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Components of the ubiquitin-proteasome pathway compete for surfaces on Rad23 family proteins |
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| Authors: | Amanda M Goh Kylie J Walters Suzanne Elsasser Rati Verma Raymond J Deshaies Daniel Finley Peter M Howley |
| Institution: | (1) Department of Pathology, Harvard Medical School, Boston, Massachusetts, USA;(2) Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota, USA;(3) Department of Cell Biology, Harvard Medical School, Boston, Massachusetts, USA;(4) Department of Biology, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, California, USA;(5) Institute of Molecular and Cell Biology, Singapore, Singapore |
| Abstract: | BackgroundThe delivery of ubiquitinated proteins to the proteasome for degradation is a key step in the regulation of the ubiquitin-proteasome pathway, yet the mechanisms underlying this step are not understood in detail. The Rad23 family of proteins is known to bind ubiquitinated proteins through its two ubiquitin-associated (UBA) domains, and may participate in the delivery of ubiquitinated proteins to the proteasome through docking via the Rad23 ubiquitin-like (UBL) domain. |
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