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| Mol. Cell Feb (2007); 25(3):385-97 | |
| Cdc48p-Npl4p-Ufd1p- binds and segregates membrane-anchored-tethered complexes via a polyubiquitin signal present on the anchors- | |
| Shcherbik N, Haines DS | |
| Fels Institute for Cancer Research and Molecular Biology, Temple University School of Medicine, Philadelphia, PA 19140, USA- | |
| Abstract: Cdc48p is an abundant and conserved member of the AAA ATPase family of molecular chaperones- Cdc48p performs ubiquitin-selective functions, which are mediated by numerous ubiquitin binding adaptors, including the Npl4p-Ufd1p complex- Previous studies suggest that Cdc48p-containing complexes carry out many biochemical activities, including ubiquitination, deubiquitination, protein complex segregation, and targeting of ubiquitinated substrates to the proteasome- The molecular mechanisms by which Cdc48p-containing complexes participate in these processes remain poorly defined- We show here by using physiologically relevant Cdc48p substrates -i-e-, endoplasmic membrane-associated-tethered dimers of Mga2p and Spt23p- and in vitro systems with purified proteins that Cdc48p-Npl4p-Ufd1p- binds to and promotes segregation of the tethered proteins via a polyubiquitin signal present on the membrane-bound proteins- Mobilization does not involve retrotranslocation of the associated anchors- These results provide biochemical evidence that Cdc48p-Npl4p-Ufd1p- functions as a polyubiquitin-selective segregase and that a polyubiquitin-Cdc48p pathway modulates protein interactions at cell membranes- | |
| [PUBMED: 17289586] |   |
| Copyright © 2009, Tyers Lab, The Samuel Lunenfeld Research Institute, Mount Sinai Hospital, All Rights Reserved. |
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| BioGRID: A General Repository for Interaction Datasets. Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers. Nucleic Acids Res. Jan 1;34:D535-9. |