Nature Cell Biology 7, 742 - 749 (2005)
doi:10.1038/ncb0805-742
Delivery of ubiquitinated substrates to protein-unfolding machinesSuzanne Elsasser
& Daniel Finley
Suzanne Elsasser and Daniel Finley are in the Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA. Daniel_Finley@hms.harvard.edu
Recent work has shown that ubiquitination leads to recognition of target proteins by diverse ubiquitin receptors. One family of receptors delivers the ubiquitinated proteins to the proteasome resulting in ATP-dependent substrate unfolding and proteolysis. A related family of ubiquitin-binding proteins seems to recruit ubiquitinated proteins to Cdc48, an ATPase ring complex that can also unfold proteins. Some targets seem to dock at Cdc48 before the proteasome does, in an ordered pathway. The intimate interplay between the proteasome and Cdc48, mediated in part by loosely associated ubiquitin receptors, has important functions in cellular regulation.
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