|
rdf:type |
|
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lifeskim:mentions |
umls-concept:C0185023,
umls-concept:C0237497,
umls-concept:C0243125,
umls-concept:C0337112,
umls-concept:C0449255,
umls-concept:C0699900,
umls-concept:C1314972,
umls-concept:C1521828,
umls-concept:C1524075,
umls-concept:C1947904,
umls-concept:C1999228,
umls-concept:C2825781
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|
pubmed:issue |
6
|
|
pubmed:dateCreated |
2003-6-24
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|
pubmed:abstractText |
The ubiquitin-dependent targeting of proteins to the proteasome is an essential mechanism for regulating eukaryotic protein stability. Here we define the minimal signal for the degradation of the S phase CDK inhibitor Sic1. Of 20 lysines scattered throughout Sic1, 6 N-terminal lysines serve as major ubiquitination sites. Sic1 lacking these lysines (K0N) is stable in vivo, but readdition of any one restores turnover. Nevertheless, ubiquitin chains attached at different N-terminal lysines specify degradation in vitro at markedly different rates. Moreover, although K0N can be ubiquitinated by SCF(Cdc4)/Cdc34 in vitro in the absence (but not in the presence) of S-CDK, it is degraded slowly. Our results reveal that a single multiubiquitin chain can sustain a physiological turnover rate, but that chain position plays an unexpectedly significant role in the rate of proteasomal proteolysis.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
|
pubmed:status |
MEDLINE
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pubmed:month |
Jun
|
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pubmed:issn |
1097-2765
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|
pubmed:author |
|
|
pubmed:issnType |
Print
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1435-44
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
|
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pubmed:year |
2003
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pubmed:articleTitle |
Context of multiubiquitin chain attachment influences the rate of Sic1 degradation.
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|
pubmed:affiliation |
Howard Hughes Medical Institute, Division of Biology 156-29, California Institute of Technology, 1200 E. California Boulevard, Pasadena, CA 91125, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|
