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TitleCryo-EM of Mitotic Checkpoint Complex-Bound APC/C Reveals Reciprocal and Conformational Regulation of Ubiquitin Ligation.
Journal, issue, pagesMol Cell, Vol. 63, Issue 4, Page 593-607, Year 2016
Publish dateAug 18, 2016
AuthorsMasaya Yamaguchi / Ryan VanderLinden / Florian Weissmann / Renping Qiao / Prakash Dube / Nicholas G Brown / David Haselbach / Wei Zhang / Sachdev S Sidhu / Jan-Michael Peters / Holger Stark / Brenda A Schulman /
PubMed AbstractThe mitotic checkpoint complex (MCC) coordinates proper chromosome biorientation on the spindle with ubiquitination activities of CDC20-activated anaphase-promoting complex/cyclosome (APC/C(CDC20)). ...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.
External linksMol Cell / PubMed:27522463 / PubMed Central
MethodsEM (single particle)
Resolution4.8 - 18.0 Å
Structure data

4021

5khu

EMDB-4021: Human Anaphase-Promoting Complex/Cyclosome (APC/C) APC15 deletion mutant with Mitotic Checkpoint Complex (MCC) in a closed conformation.
PDB-5khu: Model of human Anaphase-promoting complex/Cyclosome (APC15 deletion mutant), in complex with the Mitotic checkpoint complex (APC/C-CDC20-MCC) based on cryo EM data at 4.8 Angstrom resolution
Method: EM (single particle) / Resolution: 4.8 Å

EMDB-4022:
Human Anaphase-Promoting Complex/Cyclosome (APC/C) APC15 deletion mutant with Mitotic Checkpoint Complex (MCC) in an open conformation.
Method: EM (single particle) / Resolution: 9.0 Å

EMDB-4023:
Human Anaphase-Promoting Complex/Cyclosome bound to Mitotic Checkpoint Complex (APC/C-MCC) in a closed conformation.
Method: EM (single particle) / Resolution: 9.0 Å

EMDB-4024:
Human Anaphase-promoting complex/Cyclosome bound to Mitotic Checkpoint Complex(APC/C-MCC) in an open conformation.
Method: EM (single particle) / Resolution: 10.0 Å

4025

5khr

EMDB-4025: Human Anaphase-promoting complex/Cyclosome (APC/C) APC15 deletion mutant bound to the E2 UBE2C (aka UBCH10) poised for ubiquitin ligation to substrate.
PDB-5khr: Model of human Anaphase-promoting complex/Cyclosome complex (APC15 deletion mutant) in complex with the E2 UBE2C/UBCH10 poised for ubiquitin ligation to substrate (APC/C-CDC20-substrate-UBE2C)
Method: EM (single particle) / Resolution: 6.1 Å

EMDB-4026:
Human Anaphase-Promoting Complex/Cyclosome (APC/C) APC15 deletion mutant bound to Mitotic Checkpoint Complex (MCC) and the E2 UBE2S poised for UB chain synthesis.
Method: EM (single particle) / Resolution: 5.7 Å

EMDB-4027:
Human Anaphase-Promoting Complex/Cyclosome bound to Mitotic Checkpoint Complex (APC/C-MCC) and the E2 UBE2C (aka UBCH10) poised for ubiquitination of MCC's CDC20
Method: EM (single particle) / Resolution: 17.0 Å

EMDB-4028:
Human Anaphase-Promoting Complex/Cyclosome (APC/C) APC15 deletion mutant bound to Mitotic Checkpoint Complex (MCC) and the E2 UBE2C (aka UBCH10) poised for ubiquitination of MCC's CDC20
Method: EM (single particle) / Resolution: 18.0 Å

Source
  • homo sapiens (human)
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsCELL CYCLE / ubiquitination / protein complex / mitosis / inhibition / conformational change

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