Abstract：
:Endoplasmic reticulum (ER)-associated protein degradation by the ubiquitin-proteasome system requires the dislocation of substrates from the ER into the cytosol. It has been speculated that a functional ubiquitin proteasome pathway is not only essential for proteolysis, but also for the preceding export step. Here, we show that short ubiquitin chains synthesized on proteolytic substrates are not sufficient to complete dislocation; the size of the chain seems to be a critical determinant. Moreover, our results suggest that the AAA proteins of the 26S proteasome are not directly involved in substrate export. Instead, a related AAA complex Cdc48, is required for ER-associated protein degradation upstream of the proteasome.
journal_name
Nat Cell Bioljournal_title
Nature cell biologyauthors
Jarosch E,Taxis C,Volkwein C,Bordallo J,Finley D,Wolf DH,Sommer Tdoi
10.1038/ncb746keywords:
subject
Has Abstractpub_date
2002-02-01 00:00:00pages
134-9issue
2eissn
1465-7392issn
1476-4679pii
ncb746journal_volume
4pub_type
杂志文章abstract：:Obesity occurs when excess energy accumulates in white adipose tissue (WAT), whereas brown adipose tissue (BAT), specialized for energy expenditure through thermogenesis, potently counteracts obesity. Factors that induce brown adipocyte commitment and energy expenditure would be a promising defence against adiposity. ...
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pub_type： 杂志文章
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更新日期：2009-04-01 00:00:00
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journal_title：Nature cell biology
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pub_type： 杂志文章
doi：10.1038/ncb848
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pub_type： 杂志文章
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更新日期：2014-03-01 00:00:00
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更新日期：2015-01-01 00:00:00
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