Multiple intersecting pathways are involved in CPEB1 phosphorylation and regulation of translation during mouse oocyte meiosis.

Kunitomi, Chisato; Romero, Mayra; Daldello, Enrico Maria; Schindler, Karen; Conti, Marco

Kunitomi, Chisato; Romero, Mayra; Daldello, Enrico Maria; Schindler, Karen; Conti, Marco.

Afiliación

Kunitomi C; Center for Reproductive Sciences, University of California, San Francisco, CA 94143, USA.
Romero M; Eli and Edythe Broad Center of Regeneration Medicine and Stem Cell Research, University of California, San Francisco, CA 94143, USA.
Daldello EM; Department of Obstetrics and Gynecology and Reproductive Sciences, University of California, San Francisco, CA 94143, USA.
Schindler K; Rutgers, The State University of New Jersey, Piscataway, NJ 08854, USA.
Conti M; Human Genetics Institute of New Jersey, Piscataway, NJ 08854, USA.

Development ; 151(11)2024 Jun 01.

Article en En | MEDLINE | ID: mdl-38785133

ABSTRACT

ABSTRACT

The RNA-binding protein cytoplasmic polyadenylation element binding 1 (CPEB1) plays a fundamental role in regulating mRNA translation in oocytes. However, the specifics of how and which protein kinase cascades modulate CPEB1 activity are still controversial. Using genetic and pharmacological tools, and detailed time courses, we have re-evaluated the relationship between CPEB1 phosphorylation and translation activation during mouse oocyte maturation. We show that both the CDK1/MAPK and AURKA/PLK1 pathways converge on CPEB1 phosphorylation during prometaphase of meiosis I. Only inactivation of the CDK1/MAPK pathway disrupts translation, whereas inactivation of either pathway alone leads to CPEB1 stabilization. However, CPEB1 stabilization induced by inactivation of the AURKA/PLK1 pathway does not affect translation, indicating that destabilization and/or degradation is not linked to translational activation. The accumulation of endogenous CCNB1 protein closely recapitulates the translation data that use an exogenous template. These findings support the overarching hypothesis that the activation of translation during prometaphase in mouse oocytes relies on a CDK1/MAPK-dependent CPEB1 phosphorylation, and that translational activation precedes CPEB1 destabilization.

Asunto(s)

Meiosis; Oocitos; Biosíntesis de Proteínas; Factores de Transcripción; Factores de Escisión y Poliadenilación de ARNm; Animales; Femenino; Ratones; Aurora Quinasa A/metabolismo; Aurora Quinasa A/genética; Proteína Quinasa CDC2/metabolismo; Proteína Quinasa CDC2/genética; Proteínas de Ciclo Celular/metabolismo; Proteínas de Ciclo Celular/genética; Ciclina B1/metabolismo; Ciclina B1/genética; Factores de Escisión y Poliadenilación de ARNm/metabolismo; Factores de Escisión y Poliadenilación de ARNm/genética; Oocitos/metabolismo; Oocitos/citología; Fosforilación; Proteínas Serina-Treonina Quinasas/metabolismo; Proteínas Serina-Treonina Quinasas/genética; Proteínas Proto-Oncogénicas/metabolismo; Proteínas Proto-Oncogénicas/genética; Transducción de Señal; Factores de Transcripción/metabolismo; Factores de Transcripción/genética

Palabras clave

CPEB1; Meiosis; Oocyte; Translation; mRNA

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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Oocitos / Factores de Transcripción / Biosíntesis de Proteínas / Factores de Escisión y Poliadenilación de ARNm / Meiosis Límite: Animals Idioma: En Revista: Development Asunto de la revista: BIOLOGIA / EMBRIOLOGIA Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido

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