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MAD2 associates with the cyclosome/anaphase-promoting complex and inhibits its activity.
Li, Y; Gorbea, C; Mahaffey, D; Rechsteiner, M; Benezra, R.
Afiliación
  • Li Y; Cell Biology Program, Memorial-Sloan Kettering Cancer Center, 1275 York Avenue, New York, NY 10021, USA.
Proc Natl Acad Sci U S A ; 94(23): 12431-6, 1997 Nov 11.
Article en En | MEDLINE | ID: mdl-9356466
Cell cycle progression is monitored by checkpoint mechanisms that ensure faithful duplication and accurate segregation of the genome. Defects in spindle assembly or spindle-kinetochore attachment activate the mitotic checkpoint. Once activated, this checkpoint arrests cells prior to the metaphase-anaphase transition with unsegregated chromosomes, stable cyclin B, and elevated M phase promoting factor activity. However, the mechanisms underlying this process remain obscure. Here we report that upon activation of the mitotic checkpoint, MAD2, an essential component of the mitotic checkpoint, associates with the cyclin B-ubiquitin ligase, known as the cyclosome or anaphase-promoting complex. Moreover, purified MAD2 causes a metaphase arrest in cycling Xenopus laevis egg extracts and prevents cyclin B proteolysis by blocking its ubiquitination, indicating that MAD2 functions as an inhibitor of the cyclosome. Thus, MAD2 links the mitotic checkpoint pathway to the cyclin B destruction machinery which is critical in controlling the metaphase-anaphase transition.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Unión al Calcio / Proteínas Fúngicas / Proteínas Portadoras / Complejos de Ubiquitina-Proteína Ligasa / Ligasas / Mitosis Tipo de estudio: Risk_factors_studies Límite: Animals / Humans Idioma: En Revista: Proc Natl Acad Sci U S A Año: 1997 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Unión al Calcio / Proteínas Fúngicas / Proteínas Portadoras / Complejos de Ubiquitina-Proteína Ligasa / Ligasas / Mitosis Tipo de estudio: Risk_factors_studies Límite: Animals / Humans Idioma: En Revista: Proc Natl Acad Sci U S A Año: 1997 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos