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  Cryo-EM of mitotic checkpoint complex-bound APC/C reveals reciprocal and conformational regulation of ubiquitin ligation.

Yamaguchi, M., VanderLinden, R., Weissmann, F., Qiao, R., Dube, P., Brown, N. G., et al. (2016). Cryo-EM of mitotic checkpoint complex-bound APC/C reveals reciprocal and conformational regulation of ubiquitin ligation. Molecular Cell, 63(4), 593-607. doi:10.1016/j.molcel.2016.07.003.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-42BE-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-2F26-8
Genre: Journal Article

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 Creators:
Yamaguchi, M., Author
VanderLinden, R., Author
Weissmann, F., Author
Qiao, R., Author
Dube, P.1, Author              
Brown, N. G., Author
Haselbach, D.1, Author              
Zhang, W., Author
Sidhu, S. S., Author
Peters, J. M., Author
Stark, H.1, Author              
Schulman, B. A., Author
Affiliations:
1Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society, ou_2205645              

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 Abstract: The mitotic checkpoint complex (MCC) coordinates proper chromosome biorientation on the spindle with ubiquitination activities of CDC20-activated anaphase-promoting complex/cyclosome (APC/C(CDC20)). APC/C(CDC20) and two E2s, UBE2C and UBE2S, catalyze ubiquitination through distinct architectures for linking ubiquitin (UB) to substrates and elongating polyUB chains, respectively. MCC, which contains a second molecule of CDC20, blocks APC/C(CDC20)-UBE2C-dependent ubiquitination of Securin and Cyclins, while differentially determining or inhibiting CDC20 ubiquitination to regulate spindle surveillance, checkpoint activation, and checkpoint termination. Here electron microscopy reveals conformational variation of APC/C(CDC20)-MCC underlying this multifaceted regulation. MCC binds APC/C-bound CDC20 to inhibit substrate access. However, rotation about the CDC20-MCC assembly and conformational variability of APC/C modulate UBE2C-catalyzed ubiquitination of MCC's CDC20 molecule. Access of UBE2C is limiting for subsequent polyubiquitination by UBE2S. We propose that conformational dynamics of APC/C(CDC20)-MCC modulate E2 activation and determine distinctive ubiquitination activities as part of a response mechanism ensuring accurate sister chromatid segregation.

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Language(s): eng - English
 Dates: 2016-08-102016-08-18
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.molcel.2016.07.003
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Title: Molecular Cell
Source Genre: Journal
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Pages: - Volume / Issue: 63 (4) Sequence Number: - Start / End Page: 593 - 607 Identifier: -