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Physical association of ubiquitin ligases and the 26S proteasome
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| Zeitschriftentitel: | Proceedings of the National Academy of Sciences |
|---|---|
| Personen und Körperschaften: | , |
| In: | Proceedings of the National Academy of Sciences, 97, 2000, 6, S. 2497-2502 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Proceedings of the National Academy of Sciences
|
| Schlagwörter: |
| author_facet |
Xie, Youming Varshavsky, Alexander Xie, Youming Varshavsky, Alexander |
|---|---|
| author |
Xie, Youming Varshavsky, Alexander |
| spellingShingle |
Xie, Youming Varshavsky, Alexander Proceedings of the National Academy of Sciences Physical association of ubiquitin ligases and the 26S proteasome Multidisciplinary |
| author_sort |
xie, youming |
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Xie, Youming Varshavsky, Alexander 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.060025497 <jats:p> The ubiquitin (Ub) system recognizes degradation signals of the target proteins through the E3 components of E3-E2 Ub ligases. A targeted substrate bears a covalently linked multi-Ub chain and is degraded by the ATP-dependent 26S proteasome, which consists of the 20S core protease and two 19S particles. The latter mediate the binding and unfolding of a substrate protein before its transfer to the interior of the 20S core. It is unclear how a targeted substrate is delivered to the 26S proteasome, inasmuch as Rpn10p, the only known proteasomal subunit that binds multi-Ub chains, has been found to be not essential for degradation of many proteins in the yeast <jats:italic>Saccharomyces cerevisiae</jats:italic> . Here we show that Ubr1p and Ufd4p, the E3 components of two distinct Ub ligases, directly interact with the 26S proteasome. Specifically, Ubr1p is shown to bind to the Rpn2p, Rpt1p, and Rpt6p proteins of the 19S particle, and Ufd4p is shown to bind to Rpt6p. These and related results suggest that a substrate-bound Ub ligase participates in the delivery of substrates to the proteasome, because of affinity between the ligase's E3 component and specific proteins of the 19S particle. </jats:p> Physical association of ubiquitin ligases and the 26S proteasome Proceedings of the National Academy of Sciences |
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| title |
Physical association of ubiquitin ligases and the 26S proteasome |
| title_unstemmed |
Physical association of ubiquitin ligases and the 26S proteasome |
| title_full |
Physical association of ubiquitin ligases and the 26S proteasome |
| title_fullStr |
Physical association of ubiquitin ligases and the 26S proteasome |
| title_full_unstemmed |
Physical association of ubiquitin ligases and the 26S proteasome |
| title_short |
Physical association of ubiquitin ligases and the 26S proteasome |
| title_sort |
physical association of ubiquitin ligases and the 26s proteasome |
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Multidisciplinary |
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http://dx.doi.org/10.1073/pnas.060025497 |
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2000 |
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2497-2502 |
| description |
<jats:p>
The ubiquitin (Ub) system recognizes degradation signals of the
target proteins through the E3 components of E3-E2 Ub ligases. A
targeted substrate bears a covalently linked multi-Ub chain and is
degraded by the ATP-dependent 26S proteasome, which consists of the 20S
core protease and two 19S particles. The latter mediate the binding and
unfolding of a substrate protein before its transfer to the interior of
the 20S core. It is unclear how a targeted substrate is delivered to
the 26S proteasome, inasmuch as Rpn10p, the only known proteasomal
subunit that binds multi-Ub chains, has been found to be not essential
for degradation of many proteins in the yeast
<jats:italic>Saccharomyces
cerevisiae</jats:italic>
. Here we show that Ubr1p and Ufd4p, the E3
components of two distinct Ub ligases, directly interact with the 26S
proteasome. Specifically, Ubr1p is shown to bind to the Rpn2p, Rpt1p,
and Rpt6p proteins of the 19S particle, and Ufd4p is shown to bind to
Rpt6p. These and related results suggest that a substrate-bound Ub
ligase participates in the delivery of substrates to the proteasome,
because of affinity between the ligase's E3 component and specific
proteins of the 19S particle.
</jats:p> |
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| description | <jats:p> The ubiquitin (Ub) system recognizes degradation signals of the target proteins through the E3 components of E3-E2 Ub ligases. A targeted substrate bears a covalently linked multi-Ub chain and is degraded by the ATP-dependent 26S proteasome, which consists of the 20S core protease and two 19S particles. The latter mediate the binding and unfolding of a substrate protein before its transfer to the interior of the 20S core. It is unclear how a targeted substrate is delivered to the 26S proteasome, inasmuch as Rpn10p, the only known proteasomal subunit that binds multi-Ub chains, has been found to be not essential for degradation of many proteins in the yeast <jats:italic>Saccharomyces cerevisiae</jats:italic> . Here we show that Ubr1p and Ufd4p, the E3 components of two distinct Ub ligases, directly interact with the 26S proteasome. Specifically, Ubr1p is shown to bind to the Rpn2p, Rpt1p, and Rpt6p proteins of the 19S particle, and Ufd4p is shown to bind to Rpt6p. These and related results suggest that a substrate-bound Ub ligase participates in the delivery of substrates to the proteasome, because of affinity between the ligase's E3 component and specific proteins of the 19S particle. </jats:p> |
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| spelling | Xie, Youming Varshavsky, Alexander 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.060025497 <jats:p> The ubiquitin (Ub) system recognizes degradation signals of the target proteins through the E3 components of E3-E2 Ub ligases. A targeted substrate bears a covalently linked multi-Ub chain and is degraded by the ATP-dependent 26S proteasome, which consists of the 20S core protease and two 19S particles. The latter mediate the binding and unfolding of a substrate protein before its transfer to the interior of the 20S core. It is unclear how a targeted substrate is delivered to the 26S proteasome, inasmuch as Rpn10p, the only known proteasomal subunit that binds multi-Ub chains, has been found to be not essential for degradation of many proteins in the yeast <jats:italic>Saccharomyces cerevisiae</jats:italic> . Here we show that Ubr1p and Ufd4p, the E3 components of two distinct Ub ligases, directly interact with the 26S proteasome. Specifically, Ubr1p is shown to bind to the Rpn2p, Rpt1p, and Rpt6p proteins of the 19S particle, and Ufd4p is shown to bind to Rpt6p. These and related results suggest that a substrate-bound Ub ligase participates in the delivery of substrates to the proteasome, because of affinity between the ligase's E3 component and specific proteins of the 19S particle. </jats:p> Physical association of ubiquitin ligases and the 26S proteasome Proceedings of the National Academy of Sciences |
| spellingShingle | Xie, Youming, Varshavsky, Alexander, Proceedings of the National Academy of Sciences, Physical association of ubiquitin ligases and the 26S proteasome, Multidisciplinary |
| title | Physical association of ubiquitin ligases and the 26S proteasome |
| title_full | Physical association of ubiquitin ligases and the 26S proteasome |
| title_fullStr | Physical association of ubiquitin ligases and the 26S proteasome |
| title_full_unstemmed | Physical association of ubiquitin ligases and the 26S proteasome |
| title_short | Physical association of ubiquitin ligases and the 26S proteasome |
| title_sort | physical association of ubiquitin ligases and the 26s proteasome |
| title_unstemmed | Physical association of ubiquitin ligases and the 26S proteasome |
| topic | Multidisciplinary |
| url | http://dx.doi.org/10.1073/pnas.060025497 |