کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2050540 | 1074173 | 2009 | 4 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Degradation of FAT10 by the 26S proteasome is independent of ubiquitylation but relies on NUB1L
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Degradation of FAT10 by the 26S proteasome is independent of ubiquitylation but relies on NUB1L Degradation of FAT10 by the 26S proteasome is independent of ubiquitylation but relies on NUB1L](/preview/png/2050540.png)
چکیده انگلیسی
The ubiquitin-like modifier FAT10 targets proteins for degradation by the proteasome, a process accelerated by the UBL-UBA domain protein NEDD8 ultimate buster 1-long. Here, we show that FAT10-mediated degradation occurs independently of poly-ubiquitylation as purified 26S proteasome readily degraded FAT10-dihydrofolate reductase (DHFR) but not ubiquitin-DHFR in vitro. Interestingly, the 26S proteasome could only degrade FAT10-DHFR when NUB1L was present. Knock-down of NUB1L attenuated the degradation of FAT10-DHFR in intact cells suggesting that NUB1L determines the degradation rate of FAT10-linked proteins. In conclusion, our data establish FAT10 as a ubiquitin-independent but NUB1L-dependent targeting signal for proteasomal degradation.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 583, Issue 3, 4 February 2009, Pages 591–594
Journal: FEBS Letters - Volume 583, Issue 3, 4 February 2009, Pages 591–594
نویسندگان
Gunter Schmidtke, Birte Kalveram, Marcus Groettrup,