Ubiquitin ligase trapping identifies an SCF(Saf1) pathway targeting unprocessed vacuolar/lysosomal proteins.
Ubiquitin ligase trapping identifies an SCF(Saf1) pathway targeting unprocessed vacuolar/lysosomal proteins.
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DOI：
10.1016/j.molcel.2013.12.003
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发表时间：
2014-01-09
期刊：
影响因子：
16
通讯作者：
Toczyski, David P.
中科院分区：
文献类型：
--
作者：
Mark, Kevin G.;Simonetta, Marco;Maiolica, Alessio;Seller, Charles A.;Toczyski, David P.
We have developed a technique, called Ubiquitin Ligase Substrate Trapping, for the isolation of ubiquitinated substrates in complex with their ubiquitin ligase (E3). By fusing a ubiquitin associated (UBA) domain to an E3 ligase, we were able to selectively purify the polyubiquitinated forms of E3 substrates. Using Ligase Traps of eight different F-box proteins (SCF specificity factors) coupled with mass spectrometry, we identified known, as well as previously uncharacterized substrates. Polyubiquitinated forms of candidate substrates associated with their cognate F-box partner, but not other Ligase Traps. Interestingly, the four most abundant candidate substrates identified for the F-box protein Saf1 were all vacuolar/lysosomal proteins. Analysis of one of these substrates, Prb1, showed that Saf1 selectively promotes ubiquitination of the unprocessed form of the zymogen. This suggests that Saf1 is part of a pathway that targets protein precursors for proteasomal degradation.
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