Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7194
pubmed:dateCreated
2008-5-23
pubmed:databankReference
pubmed:abstractText
Targeted protein degradation is largely performed by the ubiquitin-proteasome pathway, in which substrate proteins are marked by covalently attached ubiquitin chains that mediate recognition by the proteasome. It is currently unclear how the proteasome recognizes its substrates, as the only established ubiquitin receptor intrinsic to the proteasome is Rpn10/S5a (ref. 1), which is not essential for ubiquitin-mediated protein degradation in budding yeast. In the accompanying manuscript we report that Rpn13 (refs 3-7), a component of the nine-subunit proteasome base, functions as a ubiquitin receptor, complementing its known role in docking de-ubiquitinating enzyme Uch37/UCHL5 (refs 4-6) to the proteasome. Here we merge crystallography and NMR data to describe the ubiquitin-binding mechanism of Rpn13. We determine the structure of Rpn13 alone and complexed with ubiquitin. The co-complex reveals a novel ubiquitin-binding mode in which loops rather than secondary structural elements are used to capture ubiquitin. Further support for the role of Rpn13 as a proteasomal ubiquitin receptor is demonstrated by its ability to bind ubiquitin and proteasome subunit Rpn2/S1 simultaneously. Finally, we provide a model structure of Rpn13 complexed to diubiquitin, which provides insights into how Rpn13 as a ubiquitin receptor is coupled to substrate deubiquitination by Uch37.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-11029046, http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-11283351, http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-12183636, http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-12353037, http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-12750381, http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-12787503, http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-12970172, http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-15493994, http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-15826667, http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-15837191, http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-16462746, http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-16499958, http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-16501559, http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-16815440, http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-16906146, http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-16990800, http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-17018280, http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-17057714, http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-17057716, http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-17139257, http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-17190603, http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-17304240, http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-18497808, http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-2538923, http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-8035826, http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-8125911, http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-9034192, http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-9353303, http://linkedlifedata.com/resource/pubmed/commentcorrection/18497827-9442033
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1476-4687
pubmed:author
pubmed:issnType
Electronic
pubmed:day
22
pubmed:volume
453
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
548-52
pubmed:dateRevised
2011-9-26
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction.
pubmed:affiliation
Center for Integrated Protein Science at the Department Chemie, Lehrstuhl für Biochemie, Technische Universität München, Lichtenbergstrasse 4, D-85747 Garching, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural