NATURE
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/s42003-019-0283-z

    DOI

    http://dx.doi.org/10.1038/s42003-019-0283-z

    DIMENSIONS

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    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/30675527


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