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  Mechanism of polyubiquitination by human anaphase-promoting complex: RING repurposing for ubiquitin chain assembly.

Brown, N. G., Watson, E. R., Weissmann, F., Jarvis, M. A., VanderLinden, R., Grace, C., et al. (2014). Mechanism of polyubiquitination by human anaphase-promoting complex: RING repurposing for ubiquitin chain assembly. Molecular Cell, 56(2), 246-260. doi:10.1016/j.molcel.2014.09.009.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-4AB1-9 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-945A-A
Genre: Journal Article

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 Creators:
Brown, N. G., Author
Watson, E. R., Author
Weissmann, F., Author
Jarvis, M. A., Author
VanderLinden, R., Author
Grace, C.R.R., Author
Frye, J. J., Author
Qiao, R., Author
Dube, P.1, Author              
Petzold, G., Author
Cho, S. E., Author
Alsharif, O., Author
Bao, J., Author
Davidson, I.F., Author
Zheng, J. J., Author
Nourse, A., Author
Kurinov, I., Author
Peters, J. M., Author
Stark, H.1, Author              
Schulman, B. A., Author
Affiliations:
1Research Group of 3D Electron Cryo-Microscopy, MPI for biophysical chemistry, Max Planck Society, ou_578577              

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 Abstract: Polyubiquitination by E2 and E3 enzymes is a predominant mechanism regulating protein function. Some RINGE3s, including anaphase-promoting complex/cyclosome (APC), catalyze polyubiquitination by sequential reactions with two different E2s. An initiating E2 ligates ubiquitin to an E3-bound substrate. Another E2 grows a polyubiquitin chain on the ubiquitin-primed substrate through poorly defined mechanisms. Here we show that human APC's RING domain is repurposed for dual functions in polyubiquitination. The canonical RING surface activates an initiating E2-ubiquitin intermediate for substrate modification. However, APC engages and activates its specialized ubiquitin chain-elongating E2 UBE2S in ways that differ from current paradigms. During chain assembly, a distinct APC11 RING surface helps deliver a substrate-linked ubiquitin to accept another ubiquitin from UBE2S. Our data define mechanisms of APC/UBE2S-mediated polyubiquitination, reveal diverse functions of RING E3s and E2s, and provide a framework for understanding distinctive RING E3 features specifying ubiquitin chain elongation.

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Language(s): eng - English
 Dates: 2014-10-092014-10-23
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.molcel.2014.09.009
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Title: Molecular Cell
Source Genre: Journal
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Pages: - Volume / Issue: 56 (2) Sequence Number: - Start / End Page: 246 - 260 Identifier: -