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  Dual RING E3 architectures regulate multiubiquitination and ubiquitin chain elongation by APC/C.

Brown, N. G., VanderLinden, R., Watson, E. R., Weissmann, F., Ordureau, A., Wu, K. P., et al. (2016). Dual RING E3 architectures regulate multiubiquitination and ubiquitin chain elongation by APC/C. Cell, 165(6), 1440-1453. doi:10.1016/j.cell.2016.05.037.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-E4AF-4 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-E4B6-3
Genre: Journal Article

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 Creators:
Brown, N. G., Author
VanderLinden, R., Author
Watson, E. R., Author
Weissmann, F., Author
Ordureau, A., Author
Wu, K. P., Author
Zhang, W., Author
Yu, S., Author
Mercredi, P. Y., Author
Harrison, J. S., Author
Davidson, I. F., Author
Qiao, R. P., Author
Lu, Y., Author
Dube, P.1, Author              
Brunner, M. R., Author
Grace, C. R. R., Author
Miller, D. J., Author
Haselbach, D.2, Author              
Jarvis, M. A., Author
Yamaguchi, M., Author
Yanishevski, D., AuthorPetzold, G., AuthorSidhu, S. S., AuthorKuhlman, B., AuthorKirschner, M. W., AuthorHarper, J. W., AuthorPeters, J. M., AuthorStark, H.3, Author              Schulman, B. A., Author more..
Affiliations:
1Research Group of 3D Electron Cryo-Microscopy, MPI for biophysical chemistry, Max Planck Society, ou_578577              
2Research Group of 3D Electron Cryo-Microscopy, MPI for Biophysical Chemistry, Max Planck Society, ou_578577              
3Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society, ou_2205645              

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 Abstract: Protein ubiquitination involves E1, E2, and E3 trienzyme cascades. E2 and RING E3 enzymes often collaborate to first prime a substrate with a single ubiquitin (UB) and then achieve different forms of polyubiquitination: multiubiquitination of several sites and elongation of linkage-specific UB chains. Here, cryo-EM and biochemistry show that the human E3 anaphase-promoting complex/cyclosome (APC/C) and its two partner E2s, UBE2C (aka UBCH10) and UBE2S, adopt specialized catalytic architectures for these two distinct forms of polyubiquitination. The APC/C RING constrains UBE2C proximal to a substrate and simultaneously binds a substrate-linked UB to drive processive multiubiquitination. Alternatively, during UB chain elongation, the RING does not bind UBE2S but rather lures an evolving substrate-linked UB to UBE2S positioned through a cullin interaction to generate a Lys11-linked chain. Our findings define mechanisms of APC/C regulation, and establish principles by which specialized E3-E2-substrate-UB architectures control different forms of polyubiquitination.

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Language(s): eng - English
 Dates: 2016-06-02
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.cell.2016.05.037
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Title: Cell
Source Genre: Journal
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Pages: - Volume / Issue: 165 (6) Sequence Number: - Start / End Page: 1440 - 1453 Identifier: -