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  Determinants of conformational dimerization of Mad2 and its inhibition by p31comet

Mapelli, M., Filipp, F. V., Rancati, G., Massimiliano, L., Nezi, L., Stier, G., et al. (2006). Determinants of conformational dimerization of Mad2 and its inhibition by p31comet. EMBO Journal, 25(6), 1273-1284. doi:10.1038/sj.emboj.7601033.

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 Urheber:
Mapelli, M., Autor
Filipp, F. V., Autor
Rancati, G., Autor
Massimiliano, L., Autor
Nezi, L., Autor
Stier, Gunter1, Autor           
Hagan, R. S., Autor
Confalonieri, S., Autor
Piatti, S., Autor
Sattler, Michael, Autor
Musacchio, A., Autor
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Schlagwörter: Cdc20; centromere; kinetochore; mitosis; mitotic arrest deficient; spindle assembly checkpoint
 Zusammenfassung: The spindle assembly checkpoint (SAC) monitors chromosome attachment to spindle microtubules. SAC proteins operate at kinetochores, scaffolds mediating chromosome-microtubule attachment. The ubiquitous SAC constituents Mad1 and Mad2 are recruited to kinetochores in prometaphase. Mad2 sequesters Cdc20 to prevent its ability to mediate anaphase onset. Its function is counteracted by p31comet (formerly CMT2). Upon binding Cdc20, Mad2 changes its conformation from O-Mad2 (Open) to C-Mad2 (Closed). A Mad1-bound C-Mad2 template, to which O-Mad2 binds prior to being converted into Cdc20-bound C-Mad2, assists this process. A molecular understanding of this prion-like property of Mad2 is missing. We characterized the molecular determinants of the O-Mad2:C-Mad2 conformational dimer and derived a rationalization of the binding interface in terms of symmetric and asymmetric components. Mutation of individual interface residues abrogates the SAC in Saccharomyces cerevisiae. NMR chemical shift perturbations indicate that O-Mad2 undergoes a major conformational rearrangement upon binding C-Mad2, suggesting that dimerization facilitates the structural conversion of O-Mad2 required to bind Cdc20. We also show that the negative effects of p31comet on the SAC are based on its competition with O-Mad2 for C-Mad2 binding.

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Sprache(n): eng - English
 Datum: 2005-12-022006-02-092006-03-092006-03-22
 Publikationsstatus: Erschienen
 Seiten: 12
 Ort, Verlag, Ausgabe: -
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Titel: EMBO Journal
  Andere : EMBO J.
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Nature Publishing Group
Seiten: - Band / Heft: 25 (6) Artikelnummer: - Start- / Endseite: 1273 - 1284 Identifikator: ISSN: 0261-4189
CoNE: https://pure.mpg.de/cone/journals/resource/954925497061