| Mad2 binding to Mad1 and Cdc20, rather than oligomerization, is required for the spindle checkpoint. | |
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MedLine Citation:
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PMID: 11707408 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Mad2 is a key component of the spindle checkpoint, a device that controls the fidelity of chromosome segregation in mitosis. The ability of Mad2 to form oligomers in vitro has been correlated with its ability to block the cell cycle upon injection into Xenopus embryos. Here we show that Mad2 forms incompatible complexes with Mad1 and Cdc20, neither of which requires Mad2 oligomerization. A monomeric point mutant of Mad2 can sustain a cell cycle arrest of comparable strength to that of the wild-type protein. We show that the interaction of Mad2 with Mad1 is crucial for the localization of Mad2 to kinetochores, where Mad2 interacts with Cdc20. We propose a model that features the kinetochore as a 'folding factory' for the formation of a Mad2-Cdc20 complex endowed with inhibitory activity on the anaphase promoting complex. |
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Authors:
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L Sironi; M Melixetian; M Faretta; E Prosperini; K Helin; A Musacchio |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: The EMBO journal Volume: 20 ISSN: 0261-4189 ISO Abbreviation: EMBO J. Publication Date: 2001 Nov |
Date Detail:
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Created Date: 2001-11-14 Completed Date: 2002-01-17 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 8208664 Medline TA: EMBO J Country: England |
Other Details:
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Languages: eng Pagination: 6371-82 Citation Subset: IM |
Affiliation:
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Department of Experimental Oncology, European Institute of Oncology, Via Ripamonti 435, 20141 Milan, Italy. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Anaphase Animals Antibodies, Monoclonal / metabolism Binding Sites Calcium-Binding Proteins / metabolism* Carrier Proteins* Cell Cycle Cell Cycle Proteins / metabolism* Chromatography, Gel DNA, Complementary / metabolism Electrophoresis, Polyacrylamide Gel Escherichia coli / metabolism Fungal Proteins / metabolism* Hela Cells Humans Kinetochores / metabolism Mice Microscopy, Fluorescence Mitosis Models, Biological Mutagenesis, Site-Directed Nuclear Proteins Peptides / chemistry Phosphoproteins / metabolism* Plasmids / metabolism Point Mutation Polymerase Chain Reaction Precipitin Tests Protein Binding Recombinant Proteins / metabolism Repressor Proteins / metabolism* Saccharomyces cerevisiae Proteins* Sodium Chloride / pharmacology Transfection Urea / pharmacology |
| Chemical | |
Reg. No./Substance:
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0/Antibodies, Monoclonal; 0/CDC20 protein, S cerevisiae; 0/Calcium-Binding Proteins; 0/Carrier Proteins; 0/Cell Cycle Proteins; 0/DNA, Complementary; 0/Fungal Proteins; 0/MAD1 protein, S cerevisiae; 0/MAD1L1 protein, human; 0/MAD2 protein, S cerevisiae; 0/Mad1l1 protein, mouse; 0/Mad2l1 protein, mouse; 0/Mad2l2 protein, mouse; 0/Nuclear Proteins; 0/Peptides; 0/Phosphoproteins; 0/Recombinant Proteins; 0/Repressor Proteins; 0/Saccharomyces cerevisiae Proteins; 57-13-6/Urea; 7647-14-5/Sodium Chloride |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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