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  FAT10, a ubiquitin-independent signal for proteasomal degradation

Hipp, M. S., Kalveram, B., Raasi, S., Groettrup, M., & Schmidtke, G. (2005). FAT10, a ubiquitin-independent signal for proteasomal degradation. Mol Cell Biol, 25(9), 3483-91. doi:10.1128/MCB.25.9.3483-3491.2005.

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 Creators:
Hipp, M. S.1, Author              
Kalveram, B.2, Author
Raasi, S.2, Author
Groettrup, M.2, Author
Schmidtke, G.2, Author
Affiliations:
1Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              
2External Organizations, ou_persistent22              

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Free keywords: Animals Cell Line Green Fluorescent Proteins/genetics/metabolism Half-Life Humans Mice Mutation/genetics Proteasome Endopeptidase Complex/*physiology Recombinant Fusion Proteins/genetics/metabolism Transcription Factors/metabolism/physiology Transfection Ubiquitin/genetics/*metabolism Ubiquitins/genetics/*metabolism
 Abstract: FAT10 is a small ubiquitin-like modifier that is encoded in the major histocompatibility complex and is synergistically inducible by tumor necrosis factor alpha and gamma interferon. It is composed of two ubiquitin-like domains and possesses a free C-terminal diglycine motif that is required for the formation of FAT10 conjugates. Here we show that unconjugated FAT10 and a FAT10 conjugate were rapidly degraded by the proteasome at a similar rate. Fusion of FAT10 to the N terminus of very long-lived proteins enhanced their degradation rate as potently as fusion with ubiquitin did. FAT10-green fluorescent protein fusion proteins were not cleaved but entirely degraded, suggesting that FAT10-specific deconjugating enzymes were not present in the analyzed cell lines. Interestingly, the prevention of ubiquitylation of FAT10 by mutation of all lysines or by expression in ubiquitylation-deficient cells did not affect FAT10 degradation. Thus, conjugation with FAT10 is an alternative and ubiquitin-independent targeting mechanism for degradation by the proteasome, which, in contrast to polyubiquitylation, is cytokine inducible and irreversible.

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 Dates: 2005
 Publication Status: Published in print
 Pages: -
 Publishing info: -
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 Rev. Type: -
 Identifiers: Other: 15831455
DOI: 10.1128/MCB.25.9.3483-3491.2005
ISSN: 0270-7306 (Print) 0270-7306 (Linking)
URI: http://www.ncbi.nlm.nih.gov/pubmed/15831455
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Title: Mol Cell Biol
Source Genre: Journal
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Pages: - Volume / Issue: 25 (9) Sequence Number: - Start / End Page: 3483 - 91 Identifier: -